ATP-dependent DNA helicase important for chromosome transmission and normal cell cycle progression in G(2)/M (By similarity). May have a role in changing DNA topology to allow the loading of proteins involved in maintaining sister chromatid cohesion in the vicinity of the centromeres (By similarity). Has a specific role in chromosome segregation during meiosis II.
Belongs to the helicase family. RAD3/XPD subfamily.
Belongs to the nucleosome assembly protein (NAP) family.
Belongs to the universal ribosomal protein uL2 family.
Belongs to the phosphohexose mutase family.
Belongs to the anthrone oxygenase family.
Belongs to the universal ribosomal protein uL11 family.
Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family.
Belongs to the AB hydrolase superfamily. MetX family.
Expression is positively regulated by the secondary metabolism regulator LAE1 (PubMed:22713715).
Fusaric acid is phytotoxic to plants such as cotton and banana (PubMed:20955724, PubMed:23922960). It has been shown to induce programmed cell death in plants (PubMed:16868776, PubMed:23838885). In addition to a mild toxicity to animals, fusaric acid exhibits acanthamoebicidal, antioomycete, and antimycobacterial activities (PubMed:17927749, PubMed:22864988, PubMed:21811925).
Homoserine O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties (PubMed:22652150, PubMed:25372119). L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L-homoserine by cluster enzymes aspartate kinase FUB3 and homoserine O-acetyltransferase FUB5, as well as enzymes of the primary metabolism (By similarity). The polyketide synthase (PKS) FUB1 generates the triketide trans-2-hexenal which is presumptively released by the hydrolase FUB4 and linked to the NRPS-bound amino acid precursor by NAD(P)-dependent dehydrogenase FUB6 (By similarity). FUB1, FUB4, and the non-canonical NRPS Fub8 may form an enzyme complex (By similarity). Further processing of the NRPS-bound intermediate might be carried out by FUB6 and the sulfhydrylase FUB7, enabling a spontaneous electrocyclization to close the carbon backbone of fusaric acid (By similarity). Dihydrofusaric acid is likely to be released via reduction by the thioester reductase (TR) domain of FUB8 whereupon the final oxidation to fusaric acid may (also) be performed by the FMN-dependent dehydrogenase FUB9 (By similarity).
Belongs to the SMC family. SMC3 subfamily.
The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity.
Component of the oligosaccharyltransferase (OST) complex.
Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Component of the NOP7 complex, composed of ERB1, NOP7 and YTM1. Within the NOP7 complex ERB1 appears to interact directly with NOP7 and YTM1. The NOP7 complex also associates with the 66S pre-ribosome.
Component of the NOP7 complex, which is required for maturation of the 25S and 5.8S ribosomal RNAs and formation of the 60S ribosome.
Belongs to the cerato-ulmin hydrophobin family.
Belongs to the cyclophilin-type PPIase family.
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Belongs to the eukaryotic RPC34/RPC39 RNA polymerase subunit family.
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs.
Belongs to the aldehyde dehydrogenase family.
Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1), a complex that is involved in endosomal cargo sorting.
Component of the ESCRT-0 complex composed of HSE1 and VPS27.
Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB).
The SPT4-SPT5 complex mediates both activation and inhibition of transcription elongation, and plays a role in pre-mRNA processing. This complex seems to be important for the stability of the RNA polymerase II elongation machinery on the chromatin template but not for the inherent ability of this machinery to translocate down the gene.
Belongs to the PheA/TfdB FAD monooxygenase family.
Belongs to the paxM FAD-dependent monooxygenase family.
Belongs to the universal ribosomal protein uS5 family.
Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration.
Belongs to the adaptor complexes large subunit family.
Belongs to the eukaryotic ribosomal protein eS25 family.
Belongs to the zinc-containing alcohol dehydrogenase family.
Belongs to the ubiquitin-conjugating enzyme family.
Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.
Belongs to the adaptor complexes medium subunit family.
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19) family.
Belongs to the RNA polymerase beta' chain family.
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Belongs to the eukaryotic ribosomal protein eL43 family.
Belongs to the amino acid/polyamine transporter 2 family.
Belongs to the GMC oxidoreductase family.
Belongs to the PIGG/PIGN/PIGO family. PIGN subfamily.
Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor.
Belongs to the oligopeptide OPT transporter family.
Required for exosome-dependent processing of pre-rRNA and small nucleolar RNA (snRNA) precursors. Involved in processing of 35S pre-rRNA at the A0, A1 and A2 sites.
Belongs to the protein kinase superfamily.
Belongs to the WD repeat coronin family.
Belongs to the sphingosine N-acyltransferase family.
Belongs to the ABC transporter superfamily. ABCG family. PDR (TC 3.A.1.205) subfamily.
Belongs to the DPH1/DPH2 family. DPH1 subfamily.
Belongs to the alpha-IPM synthase/homocitrate synthase family.
Belongs to the SMC family. RAD50 subfamily.
Belongs to the glycosyltransferase 32 family.
Involved in nucleolar integrity and required for processing of the pre-rRNA for the 60S ribosome subunit.
Belongs to the succinate/malate CoA ligase alpha subunit family.
Heterodimer of an alpha and a beta subunit.
Lacks conserved residue(s) required for the propagation of feature annotation.
Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit.
Belongs to the trichodiene synthase family.
Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CHEK2 subfamily.
Aspartate kinase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties (PubMed:22652150, PubMed:25372119). L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L-homoserine by cluster enzymes aspartate kinase FUB3 and homoserine O-acetyltransferase FUB5, as well as enzymes of the primary metabolism (By similarity). The polyketide synthase (PKS) FUB1 generates the triketide trans-2-hexenal which is presumptively released by the hydrolase FUB4 and linked to the NRPS-bound amino acid precursor by NAD(P)-dependent dehydrogenase FUB6 (By similarity). FUB1, FUB4, and the non-canonical NRPS Fub8 may form an enzyme complex (By similarity). Further processing of the NRPS-bound intermediate might be carried out by FUB6 and the sulfhydrylase FUB7, enabling a spontaneous electrocyclization to close the carbon backbone of fusaric acid (By similarity). Dihydrofusaric acid is likely to be released via reduction by the thioester reductase (TR) domain of FUB8 whereupon the final oxidation to fusaric acid may (also) be performed by the FMN-dependent dehydrogenase FUB9 (By similarity).
Expression is positively regulated by the fusaric acid cluster specific transcription factor FUB10 (PubMed:25372119). Expression is also positively regulated by the secondary metabolism regulator LAE1 (PubMed:22713715).
Strongly reduces production of fusaric acid (PubMed:25372119).
Belongs to the methylenetetrahydrofolate reductase family.
Belongs to the pterin-4-alpha-carbinolamine dehydratase family.
Belongs to the TrkH potassium transport family.
Belongs to the metallo-dependent hydrolases superfamily. ATZ/TRZ family.
Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia.
Belongs to the peroxidase family. Cytochrome c peroxidase subfamily.
Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity.
Belongs to the ATP-dependent AMP-binding enzyme family.
Belongs to the glycosyl hydrolase 28 family.
eIF-5A seems to be the only eukaryotic protein to have a hypusine residue which is a post-translational modification of a lysine by the addition of a butylamino group.
Belongs to the ketopantoate reductase family.
Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.
Belongs to the protein kinase superfamily. BUD32 family.
Component of the EKC/KEOPS complex composed of at least BUD32, CGI121, GON7, KAE1 and PCC1; the whole complex dimerizes.
Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Belongs to the mitochondrial carrier (TC 2.A.29) family.
In the central section; belongs to the metallo-dependent hydrolases superfamily. DHOase family. CAD subfamily.
Belongs to the beta-class carbonic anhydrase family.
Belongs to the short-chain dehydrogenases/reductases (SDR) family.
Belongs to the acetyltransferase family. GNA1 subfamily.
Belongs to the mitochondrion-specific ribosomal protein mL54 family.
In the C-terminal section; belongs to the TrpB family.
In the N-terminal section; belongs to the TrpA family.
Belongs to the AB hydrolase superfamily. Lipase family.
Belongs to the acetyltransferase family.
N-acetylglutamate synthase involved in arginine biosynthesis.
Belongs to the glycosyltransferase 28 family.
Belongs to the glucose-6-phosphate 1-epimerase family.
Catalyzes the interconversion between the alpha and beta anomers from at least three hexose 6-phosphate sugars (Glc6P, Gal6P, and Man6P).
Belongs to the type-B carboxylesterase/lipase family.
Belongs to the glycosyl hydrolase 31 family.
Belongs to the universal ribosomal protein uS2 family.
Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.
Belongs to the thiolase-like superfamily. Thiolase family.
Belongs to the DNA polymerase delta/II small subunit family.
Belongs to the glycosyltransferase 2 family.
Component of the dolichol-phosphate mannose (DPM) synthase complex.
Transfers mannose from GDP-mannose to dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl donor in pathways leading to N-glycosylation, glycosyl phosphatidylinositol membrane anchoring, and O-mannosylation of proteins.
Converts proline to delta-1-pyrroline-5-carboxylate.
Belongs to the cysteine dioxygenase family.
Belongs to the oxygen-dependent FAD-linked oxidoreductase family.
Belongs to the peroxisomal membrane protein PXMP2/4 family.
Belongs to the protein kinase superfamily. RIO-type Ser/Thr kinase family.
The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits.
Involved in the retrieval of endoplasmic reticulum membrane proteins from the early Golgi compartment.
Belongs to the glycosyltransferase 22 family.
Belongs to the archaeal rpoM/eukaryotic RPA12/RPB9/RPC11 RNA polymerase family.
Microtubule binding protein that promotes the stabilization of dynamic microtubules. Required for mitotic spindle formation.
Required for 60S pre-ribosomal subunits export to the cytoplasm.
Involved in cytoplasm to vacuole transport (Cvt) and autophagic vesicle formation.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA methyltransferase RlmE family.
Belongs to the aspartate/ornithine carbamoyltransferase superfamily.
Belongs to the GPI inositol-deacylase family.
Involved in inositol deacylation of GPI-anchored proteins which plays important roles in the quality control and ER-associated degradation of GPI-anchored proteins.
Belongs to the nucleobase:cation symporter-2 (NCS2) (TC 2.A.40) family. Azg-like subfamily.
Belongs to the DNA mismatch repair MutS family. MSH3 subfamily.
Component of the post-replicative DNA mismatch repair system (MMR).
Belongs to the alkaline ceramidase family.
Belongs to the acyl carrier protein (ACP) family.
Carrier of the growing fatty acid chain in fatty acid biosynthesis.
Belongs to the flavin monoamine oxidase family.
Belongs to the XPG/RAD2 endonuclease family.
Belongs to the Mrp/NBP35 ATP-binding proteins family.
Global transcriptional regulator of transcription that impacts, but is not absolutely required for secondary metabolism and pathogenicity on maize. Regulates synthesis of multiple secondary metabolites, including fumonisins and fusarins.
Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair.
Belongs to the tRNA-intron endonuclease family.
Constitutes one of the two catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3'-cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body.
Belongs to the iron/ascorbate-dependent oxidoreductase family.
Belongs to the Mediator complex subunit 12 family.
Component of the SRB8-11 complex, which itself associates with the Mediator complex.
Component of the SRB8-11 complex. The SRB8-11 complex is a regulatory module of the Mediator complex which is itself involved in regulation of basal and activated RNA polymerase II-dependent transcription. The SRB8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by Mediator. It may inhibit the association of the Mediator complex with RNA polymerase II to form the holoenzyme complex.
Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family.
Belongs to the eukaryotic GSH synthase family.
Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)-oxygenase family.
Belongs to the universal ribosomal protein uS15 family.
Belongs to the 3-oxoacid CoA-transferase family.
Key enzyme for ketone body catabolism. Transfers the CoA moiety from succinate to acetoacetate. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate.
Belongs to the eukaryotic RPB7/RPC8 RNA polymerase subunit family.
Belongs to the GTP-binding elongation factor family. EF-G/EF-2 subfamily.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
Belongs to the G-alpha family. G(q) subfamily.
G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site.
Belongs to the glycosyl hydrolase 47 family.
Adds a GMP to the 5'-end of tRNA(His) after transcription and RNase P cleavage.
Belongs to the tRNA(His) guanylyltransferase family.
Plays a role in vesicular protein sorting.
Belongs to the isocitrate and isopropylmalate dehydrogenases family.
Belongs to the glycosyl hydrolase 43 family.
Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.
Belongs to the universal ribosomal protein uS12 family.
Component of the ribosomal small subunit (SSU) processome.
Involved in nucleolar processing of pre-18S ribosomal RNA. Involved in ribosome biosynthesis.
Belongs to the class-I aminoacyl-tRNA synthetase family.
Belongs to the ribose-phosphate pyrophosphokinase family.
Belongs to the glycosyl hydrolase 18 family. Chitinase class V subfamily.
Belongs to the glycosyl hydrolase 45 (cellulase K) family.
Belongs to the universal ribosomal protein uS14 family.
Vacuolar effluxer which mediate the efflux of amino acids resulting from autophagic degradation. The release of autophagic amino acids allows the maintenance of protein synthesis and viability during nitrogen starvation.
Belongs to the purine-cytosine permease (2.A.39) family.
Highly specific phosphatase involved in the metabolism of ADP-ribose 1''-phosphate (Appr1p) which is produced as a consequence of tRNA splicing.
Belongs to the archaeal Rpo5/eukaryotic RPB5 RNA polymerase subunit family.
Belongs to the gamma-glutamylcyclotransferase family.
Belongs to the glycosyl hydrolase 3 family.
Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER).
Belongs to the CoA-transferase III family.
Belongs to the acetolactate synthase small subunit family.
Belongs to the histidine acid phosphatase family. VIP1 subfamily.
Bifunctional inositol kinase that acts in concert with the IP6K kinases to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-InsP4, also respectively called InsP7 and InsP8, may regulate a variety of cellular processes, including apoptosis, vesicle trafficking, cytoskeletal dynamics, and exocytosis. Phosphorylates inositol hexakisphosphate (InsP6).
Belongs to the pantothenate synthetase family.
Belongs to the protein prenyltransferase subunit beta family.
Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins. The beta subunit is responsible for peptide-binding.
Belongs to the glycosyl hydrolase 5 (cellulase A) family.
Belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.
Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II.
Belongs to the ZIP transporter (TC 2.A.5) family.
Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
Maintains high levels of reduced glutathione in the cytosol.
Belongs to the diaminopimelate epimerase family.
Component of a fungal signal recognition particle (SRP) complex that consists of a 7SL RNA molecule (scR1) and at least six protein subunits: SRP72, SRP68, SRP54, SEC65, SRP21 and SRP14.
Plays a role in maintenance of chromatin structure during RNA polymerase II transcription elongation thereby repressing transcription initiation from cryptic promoters. Mediates the reassembly of nucleosomes onto the promoters of at least a selected set of genes during repression; the nucleosome reassembly is essential for transcriptional repression.
Belongs to the carbon-nitrogen hydrolase superfamily. Nitrilase family.
Belongs to the universal ribosomal protein uL15 family.
Belongs to the inositol monophosphatase superfamily.
Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP.
Single-stranded DNA-dependent ATP-dependent helicase. Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Required also for telomere recombination to repair telomeric ends in the absence of telomerase. KU70, of the KU70/KU80 heterodimer, binds to the stem loop of TLC1, the RNA component of telomerase. Involved in telomere maintenance. Interacts with telomeric repeats and subtelomeric sequences thereby controlling telomere length and protecting against subtelomeric rearrangement. Maintains telomeric chromatin, which is involved in silencing the expression of genes located at the telomere. Required for mating-type switching.
Belongs to the CSN7/EIF3M family. CSN7 subfamily.
Belongs to the metallo-dependent hydrolases superfamily. Peptidase M19 family.
Belongs to the class I-like SAM-binding methyltransferase superfamily. METTL21 family. EFM6 subfamily.
S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that methylates elongation factor 1-alpha.
Involved in nucleolar processing of pre-18S ribosomal RNA. Has a role in the nuclear export of 40S pre-ribosomal subunit to the cytoplasm.
Belongs to the methyltransferase superfamily. LCMT family.
Probable S-adenosyl-L-methionine-dependent methyltransferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. May methylate the carboxyl group of leucine residues to form alpha-leucine ester residues.
Belongs to the glycosyltransferase 15 family.
Secreted metalloproteinase that allows assimilation of proteinaceous substrates.
Belongs to the cytochrome c oxidase subunit 5A family.
Component of the cytochrome c oxidase (complex IV, CIV), a multisubunit enzyme composed of a catalytic core of 3 subunits and several supernumerary subunits.
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Belongs to the pyrroline-5-carboxylate reductase family.
Belongs to the glycosyl hydrolase 10 (cellulase F) family.
The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.
Belongs to the Mediator complex subunit 13 family.
Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Septin GTPase family.
Belongs to the ABC transporter superfamily. ABCF family. EF3 subfamily.
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Belongs to the complex I NDUFA12 subunit family.
Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.
Belongs to the metallo-dependent hydrolases superfamily. DHOase family. Class II DHOase subfamily.
Contains three distinct domains: an adenylation (A) domain that activates the substrate amino acid which is subsequently covalently linked as a thioester (aminoacyl-S-PCP) to the 4'-phosphopantetheine prosthetic group of the second domain, the peptidyl carrier protein (PCP) domain, as well as a thioester reductase (TR) release domain.
Non-canonical non-ribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties (PubMed:25372119). L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L-homoserine by cluster enzymes aspartate kinase FUB3 and homoserine O-acetyltransferase FUB5, as well as enzymes of the primary metabolism (By similarity). The polyketide synthase (PKS) FUB1 generates the triketide trans-2-hexenal which is presumptively released by the hydrolase FUB4 and linked to the NRPS-bound amino acid precursor by NAD(P)-dependent dehydrogenase FUB6 (By similarity). FUB1, FUB4, and the non-canonical NRPS Fub8 may form an enzyme complex (By similarity). Further processing of the NRPS-bound intermediate might be carried out by FUB6 and the sulfhydrylase FUB7, enabling a spontaneous electrocyclization to close the carbon backbone of fusaric acid (By similarity). Dihydrofusaric acid is likely to be released via reduction by the thioester reductase (TR) domain of FUB8 whereupon the final oxidation to fusaric acid may (also) be performed by the FMN-dependent dehydrogenase FUB9 (By similarity).
Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells.
Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Decreases, but does not eliminate the ability to metabolize 2-benzoxasolinone (BOA).
Expression is induced in response to 2-benzoxasolinone (BOA) exposure.
Fusarium verticillioides possesses 2 unlinked loci, FDB1 and FDB2, necessary for detoxification of antimicrobial compounds produced by maize, including 2-benzoxazolinone (BOA) (Probable). The FDB2 cluster arose as a duplication of the FDB1 cluster with rearrangement and expansion by incorporating additional genes (Probable).
Transcription factor; part of the Fusarium detoxification of benzoxazolinone cluster 2 (FDB2) involved in the degradation of benzoxazolinones produced by the host plant (PubMed:19302487, PubMed:26808652). Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their inherent instability once released, spontaneously degrade to the more stable corresponding benzoxazolinones, 6-methoxy-2-benzoxazolinone (MBOA) and 2-benzoxazolinone (BOA), respectively (PubMed:11876429). FDB3 is not essentiel, but contributes to efficient BOA biotransformation (PubMed:19302487).
Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules.
Belongs to the proteasome subunit S11 family.
Belongs to the casein kinase 2 subunit beta family.
Regulatory subunit of casein kinase II/CK2 (By similarity). As part of the kinase complex regulates the basal catalytic activity of the alpha subunit a constitutively active serine/threonine-protein kinase that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine.
Regulatory subunit of casein kinase II/CK2. As part of the kinase complex regulates the basal catalytic activity of the alpha subunit a constitutively active serine/threonine-protein kinase that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine.
Tetramer of two alpha and two beta subunits.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA methyltransferase RlmE family. SPB1 subfamily.
Component of the nucleolar and nucleoplasmic pre-60S ribosomal particle.
Required for proper assembly of pre-ribosomal particles during the biogenesis of the 60S ribosomal subunit.
Required for the function of coenzyme Q in the respiratory chain. May serve as a chaperone or may be involved in the transport of Q6 from its site of synthesis to the catalytic sites of the respiratory complexes.
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex.
Belongs to the prokaryotic/mitochondrial release factor family.
Involved in the proteasome-dependent degradation of fructose-1,6-bisphosphatase.
Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family.
Belongs to the AAA ATPase family. BCS1 subfamily.
Catalyzes the condensation of formaldehyde and glutathione to S-hydroxymethylglutathione.
Belongs to the shaker potassium channel beta subunit family.
Belongs to the WD repeat PRL1/PRL2 family.
Involved in pre-mRNA splicing and required for cell cycle progression at G2/M.
Belongs to the universal ribosomal protein uL30 family.
Belongs to the Mediator complex subunit 18 family.
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Aldo-keto reductase; part of the Fusarium detoxification of benzoxazolinone cluster 2 (FDB2) involved in the degradation of benzoxazolinones produced by the host plant (PubMed:19302487, PubMed:26808652). Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their inherent instability once released, spontaneously degrade to the more stable corresponding benzoxazolinones, 6-methoxy-2-benzoxazolinone (MBOA) and 2-benzoxazolinone (BOA), respectively (PubMed:11876429). The first step in the detoxification of benzoxazolinones involves the hydrolysis of the cyclic ester bond of benzoxazolinones by the FDB1 cluster gamma-lactamase MBL1 to aminophenols (PubMed:26808652, PubMed:12788712). MBL1 is able to convert BOA into 2-aminophenol (2-AP), as well as MBOA into 5-methoxy-2-aminophenol (2-AMP) (PubMed:26808652, PubMed:12788712). The FDB2 cluster N-malonyltransferase FDB2/NAT1 then metabolizes aminophenols via N-malonylation to non-toxic malonamic acids (PubMed:19302487, PubMed:12788712). FDB2/NAT1 converts 2-AP into N-(2-hydroxyphenyl) malonamic acid (HPMA) and 2-AMP into N-(2-hydroxy-4-methoxyphenyl) malonamic acid (HMPMA) (PubMed:19302487, PubMed:12788712). The duplicated dienlactone hydrolases DLH1 and DLH2 may provide redundant function for hydrolyzing the lactone moiety in the BOA molecule (Probable). The roles of the amidases an other enzymes encoded by the 2 FDB clusters have not been identified so far (Probable).
Belongs to the aldo/keto reductase family. Aldo/keto reductase 2 subfamily.
Does not affect tolerance to 2-benzoxazolinone (BOA).
Belongs to the 6-phosphogluconate dehydrogenase family.
Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH.
Belongs to the major facilitator superfamily. Nitrate/nitrite porter (TC 2.A.1.8) family.
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Belongs to the iron-containing alcohol dehydrogenase family.
Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.
Belongs to the Mediator complex subunit 5 family.
Belongs to the tyrosyl-DNA phosphodiesterase family.
Cleaves proteins, imported into the mitochondrion, to their mature size. While most mitochondrial precursor proteins are processed to the mature form in one step by mitochondrial processing peptidase (MPP), the sequential cleavage by MIP of an octapeptide after initial processing by MPP is a required step for a subgroup of nuclear-encoded precursor proteins destined for the matrix or the inner membrane.
Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Belongs to the protein-tyrosine phosphatase family.
Belongs to the xanthine dehydrogenase family.
Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
SNARE required for protein transport between the ER and the Golgi complex.
Belongs to the four-carbon acid sugar kinase family.
Activated by a monovalent cation that binds near, but not in, the active site. The most likely occupant of the site in vivo is potassium. Ion binding induces a conformational change that may alter substrate affinity.
Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily.
Belongs to the carbohydrate kinase pfkB family.
Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway.
Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate.
Involved in the secretory pathway as part of the exocyst complex which tethers secretory vesicles to the sites of exocytosis. Also plays a role in the assembly of the exocyst.
ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon.
Belongs to the DEAD box helicase family. eIF4A subfamily.
Component of the eIF4F complex, which composition varies with external and internal environmental conditions. It is composed of at least eIF4A, eIF4E and eIF4G.
Belongs to the actin-binding proteins ADF family.
Belongs to the glycosyl hydrolase 61 family.
Belongs to the eukaryotic ribosomal protein eS21 family.
Component of the small ribosomal subunit.
Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Has a physiological role leading to 18S rRNA stability.
Required for respiratory activity and maintenance and expression of the mitochondrial genome.
Functions in the early steps of protein synthesis of a small number of specific mRNAs. Acts by directing the binding of methionyl-tRNAi to 40S ribosomal subunits. In contrast to the eIF-2 complex, it binds methionyl-tRNAi to 40S subunits in a codon-dependent manner, whereas the eIF-2 complex binds methionyl-tRNAi to 40S subunits in a GTP-dependent manner.
Belongs to the chorismate synthase family.
Interacts with the 40S ribosomal subunit.
The SUI1 domain may be involved in RNA binding.
Belongs to the glycosyltransferase 39 family.
Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.
Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides.
Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family.
Mediator of diverse signals that repress RNA polymerase III transcription. Inhibits the de novo assembly of TFIIIB onto DNA.
Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Belongs to the universal ribosomal protein uS8 family.
Belongs to the glycosyl hydrolase 15 family.
Heterodimer with ALG13 to form a functional enzyme.
Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Anchors the catalytic subunit ALG13 to the ER.
Belongs to the Mediator complex subunit 8 family.
Belongs to the triosephosphate isomerase family.
Belongs to the Mediator complex subunit 19 family.
Mitochondrial mRNA stabilization factor.
Probable mitochondrial mRNA stabilization factor.
Belongs to the archaeal Rpo6/eukaryotic RPB6 RNA polymerase subunit family.
Belongs to the DNA polymerase type-B-like family.
Belongs to the kynurenine formamidase family.
Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation. Kynurenine may be further oxidized to nicotinic acid, NAD(H) and NADP(H). Required for elimination of toxic metabolites.
The main chain amide nitrogen atoms of the second glycine and its adjacent residue in the HGGXW motif define the oxyanion hole, and stabilize the oxyanion that forms during the nucleophilic attack by the catalytic serine during substrate cleavage.
Belongs to the small heat shock protein (HSP20) family.
Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.
Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+).
Pyrophosphatase that hydrolyzes non-canonical purine nucleotides such as inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) or xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions.
Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.
Irreversibly catalyzes the reduction of fumarate to succinate.
Involved in the early part of the secretory pathway.
Belongs to the glycosyl hydrolase 39 family.
Belongs to the FPP/GGPP synthase family.
Negative regulator of transcription elongation.
Belongs to the universal ribosomal protein uL5 family.
Belongs to the cytochrome c oxidase subunit 6B family.
Belongs to the replication factor A protein 3 family.
Component of the cleavage factor IA (CFIA) complex, which is involved in the endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation.
Belongs to the putative lipase ROG1 family.
Belongs to the helicase family. UvrD subfamily.
Golgi membrane protein involved in vesicular trafficking.
Belongs to the GTP-binding SRP family. SRP54 subfamily.
Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER). Binds to the signal sequence of presecretory proteins when they emerge from the ribosomes.
Has a two domain structure: the G-domain binds GTP; the M-domain binds the 7S RNA in presence of SRP19 and also binds the signal sequence.
Signal recognition particle consists of a 7S RNA molecule and at least six protein subunits.
Both substrate-binding domains (SBD1 and SBD2) are involved in the substrate recognition, and are sufficient to confer the substrate specificity.
CoA ligase; part of the Fusarium detoxification of benzoxazolinone cluster 2 (FDB2) involved in the degradation of benzoxazolinones produced by the host plant (PubMed:19302487, PubMed:26808652). Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their inherent instability once released, spontaneously degrade to the more stable corresponding benzoxazolinones, 6-methoxy-2-benzoxazolinone (MBOA) and 2-benzoxazolinone (BOA), respectively (PubMed:11876429). The first step in the detoxification of benzoxazolinones involves the hydrolysis of the cyclic ester bond of benzoxazolinones by the FDB1 cluster gamma-lactamase MBL1 to aminophenols (PubMed:26808652, PubMed:12788712). MBL1 is able to convert BOA into 2-aminophenol (2-AP), as well as MBOA into 5-methoxy-2-aminophenol (2-AMP) (PubMed:26808652, PubMed:12788712). The FDB2 cluster N-malonyltransferase FDB2/NAT1 then metabolizes aminophenols via N-malonylation to non-toxic malonamic acids (PubMed:19302487, PubMed:12788712). FDB2/NAT1 converts 2-AP into N-(2-hydroxyphenyl) malonamic acid (HPMA) and 2-AMP into N-(2-hydroxy-4-methoxyphenyl) malonamic acid (HMPMA) (PubMed:19302487, PubMed:12788712). The duplicated dienlactone hydrolases DLH1 and DLH2 may provide redundant function for hydrolyzing the lactone moiety in the BOA molecule (Probable). The roles of the amidases an other enzymes encoded by the 2 FDB clusters have not been identified so far (Probable).
Belongs to the peptidase S26 family. IMP2 subfamily.
Belongs to the FKBP-type PPIase family. FKBP3/4 subfamily.
PPIase that acts as a histone chaperone. Histone proline isomerase that increases the rate of cis-trans isomerization at prolines on the histone H3 N-terminal tail. Proline isomerization influences H3 methylation thereby regulating gene expression.
Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Arp2/3 complex plays a critical role in the control of cell morphogenesis via the modulation of cell polarity development.
Belongs to the Clp1 family. NOL9/GRC3 subfamily.
Polynucleotide 5'-kinase involved in rRNA processing.
Required for growth under high-pressure and low-temperature conditions.
Belongs to the CND3 (condensin subunit 3) family.
Belongs to the trans-sulfuration enzymes family.
Belongs to the dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family.
Belongs to the FIT family. Fungal FIT2B/SCS3 subfamily.
Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'-bisphosphate. Preferentially hydrolyzes unsaturated long-chain acyl-CoA substrates in the endoplasmic reticulum (ER) lumen. This catalytic activity is required for maintaining ER structure and for lipid droplets (LDs) biogenesis, which are lipid storage organelles involved in maintaining lipid and energy homeostasis. May directly bind to diacylglycerol (DAGs) and triacylglycerol, which is also important for LD biogenesis. May support directional budding of nacent LDs from the ER into the cytosol by reducing DAG levels at sites of LD formation. May play a role in the regulation of cell morphology and cytoskeletal organization. Involved in phospholipid biosynthesis.
Belongs to the tellurite-resistance/dicarboxylate transporter (TDT) family.
Belongs to the acetate uptake transporter (AceTr) (TC 2.A.96) family.
Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
Serves to protect cells from the toxic effects of hydrogen peroxide.
Belongs to the class VI-like SAM-binding methyltransferase superfamily. Isoprenylcysteine carboxyl methyltransferase family.
Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen.
Belongs to the thiolase-like superfamily. HMG-CoA synthase family.
Catalyzes the condensation of acetyl-CoA with acetoacetyl-CoA to form HMG-CoA.
Mitochondrial transcription factor that confers selective promoter recognition on the core subunit of the yeast mitochondrial RNA polymerase. Interacts with DNA in a non-specific manner.
Belongs to the peptidase M28 family. M28A subfamily.
Belongs to the NmrA-type oxidoreductase family.
NmrA-like family domain-containing oxidoreductase; part of the Fusarium detoxification of benzoxazolinone cluster 1 (FDB1) involved in the degradation of benzoxazolinones produced by the host plant (PubMed:19302487, PubMed:26808652). Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their inherent instability once released, spontaneously degrade to the more stable corresponding benzoxazolinones, 6-methoxy-2-benzoxazolinone (MBOA) and 2-benzoxazolinone (BOA), respectively (PubMed:11876429). The first step in the detoxification of benzoxazolinones involves the hydrolysis of the cyclic ester bond of benzoxazolinones by the FDB1 cluster gamma-lactamase MBL1 to aminophenols (PubMed:26808652, PubMed:12788712). MBL1 is able to convert BOA into 2-aminophenol (2-AP), as well as MBOA into 5-methoxy-2-aminophenol (2-AMP) (PubMed:26808652, PubMed:12788712). The FDB2 cluster N-malonyltransferase FDB2/NAT1 then metabolizes aminophenols via N-malonylation to non-toxic malonamic acids (PubMed:19302487, PubMed:12788712). FDB2/NAT1 converts 2-AP into N-(2-hydroxyphenyl) malonamic acid (HPMA) and 2-AMP into N-(2-hydroxy-4-methoxyphenyl) malonamic acid (HMPMA) (PubMed:19302487, PubMed:12788712). The duplicated dienlactone hydrolases DLH1 and DLH2 may provide redundant function for hydrolyzing the lactone moiety in the BOA molecule (Probable). The roles of the amidases an other enzymes encoded by the 2 FDB clusters have not been identified so far (Probable).
Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 2 subfamily.
Belongs to the ATPase alpha/beta chains family.
Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily.
Essential for vacuolar protein sorting. Required for vacuole biogenesis, stability and to maintain vacuole morphology.
Involved in DNA double-strand break repair (DSBR). Possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity. Also involved in meiotic DSB processing.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily.
Belongs to the polysaccharide lyase 3 family.
Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester.
Probable component of the endoplasmic reticulum-associated degradation (ERAD) pathway.
May be involved in the degradation of misfolded endoplasmic reticulum (ER) luminal proteins.
Belongs to the tryptophan dimethylallyltransferase family.
Catalyzes an early step in riboflavin biosynthesis, the NADPH-dependent reduction of the ribose side chain of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate, yielding 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate.
Belongs to the universal ribosomal protein uS10 family.
Belongs to the polyketide transferase af380 family.
Belongs to the ammonia transporter channel (TC 1.A.11.2) family.
Belongs to the DNA2/NAM7 helicase family.
Part of the nascent polypeptide-associated complex (NAC).
Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family.
Pyridoxal 5'-phosphate (PLP)-binding protein, which may be involved in intracellular homeostatic regulation of pyridoxal 5'-phosphate (PLP), the active form of vitamin B6.
Belongs to the histidine acid phosphatase family.
Required for the synthesis of 40S ribosome subunits. Has a role in processing 20S pre-rRNA into the mature 18S rRNA, where it is required for cleavage at the 3' end of the mature 18S rRNA (D-site). Accompanies the 20S pre-rRNA from the nucleus to the cytoplasm.
Belongs to the G-protein coupled receptor 4 family.
Catalyzes the ferrous insertion into protoporphyrin IX.
Required for the maintenance of the structure of the mitochondrial inner membrane. Involved in mitochondrial morphology. Causes growth arrest when highly overexpressed.
The active site is a redox-active disulfide bond.
Belongs to the glycosyl hydrolase 35 family.
Belongs to the TPT transporter family. SLC35D subfamily.
Involved in the import of GDP-mannose from the cytoplasm into the Golgi lumen.
Belongs to the GST superfamily. Omega family.
This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Belongs to the multicopper oxidase family.
Belongs to the archaeal Rpo12/eukaryotic RPC10 RNA polymerase subunit family.
Belongs to the multi antimicrobial extrusion (MATE) (TC 2.A.66.1) family.
Belongs to the glycosyl hydrolase 51 family.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family.
Functions as actin-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the mother actin filament.
Belongs to the helicase family. Dicer subfamily.
Belongs to the peptidase S8 family. Furin subfamily.
Serine hydrolase involved in the detoxification of formaldehyde.
Belongs to the glycosyl hydrolase 72 family.
Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall.
Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides.
Belongs to the glycosyl hydrolase 32 family.
Belongs to the folylpolyglutamate synthase family.
Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks.
Component of the cytosolic Fe/S protein assembly machinery. Required for maturation of extramitochondrial Fe/S proteins. May play a role in the transfer of pre-assembled Fe/S clusters to target apoproteins.
Required for replication-independent chromatin assembly and for the periodic repression of histone gene transcription during the cell cycle.
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Belongs to the activator 1 small subunits family.
Belongs to the SIMIBI class G3E GTPase family. UreG subfamily.
Belongs to the universal ribosomal protein uL10 family.
Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.
Belongs to the RNA polymerase beta chain family.
Belongs to the peroxidase family. Peroxidase/catalase subfamily.
Binds 1 heme b (iron(II)-protoporphyrin IX) group per monomer.
Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme.
Amidase; part of the Fusarium detoxification of benzoxazolinone cluster 1 (FDB1) involved in the degradation of benzoxazolinones produced by the host plant (PubMed:19302487, PubMed:26808652). Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their inherent instability once released, spontaneously degrade to the more stable corresponding benzoxazolinones, 6-methoxy-2-benzoxazolinone (MBOA) and 2-benzoxazolinone (BOA), respectively (PubMed:11876429). The first step in the detoxification of benzoxazolinones involves the hydrolysis of the cyclic ester bond of benzoxazolinones by the FDB1 cluster gamma-lactamase MBL1 to aminophenols (PubMed:26808652, PubMed:12788712). MBL1 is able to convert BOA into 2-aminophenol (2-AP), as well as MBOA into 5-methoxy-2-aminophenol (2-AMP) (PubMed:26808652, PubMed:12788712). The FDB2 cluster N-malonyltransferase FDB2/NAT1 then metabolizes aminophenols via N-malonylation to non-toxic malonamic acids (PubMed:19302487, PubMed:12788712). FDB2/NAT1 converts 2-AP into N-(2-hydroxyphenyl) malonamic acid (HPMA) and 2-AMP into N-(2-hydroxy-4-methoxyphenyl) malonamic acid (HMPMA) (PubMed:19302487, PubMed:12788712). The duplicated dienlactone hydrolases DLH1 and DLH2 may provide redundant function for hydrolyzing the lactone moiety in the BOA molecule (Probable). The roles of the amidases an other enzymes encoded by the 2 FDB clusters have not been identified so far (Probable).
Belongs to the glucose-6-phosphate dehydrogenase family.
Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis.
Belongs to the methyltransferase superfamily. LaeA methyltransferase family.
Component of the heterotrimeric velvet complex composed of LAE1, VE1 and VELB; VE1 acting as a bridging protein between LAE1 and VELB (By similarity).
Impairs production of bikaverin, fumonisins, fusaric acid, and fusarins (PubMed:22713715).
Methyltransferase that performs automethylation (By similarity). No other methyl-accepting substrate has been identified yet (By similarity). Component of the velvet transcription factor complex that acts as a global regulator for secondary metabolite gene expression (PubMed:22713715). Controls the expression of the bikaverin, fumonisins, fusaric acid, and fusarins gene clusters; as well as two clusters for which the corresponding secondary metabolite is unknown (PubMed:22713715).
Belongs to the copper/topaquinone oxidase family.
Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Belongs to the concentrative nucleoside transporter (CNT) (TC 2.A.41) family.
Belongs to the cytochrome c-type heme lyase family.
Lyase that catalyzes the covalent linking of the heme group to the cytochrome C apoprotein to produce the mature functional cytochrome.
Belongs to the eukaryotic ribosomal protein eL42 family.
Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 2 subfamily.
Belongs to the SEC23/SEC24 family. SEC24 subfamily.
Belongs to the choline monooxygenase family.
Catalyzes the first step of the osmoprotectant glycine betaine synthesis.
ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner.
Homohexamer or homoheptamer. Organized in a ring with a central cavity.
Belongs to the poly(A) polymerase family.
Inclusion body (IB) resident protein that interacts strongly with lipid droplet (LD) proteins. Involved in LD-mediated IB clearing after protein folding stress, probably by enabling access to the IBs of an LD-stored soluble sterol derivative that acts as chaperone in inclusion clearing.
Belongs to the thioesterase PaaI family.
Belongs to the Mediator complex subunit 21 family.
Belongs to the universal ribosomal protein uL24 family.
Alpha-glucuronidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Releases 4-O-methylglucuronic acid from xylan.
Belongs to the glycosyl hydrolase 67 family.
Forms a chaperone-bound H2A.Z-H2B complex that acts as a source for SWR1 complex-dependent H2A to H2A.Z histone replacement in chromatin.
Forms a heterotrimer with H2A.Z-H2B, stabilizing the association of the histone dimer. Also, with a lower affinity, forms a heterotrimer with H2A-H2B.
Belongs to the eukaryotic RPC9 RNA polymerase subunit family.
FAD-dependent monooxygenase; part of the Fusarium detoxification of benzoxazolinone cluster 1 (FDB1) involved in the degradation of benzoxazolinones produced by the host plant (PubMed:19302487, PubMed:26808652). Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their inherent instability once released, spontaneously degrade to the more stable corresponding benzoxazolinones, 6-methoxy-2-benzoxazolinone (MBOA) and 2-benzoxazolinone (BOA), respectively (PubMed:11876429). The first step in the detoxification of benzoxazolinones involves the hydrolysis of the cyclic ester bond of benzoxazolinones by the FDB1 cluster gamma-lactamase MBL1 to aminophenols (PubMed:26808652, PubMed:12788712). MBL1 is able to convert BOA into 2-aminophenol (2-AP), as well as MBOA into 5-methoxy-2-aminophenol (2-AMP) (PubMed:26808652, PubMed:12788712). The FDB2 cluster N-malonyltransferase FDB2/NAT1 then metabolizes aminophenols via N-malonylation to non-toxic malonamic acids (PubMed:19302487, PubMed:12788712). FDB2/NAT1 converts 2-AP into N-(2-hydroxyphenyl) malonamic acid (HPMA) and 2-AMP into N-(2-hydroxy-4-methoxyphenyl) malonamic acid (HMPMA) (PubMed:19302487, PubMed:12788712). The duplicated dienlactone hydrolases DLH1 and DLH2 may provide redundant function for hydrolyzing the lactone moiety in the BOA molecule (Probable). The roles of the amidases an other enzymes encoded by the 2 FDB clusters have not been identified so far (Probable).
Belongs to the DEAD box helicase family.
Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.
Catalyzes the synthesis of 5-aminolevulinate (ALA) from succinyl-CoA and glycine, the first and rate-limiting step in heme biosynthesis.
Belongs to the type IB topoisomerase family.
Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at the specific target site 5'-[CT]CCTTp site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.
Belongs to the dihydroorotate dehydrogenase family. Type 1 subfamily.
Catalyzes the conversion of dihydroorotate to orotate with fumarate as the electron acceptor.
Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Belongs to the actin-binding proteins ADF family. Twinfilin subfamily.
Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2-thiolation reaction by being thiocarboxylated (-COSH) at its C-terminus by the MOCS3 homolog UBA4. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. Also acts as a ubiquitin-like protein (UBL) that is covalently conjugated via an isopeptide bond to lysine residues of target proteins such as AHP1. The thiocarboxylated form serves as substrate for conjugation and oxidative stress specifically induces the formation of UBL-protein conjugates.
C-terminal thiocarboxylation occurs in 2 steps, it is first acyl-adenylated (-COAMP) via the hesA/moeB/thiF part of UBA4, then thiocarboxylated (-COSH) via the rhodanese domain of UBA4.
Has a dual role in the assembly of mitochondrial ATPase. Acts as a protease that removes N-terminal residues of mitochondrial ATPase CF(0) subunit 6 at the intermembrane space side. Also involved in the correct assembly of the membrane-embedded ATPase CF(0) particle, probably mediating association of subunit 6 with the subunit 9 ring.
Necessary for protein synthesis in mitochondria. Functions as a ribosome recycling factor in mitochondria.
Belongs to the spermidine/spermine synthase family.
Belongs to the group II decarboxylase family.
Belongs to the eIF-2B alpha/beta/delta subunits family. MtnA subfamily.
Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Belongs to the dermatan-sulfate isomerase family.
Accessory subunit of the DNA polymerase alpha complex (also known as the alpha DNA polymerase-primase complex) which plays an essential role in the initiation of DNA synthesis.
Belongs to the DNA polymerase alpha subunit B family.
Belongs to the V-ATPase C subunit family.
Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment. Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity.
V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex.
Belongs to the GHMP kinase family. GalK subfamily.
Belongs to the tRNA pseudouridine synthase TruA family.
Belongs to the succinate/malate CoA ligase beta subunit family.
Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Belongs to the steroid 5-alpha reductase family.
Belongs to the TFIIF alpha subunit family.
ABC transporter that may provide the dual role fumonisin export and self-protection by allowing the fungus to evade the harmful effect of its own fumonisin production (PubMed:12620260).
Belongs to the ABC transporter superfamily. ABCC family. Conjugate transporter (TC 3.A.1.208) subfamily.
Does not affect the production of fumonisins B1 and B2, but strongly decreases the production of fumonisin B3 (PubMed:12620260).
Expression is strongly reduced by benomyl (PubMed:25217721).
Belongs to the universal ribosomal protein uL3 family.
Associates with DNA double-strand breaks.
Belongs to the PI3/PI4-kinase family. ATM subfamily.
Serine/threonine protein kinase which activates checkpoint signaling upon genotoxic stresses such as ionizing radiation (IR), ultraviolet light (UV), or DNA replication stalling, thereby acting as a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates histone H2A to form H2AS128ph (gamma-H2A) at sites of DNA damage, involved in the regulation of DNA damage response mechanism. Required for the control of telomere length and genome stability.
Belongs to the two pore domain potassium channel (TC 1.A.1.8) family.
Belongs to the diacylglycerol acyltransferase family.
3-hydroxyacyl-CoA dehydrogenase; part of the Fusarium detoxification of benzoxazolinone cluster 2 (FDB2) involved in the degradation of benzoxazolinones produced by the host plant (PubMed:19302487, PubMed:26808652). Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their inherent instability once released, spontaneously degrade to the more stable corresponding benzoxazolinones, 6-methoxy-2-benzoxazolinone (MBOA) and 2-benzoxazolinone (BOA), respectively (PubMed:11876429). The first step in the detoxification of benzoxazolinones involves the hydrolysis of the cyclic ester bond of benzoxazolinones by the FDB1 cluster gamma-lactamase MBL1 to aminophenols (PubMed:26808652, PubMed:12788712). MBL1 is able to convert BOA into 2-aminophenol (2-AP), as well as MBOA into 5-methoxy-2-aminophenol (2-AMP) (PubMed:26808652, PubMed:12788712). The FDB2 cluster N-malonyltransferase FDB2/NAT1 then metabolizes aminophenols via N-malonylation to non-toxic malonamic acids (PubMed:19302487, PubMed:12788712). FDB2/NAT1 converts 2-AP into N-(2-hydroxyphenyl) malonamic acid (HPMA) and 2-AMP into N-(2-hydroxy-4-methoxyphenyl) malonamic acid (HMPMA) (PubMed:19302487, PubMed:12788712). The duplicated dienlactone hydrolases DLH1 and DLH2 may provide redundant function for hydrolyzing the lactone moiety in the BOA molecule (Probable). The roles of the amidases an other enzymes encoded by the 2 FDB clusters have not been identified so far (Probable).
Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family.
Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites.
Belongs to the polysaccharide lyase 1 family.
Acts as a sulfur carrier required for molybdopterin biosynthesis. Component of the molybdopterin synthase complex that catalyzes the conversion of precursor Z into molybdopterin by mediating the incorporation of 2 sulfur atoms into precursor Z to generate a dithiolene group. In the complex, serves as sulfur donor by being thiocarboxylated (-COSH) at its C-terminus by UBA4. After interaction with MOCS2B, the sulfur is then transferred to precursor Z to form molybdopterin.
Belongs to the MoaD family. MOCS2A subfamily.
Heterotetramer; composed of 2 small (MOCS2A) and 2 large (MOCS2B) subunits.
Plays an important role in the control of DNA replication and the maintenance of replication fork stability.
Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. TrmE GTPase family.
Component of the NuA4 histone acetyltransferase complex.
Belongs to the WD repeat BOP1/ERB1 family.
Belongs to the C/M/P thioester hydrolase family.
ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Belongs to the DEAD box helicase family. DDX54/DBP10 subfamily.
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Catalytic subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA.
Belongs to the archaeal Rpo10/eukaryotic RPB10 RNA polymerase subunit family.
F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel.
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane.
Belongs to the glycosyl hydrolase 13 family. GlgB subfamily.
Belongs to the cytidylyltransferase family.
Belongs to the mannitol dehydrogenase family.
Catalyzes the NAD(H)-dependent interconversion of D-fructose 6-phosphate and D-mannitol 1-phosphate in the mannitol metabolic pathway.
Catalyzes the second and fifth step in the 'de novo' purine biosynthesis pathway; contains phosphoribosylamine--glycine ligase (GARS) and phosphoribosylformylglycinamidine cyclo-ligase (AIRS) activities.
In the C-terminal section; belongs to the AIR synthase family.
In the N-terminal section; belongs to the GARS family.
Acyl-CoA synthetase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), and B4 (FB4), which are carcinogenic mycotoxins (PubMed:12620260). On the basis of the chemical structures of fumonisins and precursor feeding studies, fumonisin biosynthesis is predicted to include at least five groups of biochemical reactions: synthesis of a linear polyketide with a single terminal carbonyl function and methyl groups at C-10 and C-14; condensation of the polyketide with alanine; reduction of the polyketide carbonyl to a hydroxyl; hydroxylation of 2-4 polyketide carbons; and esterification of six-carbon tricarboxylic acids to two of the hydroxyls (PubMed:12620260). The biosynthesis starts with the polyketide synthase FUM1-catalyzed carbon chain assembly from one molecule of acetyl CoA, eight molecules of malonyl CoA, and two molecules of methionine (PubMed:10413619). The C-18 polyketide chain is released from the enzyme by a nucleophilic attack of a carbanion, which is derived from R-carbon of alanine by decarboxylation, on the carbonyl carbon of polyketide acyl chain (PubMed:15137825, PubMed:12720383). This step is catalyzed by a pyridoxal 5'-phosphate-dependent aminoacyl transferase FUM8 (PubMed:15137825, PubMed:12720383). The resultant 3-keto intermediate 2-amino-3-oxo-12,16-dimethylicosane is then stereospecifically reduced to the 3-hydroxyl product 2-amino-3-hydroxy-12,16-dimethylicosane by reductase FUM13 (PubMed:12720383, PubMed:15137825). Subsequent oxidations at C-5, C-10, C-14 and C-15 followed by tricarballylic esterification of the hydroxyl groups on C-14 and C-15 furnish the biosynthesis of fumonisins (PubMed:15066782, PubMed:15137825, PubMed:16489749). The C-10 hydroxylation is performed by the cytochrome P450 monooxygenase FUM2 and occurs early in the biosynthesis (PubMed:16536629). The C-5 hydroxylation is performed by the dioxygenase FUM3 and occurs late in the biosynthesis (PubMed:20237561, PubMed:15066782, PubMed:15137825, PubMed:16536629). Cytochrome P450 monooxygenases FUM6 and FUM15 may be responsible for the two remaining hydroxylations at positions C-14 and C-15 (PubMed:12620260). The FUM11 tricarboxylate transporter makes a tricarboxylic acid precursor available for fumonisin biosynthesis via its export from the mitochondria (PubMed:12620260). If the precursor is citrate, the FUM7 dehydrogenase could remove the C-3 hydroxyl of citrate to form tricarballylic acid either before or after the CoA activation by the FUM10 acyl-CoA synthetase and FUM14 catalyzed esterification of CoA-activated tricarballylic acid to the C-14 and C-15 hydroxyls of the fumonisin backbone (PubMed:16489749, PubMed:17147424). Alternatively, if the precursor is cis-aconitate, FUM7 may function to reduce the double bond (PubMed:17147424). In this alternate proposal, feeding studies with tetradehydro-fumonisin B1 suggests that FUM7 cannot function on the tricarballylic ester and must therefore act before the FUM14-mediated esterification (PubMed:17147424).
Does not affect fumonisin production (PubMed:17147424).
Belongs to the complex I 75 kDa subunit family.
Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.
Belongs to the inorganic phosphate transporter (PiT) (TC 2.A.20) family.
Sodium-phosphate symporter which plays a fundamental housekeeping role in phosphate transport.
Belongs to the transferase hexapeptide repeat family.
Belongs to the inositol phosphokinase (IPK) family.
Belongs to the dynein heavy chain family.
Belongs to the NFYA/HAP2 subunit family.
Component of the sequence-specific heterotrimeric transcription factor (NF-Y) which specifically recognizes a 5'-CCAAT-3' box motif found in the promoters of its target genes.
Supercomplex made of cofactors A to E. Cofactors A and D function by capturing and stabilizing tubulin in a quasi-native conformation. Cofactor E binds to the cofactor D-tubulin complex; interaction with cofactor C then causes the release of tubulin polypeptides that are committed to the native state.
Belongs to the snRNP Sm proteins family.
LSm subunits form a heteromer with a doughnut shape.
Plays role in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as component of the precatalytic spliceosome (spliceosome B complex). The heptameric LSM2-8 complex binds specifically to the 3'-terminal U-tract of U6 snRNA.
Carboxylic ester hydrolase; part of the Fusarium detoxification of benzoxazolinone cluster 2 (FDB2) involved in the degradation of benzoxazolinones produced by the host plant (PubMed:19302487, PubMed:26808652). Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their inherent instability once released, spontaneously degrade to the more stable corresponding benzoxazolinones, 6-methoxy-2-benzoxazolinone (MBOA) and 2-benzoxazolinone (BOA), respectively (PubMed:11876429). The first step in the detoxification of benzoxazolinones involves the hydrolysis of the cyclic ester bond of benzoxazolinones by the FDB1 cluster gamma-lactamase MBL1 to aminophenols (PubMed:26808652, PubMed:12788712). MBL1 is able to convert BOA into 2-aminophenol (2-AP), as well as MBOA into 5-methoxy-2-aminophenol (2-AMP) (PubMed:26808652, PubMed:12788712). The FDB2 cluster N-malonyltransferase FDB2/NAT1 then metabolizes aminophenols via N-malonylation to non-toxic malonamic acids (PubMed:19302487, PubMed:12788712). FDB2/NAT1 converts 2-AP into N-(2-hydroxyphenyl) malonamic acid (HPMA) and 2-AMP into N-(2-hydroxy-4-methoxyphenyl) malonamic acid (HMPMA) (PubMed:19302487, PubMed:12788712). The duplicated dienlactone hydrolases DLH1 and DLH2 may provide redundant function for hydrolyzing the lactone moiety in the BOA molecule (Probable). The roles of the amidases an other enzymes encoded by the 2 FDB clusters have not been identified so far (Probable).
Belongs to the glycosyltransferase 34 family.
Belongs to the glycosyltransferase 77 family.
Belongs to the SLC35F solute transporter family.
Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production.
Belongs to the CTL (choline transporter-like) family.
Probably involved in transport through the plasma membrane.
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.
Belongs to the peroxiredoxin family. Prx5 subfamily.
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
Belongs to the NAD(P)-dependent epimerase/dehydratase family. GDP-mannose 4,6-dehydratase subfamily.
Belongs to the DEAD box helicase family. DDX47/RRP3 subfamily.
Has a role in mitochondrial fission. Has a role in outer membrane fission but not matrix separation.
Belongs to the helicase family. RecQ subfamily.
Belongs to the acireductone dioxygenase (ARD) family.
Binds either 1 Fe or Ni cation per monomer. Iron-binding promotes an acireductone dioxygenase reaction producing 2-keto-4-methylthiobutyrate, while nickel-binding promotes an acireductone dioxygenase reaction producing 3-(methylsulfanyl)propanoate.
Catalyzes 2 different reactions between oxygen and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway.
Belongs to the AB hydrolase superfamily. AB hydrolase 4 family.
Belongs to the aspartate-semialdehyde dehydrogenase family.
Belongs to the phage and mitochondrial RNA polymerase family.
Belongs to the class I-like SAM-binding methyltransferase superfamily. TRM5/TYW2 family.
Specifically methylates the N1 position of guanosine-37 in various cytoplasmic and mitochondrial tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs and required for accurate decoding.
Belongs to the ATP phosphoribosyltransferase family.
Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.
Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis.
Belongs to the glycogen phosphorylase family.
Component of the mitochondrial large ribosomal subunit.
Belongs to the eukaryotic ribosomal protein eL13 family.
Belongs to the squalene monooxygenase family.
Catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, and is considered to be a rate-limiting enzyme in steroid biosynthesis.
Catalytic component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity). Specifically cleaves N-terminal signal peptides that contain a hydrophobic alpha-helix (h-region) shorter than 18-20 amino acids.
Component of the signal peptidase complex (SPC) composed of a catalytic subunit SEC11 and three accessory subunits SPC1, SPC2 and SPC3 (By similarity). The complex induces a local thinning of the ER membrane which is used to measure the length of the signal peptide (SP) h-region of protein substrates. This ensures the selectivity of the complex towards h-regions shorter than 18-20 amino acids (By similarity). SPC associates with the translocon complex.
Belongs to the universal ribosomal protein uS13 family.
Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19) family. SLC24A subfamily.
Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. NOG subfamily.
Involved in the biogenesis of the 60S ribosomal subunit.
Endoplasmic reticulum-Golgi intermediate compartment membrane
Plays a role in transport between endoplasmic reticulum and Golgi.
Belongs to the glycosyl hydrolase 30 family.
Binds 2 divalent metal cations per subunit. Magnesium or manganese.
Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
Belongs to the helicase family. SKI2 subfamily.
Catalyzes the hydroxylation of 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2) during ubiquinone biosynthesis. Has also a structural role in the COQ enzyme complex, stabilizing other COQ polypeptides.
Component of a multi-subunit COQ enzyme complex, composed of at least COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9.
Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase kinase subfamily.
Belongs to the TRAFAC class YlqF/YawG GTPase family. NOG2 subfamily.
GTPase that associates with pre-60S ribosomal subunits in the nucleolus and is required for their nuclear export and maturation.
Belongs to the ETF alpha-subunit/FixB family.
The electron transfer flavoprotein serves as a specific electron acceptor for several dehydrogenases, including five acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase).
Belongs to the polysaccharide lyase 4 family.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA methyltransferase RlmE family. TRM7 subfamily.
Methylates the 2'-O-ribose of nucleotides at positions 32 and 34 of the tRNA anticodon loop of substrate tRNAs.
Belongs to the activator 1 large subunit family.
Belongs to the prefoldin subunit beta family.
Belongs to the aldo/keto reductase family.
Belongs to the mitochondrion-specific ribosomal protein mL41 family.
Belongs to the dienelactone hydrolase family.
Dienlactone hydrolase; part of the Fusarium detoxification of benzoxazolinone cluster 1 (FDB1) involved in the degradation of benzoxazolinones produced by the host plant (PubMed:19302487, PubMed:26808652). Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their inherent instability once released, spontaneously degrade to the more stable corresponding benzoxazolinones, 6-methoxy-2-benzoxazolinone (MBOA) and 2-benzoxazolinone (BOA), respectively (PubMed:11876429). The first step in the detoxification of benzoxazolinones involves the hydrolysis of the cyclic ester bond of benzoxazolinones by the FDB1 cluster gamma-lactamase MBL1 to aminophenols (PubMed:26808652, PubMed:12788712). MBL1 is able to convert BOA into 2-aminophenol (2-AP), as well as MBOA into 5-methoxy-2-aminophenol (2-AMP) (PubMed:26808652, PubMed:12788712). The FDB2 cluster N-malonyltransferase FDB2/NAT1 then metabolizes aminophenols via N-malonylation to non-toxic malonamic acids (PubMed:19302487, PubMed:12788712). FDB2/NAT1 converts 2-AP into N-(2-hydroxyphenyl) malonamic acid (HPMA) and 2-AMP into N-(2-hydroxy-4-methoxyphenyl) malonamic acid (HMPMA) (PubMed:19302487, PubMed:12788712). The duplicated dienlactone hydrolases DLH1 and DLH2 may provide redundant function for hydrolyzing the lactone moiety in the BOA molecule (Probable). The roles of the amidases and other enzymes encoded by the 2 FDB clusters have not been identified so far (Probable).
Retains 2-benzoxazolinone (BOA)-tolerance and metabolic degradation capability (PubMed:26808652). Does not affect the virulence against maize seedlings (PubMed:26808652).
Belongs to the acyl-CoA dehydrogenase family.
tRNA nucleus export receptor which facilitates tRNA translocation across the nuclear pore complex. Involved in pre-tRNA splicing, probably by affecting the interaction of pre-tRNA with splicing endonuclease.
Belongs to the mitochondrial carrier (TC 2.A.29) family. SLC25A38 subfamily.
Mitochondrial glycine transporter that imports glycine into the mitochondrial matrix. Plays an important role in providing glycine for the first enzymatic step in heme biosynthesis, the condensation of glycine with succinyl-CoA to produce 5-aminolevulinate (ALA) in the miochondrial matrix.
Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack independent of vesicle origin.
Belongs to the NADH dehydrogenase family.
In the N-terminal section; belongs to the FGAMS family.
Belongs to the WD repeat MET30/SCONB/SCON-2 family.
In the C-terminal section; belongs to the anthranilate synthase component I family.
Belongs to the bacterial ribosomal protein bL19 family.
Belongs to the mitochondrion-specific ribosomal protein mS23 family.
Component of the mitochondrial small ribosomal subunit.
Belongs to the phosphatase 2A regulatory subunit.
The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment.
Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
Belongs to the peptidase C2 family. PalB/RIM13 subfamily.
Belongs to the glycosyl hydrolase 76 family.
The EMC seems to be required for efficient folding of proteins in the endoplasmic reticulum (ER).
Belongs to the Necrosis inducing protein (NPP1) family.
Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants. Degrades cutin, a macromolecule that forms the structure of the plant cuticle.
Belongs to the isocitrate lyase/PEP mutase superfamily. Isocitrate lyase family.
Belongs to the SurE nucleotidase family.
Long-chain fatty alcohol oxidase involved in the omega-oxidation pathway of lipid degradation.
RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. This subunit can bind 18S rRNA.
Belongs to the fatty acid desaturase type 1 family. DEGS subfamily.
Delta(4)-fatty-acid desaturase which introduces a double bond at the 4-position in the long-chain base (LCB) of ceramides.
Belongs to the universal ribosomal protein uL18 family.
Belongs to the glycosyl hydrolase 37 family.
Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits.
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen.
Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.
Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1) involved in endosomal cargo sorting.
Belongs to the ERCC1/RAD10/SWI10 family.
Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation.
Component of the COMPASS (Set1C) complex.
Belongs to the FNT transporter (TC 2.A.44) family.
Belongs to the GHMP kinase family. Homoserine kinase subfamily.
Involved in the partitioning of the mitochondrial organelle and mitochondrial DNA (mtDNA) inheritance.
RNA-binding nucleolar protein required for pre-rRNA processing. Involved in production of 18S rRNA and assembly of small ribosomal subunit.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIIB subfamily.
Mediates magnesium influx to the cytosol.
Belongs to the peptidase M67A family. CSN5 subfamily.
Component of the COP9 signalosome (CSN) complex.
Belongs to the SMC family. SMC4 subfamily.
Involved in determination of the onset of polarized growth and morphogenesis. Plays a role in the regulation of branching in hyphae and spore formation.
Belongs to the glycosyl hydrolase 17 family.
Belongs to the bacterial ribosomal protein bL34 family.
Associates with the respiratory chain complex III/complex IV supercomplex.
Cytochrome c oxidase subunit which plays a role in assembly of respiratory supercomplexes.
Belongs to the glutathione peroxidase family.
Belongs to the major facilitator superfamily. Proton-dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family.
Belongs to the acetyltransferase family. GCN5 subfamily.
Belongs to the eukaryotic initiation factor 4E family.
Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures.
Secreted aspartic protease; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C (PubMed:22652150). Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production (By similarity). The other FUS cluster members are not essential for fusarin C biosynthesis (By similarity).
Belongs to the mitochondrion-specific ribosomal protein mS37 family.
Involved in mitochondrial genome encoded proteins translation.
Component of the cytoplasmic LSM1-LSM7 complex which is involved in mRNA degradation.
Component of the heptameric LSM1-LSM7 complex that forms a seven-membered ring structure with a donut shape.
The COPII coat is composed of at least 5 proteins: the SEC23/24 complex, the SEC13/31 complex, and the protein SAR1. SEC13 and SEC31 make a 2:2 tetramer that forms the edge element of the COPII outer coat. The tetramer self-assembles in multiple copies to form the complete polyhedral cage. Interacts (via WD 8) with SEC13.
Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. NIM1 subfamily.
Belongs to the SNF2/RAD54 helicase family.
Belongs to the DNA/RNA non-specific endonuclease family.
Dehydrogenase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), and B4 (FB4), which are carcinogenic mycotoxins (PubMed:11728154, PubMed:12620260, PubMed:17147424). On the basis of the chemical structures of fumonisins and precursor feeding studies, fumonisin biosynthesis is predicted to include at least five groups of biochemical reactions: synthesis of a linear polyketide with a single terminal carbonyl function and methyl groups at C-10 and C-14; condensation of the polyketide with alanine; reduction of the polyketide carbonyl to a hydroxyl; hydroxylation of 2-4 polyketide carbons; and esterification of six-carbon tricarboxylic acids to two of the hydroxyls (PubMed:12620260). The biosynthesis starts with the polyketide synthase FUM1-catalyzed carbon chain assembly from one molecule of acetyl CoA, eight molecules of malonyl CoA, and two molecules of methionine (PubMed:10413619). The C-18 polyketide chain is released from the enzyme by a nucleophilic attack of a carbanion, which is derived from R-carbon of alanine by decarboxylation, on the carbonyl carbon of polyketide acyl chain (PubMed:15137825, PubMed:12720383). This step is catalyzed by a pyridoxal 5'-phosphate-dependent aminoacyl transferase FUM8 (PubMed:15137825, PubMed:12720383). The resultant 3-keto intermediate 2-amino-3-oxo-12,16-dimethylicosane is then stereospecifically reduced to the 3-hydroxyl product 2-amino-3-hydroxy-12,16-dimethylicosane by reductase FUM13 (PubMed:12720383, PubMed:15137825). Subsequent oxidations at C-5, C-10, C-14 and C-15 followed by tricarballylic esterification of the hydroxyl groups on C-14 and C-15 furnish the biosynthesis of fumonisins (PubMed:15066782, PubMed:15137825, PubMed:16489749). The C-10 hydroxylation is performed by the cytochrome P450 monooxygenase FUM2 and occurs early in the biosynthesis (PubMed:16536629). The C-5 hydroxylation is performed by the dioxygenase FUM3 and occurs late in the biosynthesis (PubMed:20237561, PubMed:15066782, PubMed:15137825, PubMed:16536629). Cytochrome P450 monooxygenases FUM6 and FUM15 may be responsible for the two remaining hydroxylations at positions C-14 and C-15 (PubMed:12620260). The FUM11 tricarboxylate transporter makes a tricarboxylic acid precursor available for fumonisin biosynthesis via its export from the mitochondria (PubMed:12620260). If the precursor is citrate, the FUM7 dehydrogenase could remove the C-3 hydroxyl of citrate to form tricarballylic acid either before or after the CoA activation by the FUM10 acyl-CoA synthetase and FUM14 catalyzed esterification of CoA-activated tricarballylic acid to the C-14 and C-15 hydroxyls of the fumonisin backbone (PubMed:16489749, PubMed:17147424). Alternatively, if the precursor is cis-aconitate, FUM7 may function to reduce the double bond (PubMed:17147424). In this alternate proposal, feeding studies with tetradehydro-fumonisin B1 suggests that FUM7 cannot function on the tricarballylic ester and must therefore act before the FUM14-mediated esterification (PubMed:17147424).
Expression correlates with fuminisins production (PubMed:11728154).
Impairs the production of fumonisins but accumaulates the intermediate tetradehydro-fumonisin B1 (PubMed:17147424).
Belongs to the Orn/Lys/Arg decarboxylase class-II family.
Acts as catalytic component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover (By similarity). Ccr4 has 3'-5' RNase activity with a strong preference for polyadenylated substrates and also low exonuclease activity towards single-stranded DNA.
Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for the ferulic acid decarboxylase FDC1. The prenyltransferase is metal-independent and links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms of FMN.
Participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. Involved in assembling the dolichol-pyrophosphate-GlcNAc(2)-Man(5) intermediate on the cytoplasmic surface of the ER.
Activated by threonine and tyrosine phosphorylation.
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. MAP kinase subfamily.
A pair of annexin repeats may form one binding site for calcium and phospholipid.
Belongs to the homogentisate dioxygenase family.
Belongs to the glutamine synthetase family.
Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
Component of complex II composed of four subunits: a flavoprotein (FP), an iron-sulfur protein (IP), and a cytochrome b composed of a large and a small subunit.
Iron-sulfur protein (IP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Non catalytic subunit of RNase H2, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes.
Component of the pre-66S ribosomal particle.
Belongs to the amino acid-polyamine-organocation (APC) superfamily. YAT (TC 2.A.3.10) family.
Belongs to the eukaryotic ribosomal protein eL39 family.
Belongs to the histone deacetylase family. HD Type 1 subfamily.
Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of acetylglutamate from glutamate and acetyl-CoA, and of ornithine by transacetylation between acetylornithine and glutamate.
Heterodimer of an alpha and a beta chain.
The alpha and beta chains are autoproteolytically processed from a single precursor protein within the mitochondrion.
Belongs to the peptidase M67A family. CSN6 subfamily.
Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes.
Belongs to the DHHC palmitoyltransferase family. AKR/ZDHHC17 subfamily.
Palmitoyltransferase specific for casein kinase 1.
The DHHC domain is required for palmitoyltransferase activity.
Belongs to the TRAPP small subunits family. BET3 subfamily.
Part of the multisubunit TRAPP (transport protein particle) complex.
Plays a key role in the late stages of endoplasmic reticulum to Golgi traffic.
Belongs to the CDP-alcohol phosphatidyltransferase class-I family.
Belongs to the glucosamine/galactosamine-6-phosphate isomerase family.
Does not affect the production of fumonisins B1, B2 and B3 (PubMed:12620260).
Sphingosine N-acyltransferase-like protein; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), and B4 (FB4), which are carcinogenic mycotoxins (PubMed:12620260). On the basis of the chemical structures of fumonisins and precursor feeding studies, fumonisin biosynthesis is predicted to include at least five groups of biochemical reactions: synthesis of a linear polyketide with a single terminal carbonyl function and methyl groups at C-10 and C-14; condensation of the polyketide with alanine; reduction of the polyketide carbonyl to a hydroxyl; hydroxylation of 2-4 polyketide carbons; and esterification of six-carbon tricarboxylic acids to two of the hydroxyls (PubMed:12620260). The biosynthesis starts with the polyketide synthase FUM1-catalyzed carbon chain assembly from one molecule of acetyl CoA, eight molecules of malonyl CoA, and two molecules of methionine (PubMed:10413619). The C-18 polyketide chain is released from the enzyme by a nucleophilic attack of a carbanion, which is derived from R-carbon of alanine by decarboxylation, on the carbonyl carbon of polyketide acyl chain (PubMed:15137825, PubMed:12720383). This step is catalyzed by a pyridoxal 5'-phosphate-dependent aminoacyl transferase FUM8 (PubMed:15137825, PubMed:12720383). The resultant 3-keto intermediate 2-amino-3-oxo-12,16-dimethylicosane is then stereospecifically reduced to the 3-hydroxyl product 2-amino-3-hydroxy-12,16-dimethylicosane by reductase FUM13 (PubMed:12720383, PubMed:15137825). Subsequent oxidations at C-5, C-10, C-14 and C-15 followed by tricarballylic esterification of the hydroxyl groups on C-14 and C-15 furnish the biosynthesis of fumonisins (PubMed:15066782, PubMed:15137825, PubMed:16489749). The C-10 hydroxylation is performed by the cytochrome P450 monooxygenase FUM2 and occurs early in the biosynthesis (PubMed:16536629). The C-5 hydroxylation is performed by the dioxygenase FUM3 and occurs late in the biosynthesis (PubMed:20237561, PubMed:15066782, PubMed:15137825, PubMed:16536629). Cytochrome P450 monooxygenases FUM6 and FUM15 may be responsible for the two remaining hydroxylations at positions C-14 and C-15 (PubMed:12620260). The FUM11 tricarboxylate transporter makes a tricarboxylic acid precursor available for fumonisin biosynthesis via its export from the mitochondria (PubMed:12620260). If the precursor is citrate, the FUM7 dehydrogenase could remove the C-3 hydroxyl of citrate to form tricarballylic acid either before or after the CoA activation by the FUM10 acyl-CoA synthetase and FUM14 catalyzed esterification of CoA-activated tricarballylic acid to the C-14 and C-15 hydroxyls of the fumonisin backbone (PubMed:16489749, PubMed:17147424). Alternatively, if the precursor is cis-aconitate, FUM7 may function to reduce the double bond (PubMed:17147424). In this alternate proposal, feeding studies with tetradehydro-fumonisin B1 suggests that FUM7 cannot function on the tricarballylic ester and must therefore act before the FUM14-mediated esterification (PubMed:17147424). FUM17 is not required for production of fumonosins but may have an indirect role such as self-protection (PubMed:12620260).
Belongs to the ubiquitin-activating E1 family. ULA1 subfamily.
Regulatory subunit of the dimeric UBA3-ULA1 E1 enzyme.
Belongs to the glycosyl hydrolase 7 (cellulase C) family.
Belongs to the glycosyl hydrolase 2 family.
May interact with target proteins during translocation into the lumen of the endoplasmic reticulum. May protect unfolded target proteins against degradation and facilitate correct glycosylation.
Belongs to the V-ATPase D subunit family.
Belongs to the DNA polymerase type-B family.
Belongs to the TRAPP small subunits family.
Part of the multisubunit transport protein particle (TRAPP) complex.
Belongs to the low molecular weight phosphotyrosine protein phosphatase family.
Belongs to the eukaryotic release factor 1 family. Pelota subfamily.
May function in recognizing stalled ribosomes and triggering endonucleolytic cleavage of the mRNA, a mechanism to release non-functional ribosomes and degrade damaged mRNAs.
Arginine methyltransferase involved in the assembly or stability of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I).
Belongs to the universal ribosomal protein uS9 family.
Belongs to the chloride channel (TC 2.A.49) family.
Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively.
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration.
Belongs to the peptidase M28 family. M28B subfamily.
Required for efficient biogenesis of the 60S ribosomal subunit.
Belongs to the Clp1 family. Clp1 subfamily.
Component of a pre-mRNA cleavage factor complex. Interacts directly with PCF11.
May lack the polyribonucleotide 5'-hydroxyl-kinase and polynucleotide 5'-hydroxyl-kinase activities that are characteristic of the human ortholog.
Required for endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation.
Belongs to the eukaryotic ATPase B chain family.
F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. In yeast, the dimeric form of ATP synthase consists of 17 polypeptides: alpha, beta, gamma, delta, epsilon, 4 (B), 5 (OSCP), 6 (A), 8, 9 (C), d, E (Tim11), f, g, h, i/j and k.
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.
Belongs to the XRCC4-XLF family. XLF subfamily.
Belongs to the glycosyl hydrolase 16 family.
Belongs to the ThrE exporter (TC 2.A.79) family.
Consists of at least two heavy chains and a number of intermediate and light chains.
Belongs to the universal ribosomal protein uL6 family.
Belongs to the snRNP core protein family.
Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins.
Belongs to the glycosyl hydrolase 29 family.
Belongs to the poly(ADP-ribose) glycohydrolase family.
Belongs to the threonine aldolase family.
Belongs to the bacterial ribosomal protein bL27 family.
Belongs to the DDOST 48 kDa subunit family.
Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER).
Belongs to the prephenate/arogenate dehydrogenase family.
Belongs to the protein prenyltransferase subunit alpha family.
Belongs to the helicase family. RAD25/XPB subfamily.
Belongs to the dTDP-4-dehydrorhamnose reductase family. MAT2B subfamily.
Probably involved in the biogenesis of the COX complex.
Belongs to the aconitase/IPM isomerase family.
Catalyzes the reversible hydration of cis-homoaconitate to (2R,3S)-homoisocitrate, a step in the alpha-aminoadipate pathway for lysine biosynthesis.
Belongs to the OMP decarboxylase family.
GTPase-activating protein for the ADP ribosylation factor family.
Belongs to the ubiA prenyltransferase family.
Converts protoheme IX and farnesyl diphosphate to heme O.
Belongs to the PI3/PI4-kinase family. Type III PI4K subfamily.
Belongs to the carbohydrate esterase 1 (CE1) family.
Esterase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.
Belongs to the alpha-ketoglutarate dehydrogenase family.
Belongs to the ribulose-phosphate 3-epimerase family.
Binds 1 divalent metal cation per subunit.
Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.
Belongs to the proteasome subunit S1 family.
Belongs to the fungal cytochrome c oxidase subunit 7a family.
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation.
Belongs to the adaptor complexes medium subunit family. Delta-COP subfamily.
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The glutaminase domain produces the ammonia necessary for the cyclase domain to produce IGP and AICAR from PRFAR. The ammonia is channeled to the active site of the cyclase domain.
In the C-terminal section; belongs to the HisA/HisF family.
Belongs to the 2-oxoacid dehydrogenase family.
Secreted metalloproteinase that allows assimilation of proteinaceous substrates. Shows high activities on basic nuclear substrates such as histone and protamine.
Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
Component of the small ribosomal subunit. Mature ribosomes consist of a small (40S) and a large (60S) subunit. The 40S subunit contains about 33 different proteins and 1 molecule of RNA (18S). The 60S subunit contains about 49 different proteins and 3 molecules of RNA (25S, 5.8S and 5S). Interacts with RPS21.
Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits.
Belongs to the DASH complex DAD1 family.
Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Belongs to the cation diffusion facilitator (CDF) transporter (TC 2.A.4) family. SLC30A subfamily.
Belongs to the MoaE family. MOCS2B subfamily.
Catalytic subunit of the molybdopterin synthase complex, a complex that catalyzes the conversion of precursor Z into molybdopterin. Acts by mediating the incorporation of 2 sulfur atoms from thiocarboxylated MOCS2A into precursor Z to generate a dithiolene group.
Belongs to the glycosyl hydrolase 63 family.
Cleaves the distal alpha 1,2-linked glucose residue from the Glc(3)Man(9)GlcNAc(2) oligosaccharide precursor.
Type IV dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.
Belongs to the selenium-binding protein family.
Belongs to the acetyltransferase family. MAK3 subfamily.
May be involved in a process influencing telomere capping.
Has a role in the initiation of DNA replication. Required at S-phase checkpoint.
Belongs to the metallophosphoesterase superfamily. Purple acid phosphatase family.
Belongs to the carnitine/choline acetyltransferase family.
Binds ubiquitin and polyubiquitinated proteins.
Probable aspartic protease. May be involved in the regulation of exocytosis. Acts as a linker between the 19S proteasome and polyubiquitinated proteins via UBA domain interactions with ubiquitin for their subsequent degradation. Required for S-phase checkpoint control.
Belongs to the bacterial ribosomal protein bS21 family.
Belongs to the eukaryotic ribosomal protein eL34 family.
Belongs to the eukaryotic ribosomal protein eS7 family.
Belongs to the STXBP/unc-18/SEC1 family.
Belongs to the major facilitator superfamily. TCR/Tet family.
Efflux pump; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C (PubMed:22652150). Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production (By similarity). The other FUS cluster members are not essential for fusarin C biosynthesis (By similarity).
Does not alter fusaric acid production (PubMed:25372119).
Oxidase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties (PubMed:25372119). L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L-homoserine by cluster enzymes aspartate kinase FUB3 and homoserine O-acetyltransferase FUB5, as well as enzymes of the primary metabolism (By similarity). The polyketide synthase (PKS) FUB1 generates the triketide trans-2-hexenal which is presumptively released by the hydrolase FUB4 and linked to the NRPS-bound amino acid precursor by NAD(P)-dependent dehydrogenase FUB6 (By similarity). FUB1, FUB4, and the non-canonical NRPS Fub8 may form an enzyme complex (By similarity). Further processing of the NRPS-bound intermediate might be carried out by FUB6 and the sulfhydrylase FUB7, enabling a spontaneous electrocyclization to close the carbon backbone of fusaric acid (By similarity). Dihydrofusaric acid is likely to be released via reduction by the thioester reductase (TR) domain of FUB8 whereupon the final oxidation to fusaric acid may (also) be performed by the FMN-dependent dehydrogenase FUB9 (By similarity).
Has aminopeptidase activity, shortening substrate peptides sequentially by 1 amino acid. Has bleomycin hydrolase activity, which can protect the cell from the toxic effects of bleomycin. Has homocysteine-thiolactonase activity, protecting the cell against homocysteine toxicity.
Homohexamer. Binds to nucleic acids. Binds single-stranded DNA and RNA with higher affinity than double-stranded DNA.
The normal physiological role of the enzyme is unknown, but it is not essential for the viability of yeast cells. Has aminopeptidase activity, shortening substrate peptides sequentially by 1 amino acid. Has bleomycin hydrolase activity, which can protect the cell from the toxic effects of bleomycin. Has homocysteine-thiolactonase activity, protecting the cell against homocysteine toxicity. Acts as a repressor in the GAL4 regulatory system, but this does not require either the peptidase or nucleic acid-binding activities.
Belongs to the fluoride exporter Fluc/FEX family.
Fluoride channel required for the rapid expulsion of cytoplasmic fluoride.
Histone methyltransferase that trimethylates histone H3 'Lys-36' forming H3K36me3. Involved in transcription elongation as well as in transcription repression.
In eukaryotes there are cytoplasmic, mitochondrial and chloroplastic isozymes.
Histone methyltransferase that trimethylates 'Lys-20' of histone H4 to form H4K20me3.
Belongs to the adenylate kinase family. UMP-CMP kinase subfamily.
Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and dUMP as phosphate acceptors, but can also use CMP, dCMP and AMP.
Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
In the C-terminal section; belongs to the peptidase M41 family.
In the N-terminal section; belongs to the AAA ATPase family.
Expression is induced in response to 2-benzoxazolinone (BOA) exposure.
Transmembrane transporter; part of the Fusarium detoxification of benzoxazolinone cluster 2 (FDB2) involved in the degradation of benzoxazolinones produced by the host plant (PubMed:26808652). Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their inherent instability once released, spontaneously degrade to the more stable corresponding benzoxazolinones, 6-methoxy-2-benzoxazolinone (MBOA) and 2-benzoxazolinone (BOA), respectively (PubMed:11876429). Might be involved in the transport of metabolites of benzoxazolinone degradation (Probable).
In the C-terminal section; belongs to the phytoene/squalene synthase family.
In the N-terminal section; belongs to the lycopene beta-cyclase family.
Associates with 90S and pre-40S pre-ribosomal particles.
Component of the 90S pre-ribosome involved in the maturation of rRNAs. Required for early cleavages of the pre-RNAs in the 40S ribosomal subunit maturation pathway.
Belongs to the actin family. ARP6 subfamily.
E3 RING-finger protein, member of the UBC2/RAD6 epistasis group. Associates to the E2 ubiquitin conjugating enzyme UBC2/RAD6 to form the UBC2-RAD18 ubiquitin ligase complex involved in postreplicative repair (PRR) of damaged DNA.
Interacts with E2 UBC2, forming a complex with ubiquitin ligase activity.
Belongs to the universal ribosomal protein uS4 family.
Catalyzes the dephosphorylation of the nucleoside 5'-monophosphates deoxyadenosine monophosphate (dAMP), deoxycytidine monophosphate (dCMP), deoxyguanosine monophosphate (dGMP) and deoxythymidine monophosphate (dTMP).
Belongs to the eukaryotic ribosomal protein eS19 family.
Belongs to the DHHC palmitoyltransferase family.
Regulator of type 1 phosphatases which maintains protein phosphatase activity under strict control.
Belongs to the glycosyl hydrolase 27 family.
Belongs to the NtaA/SnaA/DszA monooxygenase family.
Belongs to the glycosyl hydrolase 12 (cellulase H) family.
Belongs to the V-ATPase proteolipid subunit family.
Proton-conducting pore forming of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments.
V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'', d, e, f and VOA1). The decameric c-ring forms the proton-conducting pore, and is composed of eight proteolipid subunits c, one subunit c' and one subunit c''.
Belongs to the PA-phosphatase related phosphoesterase family.
Belongs to the intradiol ring-cleavage dioxygenase family.
Belongs to the radical SAM superfamily. Biotin synthase family.
Belongs to the phosphoenolpyruvate carboxykinase (ATP) family.
Belongs to the SMC family. SMC5 subfamily.
Belongs to the ubiquitin-activating E1 family.
Belongs to the DNA photolyase class-1 family.
Belongs to the glycosyltransferase 20 family.
Belongs to the UDP-glucose/GDP-mannose dehydrogenase family.
Belongs to the polyadenylate-binding protein type-1 family.
Binds the poly(A) tail of mRNA. Appears to be an important mediator of the multiple roles of the poly(A) tail in mRNA biogenesis, stability and translation. In the nucleus, involved in both mRNA cleavage and polyadenylation. Is also required for efficient mRNA export to the cytoplasm. Acts in concert with a poly(A)-specific nuclease (PAN) to affect poly(A) tail shortening, which may occur concomitantly with either nucleocytoplasmic mRNA transport or translational initiation. In the cytoplasm, stimulates translation initiation and regulates mRNA decay through translation termination-coupled poly(A) shortening, probably mediated by PAN.
Belongs to the mitochondrial pyruvate carrier (MPC) (TC 2.A.105) family.
Mediates the uptake of pyruvate into mitochondria.
Catalyzes the exchange of ADP and ATP across the membrane.
Belongs to the universal ribosomal protein uL16 family.
Belongs to the eukaryotic ribosomal protein eL29 family.
Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.
In the cytoplasm, catalyzes the conversion of glucose-6-phosphate to fructose-6-phosphate, the second step in glycolysis, and the reverse reaction during gluconeogenesis.
Belongs to the glycosyl hydrolase 1 family.
Belongs to the neutral ceramidase family.
Component of the GPI transamidase complex. May be involved in the recognition of either the GPI attachment signal or the lipid portion of GPI.
Belongs to the class-I DAHP synthase family.
Belongs to the dihydrofolate reductase family.
Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.
Belongs to the universal ribosomal protein uS17 family.
Belongs to the class I-like SAM-binding methyltransferase superfamily. MenG/UbiE family.
Methyltransferase required for the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).
Belongs to the SAICAR synthetase family.
Belongs to the PDK/BCKDK protein kinase family.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IV subfamily.
Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during the synthesis of uridine diphosphate/UDP-GlcNAc, which is a biosynthetic precursor of chitin and also supplies the amino sugars for N-linked oligosaccharides of glycoproteins.
Belongs to the eukaryotic ribosomal protein eS17 family.
Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication.
Component of the origin recognition complex (ORC).
Transcription factor; part of the Fusarium detoxification of benzoxazolinone cluster 1 (FDB1) involved in the degradation of benzoxazolinones produced by the host plant (PubMed:26808652). Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their inherent instability once released, spontaneously degrade to the more stable corresponding benzoxazolinones, 6-methoxy-2-benzoxazolinone (MBOA) and 2-benzoxazolinone (BOA), respectively (PubMed:11876429). Might be involved in the regulation of the expression of the FDB1 cluster genes (Probable).
Belongs to the DASH complex SPC19 family.
Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins.
Heterohexamer of two PFD-alpha type and four PFD-beta type subunits.
Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits.
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs.
Involved in cell wall synthesis where it is required for glycosylation. Involved in cell cycle progression through cell-size checkpoint.
In the C-terminal section; belongs to the Cu-Zn superoxide dismutase family.
Belongs to the metallo-dependent hydrolases superfamily. Adenosine and AMP deaminases family.
Belongs to the Mediator complex subunit 1 family.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family.
Catalyzes the hydrolysis of ATP coupled with the transport of calcium.
Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN).
Component of the Golgi-associated retrograde protein (GARP) complex.
The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel.
Belongs to the endopolyphosphatase PPN1 family.
Catalyzes the hydrolysis of inorganic polyphosphate (polyP) chains of many hundreds of phosphate residues into shorter lengths.
Belongs to the peptidase C69 family. Secernin subfamily.
Acts in DNA repair and mutagenesis. Involved in promoting resistance to ionizing radiation and UV light, as well as regulating cell cycle progression after irradiation.
Plays an essential role in initiation of the G0 program by preventing the degradation of specific nutrient-regulated mRNAs via the 5'-3' mRNA decay pathway.
Trifunctional enzyme bearing the Gln amidotransferase (GATase) domain of anthranilate synthase, indole-glycerolphosphate synthase, and phosphoribosylanthranilate isomerase activities.
Involved in the catabolism of quinolinic acid (QA).
FAD-dependent monooxygenase; part of the Fusarium detoxification of benzoxazolinone cluster 2 (FDB2) involved in the degradation of benzoxazolinones produced by the host plant (PubMed:19302487, PubMed:26808652). Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their inherent instability once released, spontaneously degrade to the more stable corresponding benzoxazolinones, 6-methoxy-2-benzoxazolinone (MBOA) and 2-benzoxazolinone (BOA), respectively (PubMed:11876429). The first step in the detoxification of benzoxazolinones involves the hydrolysis of the cyclic ester bond of benzoxazolinones by the FDB1 cluster gamma-lactamase MBL1 to aminophenols (PubMed:26808652, PubMed:12788712). MBL1 is able to convert BOA into 2-aminophenol (2-AP), as well as MBOA into 5-methoxy-2-aminophenol (2-AMP) (PubMed:26808652, PubMed:12788712). The FDB2 cluster N-malonyltransferase FDB2/NAT1 then metabolizes aminophenols via N-malonylation to non-toxic malonamic acids (PubMed:19302487, PubMed:12788712). FDB2/NAT1 converts 2-AP into N-(2-hydroxyphenyl) malonamic acid (HPMA) and 2-AMP into N-(2-hydroxy-4-methoxyphenyl) malonamic acid (HMPMA) (PubMed:19302487, PubMed:12788712). The duplicated dienlactone hydrolases DLH1 and DLH2 may provide redundant function for hydrolyzing the lactone moiety in the BOA molecule (Probable). The roles of the amidases an other enzymes encoded by the 2 FDB clusters have not been identified so far (Probable).
Belongs to the eukaryotic ribosomal protein P1/P2 family.
P1 and P2 exist as dimers at the large ribosomal subunit.
Belongs to the eukaryotic RPB4 RNA polymerase subunit family.
Belongs to the CND2 (condensin subunit 2) family.
Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes.
Belongs to the nucleobase:cation symporter-2 (NCS2) (TC 2.A.40) family.
Expression is controlled by the global regulators for secondary metabolite VE1 and LAE1 (PubMed:19382792, PubMed:22713715). Expression is increased under histone deacetylase (HDAC)-inhibiting conditions (PubMed:22117026).
Impairs the production of fumonisins (PubMed:17483290).
Transcription factor that regulates the expression the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), and B4 (FB4), which are carcinogenic mycotoxins (PubMed:17483290).
Belongs to the universal ribosomal protein uS7 family.
Phospholipid scramblase involved in autophagy. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion.
Functions as a nucleotide exchange factor (NEF) for Hsp70 chaperones which accelerates the release of ADP. Required for fully efficient Hsp70-mediated folding of proteins.
Mediates inactivation of the TORC1 complex in response to amino acid starvation. Required for meiotic nuclear division.
Belongs to the GTP-binding elongation factor family. LepA subfamily.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. LepA subfamily.
Promotes mitochondrial protein synthesis. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Binds to mitochondrial ribosomes in a GTP-dependent manner.
Belongs to the UbiD family. UbiD-like/FDC subfamily.
Binds 1 prenylated FMN (prenyl-FMN) per subunit.
Catalyzes the reversible decarboxylation of aromatic carboxylic acids like ferulic acid, p-coumaric acid or cinnamic acid, producing the corresponding vinyl derivatives 4-vinylphenol, 4-vinylguaiacol, and styrene, respectively, which play the role of aroma metabolites.
Homodimer. May form higher order oligomers.
Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Belongs to the eukaryotic ribosomal protein eL30 family.
Belongs to the polysaccharide monooxygenase AA13 family.
Belongs to the TFIIE beta subunit family.
Recruits TFIIH to the initiation complex and stimulates the RNA polymerase II C-terminal domain kinase and DNA-dependent ATPase activities of TFIIH. Both TFIIH and TFIIE are required for promoter clearance by RNA polymerase.
Tetramer of two alpha and two beta chains.
Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.
Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates.
Belongs to the replication factor A protein 2 family.
Belongs to the membrane-bound acyltransferase family. Sterol o-acyltransferase subfamily.
Sterol O-acyltransferase that catalyzes the formation of stery esters.
Belongs to the adenylyl cyclase class-3 family.
Plays essential roles in regulation of cellular metabolism by catalyzing the synthesis of a second messenger, cAMP.
Belongs to the HIBADH-related family. 3-hydroxyisobutyrate dehydrogenase subfamily.
Belongs to the type II topoisomerase family.
Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks.
Belongs to the glycosyl hydrolase 11 (cellulase G) family.
Belongs to the WD repeat peroxin-7 family.
S-adenosyl-L-methionine-dependent transferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the transfer of the alpha-amino-alpha-carboxypropyl (acp) group from S-adenosyl-L-methionine to the C-7 position of 4-demethylwyosine (imG-14) to produce wybutosine-86.
Mediator of sterol homeostasis involved in sterol uptake, trafficking and distribution into membranes.
Regulates also the sphingolipid metabolism.
Belongs to the metallo-dependent hydrolases superfamily.
This enzyme is required for electron transfer from NADP to cytochrome P450.
Belongs to the pseudouridine synthase TruD family.
Guanine nucleotide-exchange factor (GEF) required for the formation or budding of transport vesicles from the ER.
Belongs to the ferroportin (FP) (TC 2.A.100) family. SLC40A subfamily.
May be involved in iron transport and iron homeostasis.
Belongs to the alpha-IPM synthase/homocitrate synthase family. Homocitrate synthase LYS20/LYS21 subfamily.
Catalyzes the aldol-type condensation of 2-oxoglutarate with acetyl-CoA to yield homocitrate. Carries out the first step of the alpha-aminoadipate (AAA) lysine biosynthesis pathway.
Belongs to the class-II aminoacyl-tRNA synthetase family.
Belongs to the copper transporter (Ctr) (TC 1.A.56) family. SLC31A subfamily.
Belongs to the eukaryotic RPB8 RNA polymerase subunit family.
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively.
Belongs to the glycosyl hydrolase 20 family.
Belongs to the threonine synthase family.
Binds 2 magnesium ions. Also active with manganese.
Polymerase that creates the 3'-poly(A) tail of mRNA's.
Belongs to the monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family.
Belongs to the SEC23/SEC24 family. SEC23 subfamily.
Belongs to the eIF-2B gamma/epsilon subunits family.
Belongs to the protein-tyrosine phosphatase family. Non-receptor class CDC14 subfamily.
Component of several multiprotein Golgi SNARE complexes.
Involved in transport from the ER to the Golgi apparatus as well as in intra-Golgi transport. It belongs to a super-family of proteins called t-SNAREs or soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptor.
ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the membrane-bound receptor, and returning it to the cytosol to initiate a new round of targeting.
Belongs to the Mediator complex subunit 11 family.
Belongs to the glycosyl hydrolase 75 family.
Chitosanase catalyzing the endo-type cleavage of chitosan, the deacylated form of chitin. Chitosanase may be crucial in the degradation of the deacetylated portion of chitin in the fungal cell wall.
Belongs to the dynactin 150 kDa subunit family.
Belongs to the VEFS (VRN2-EMF2-FIS2-SU(Z)12) family.
Belongs to the prenylcysteine oxidase family.
Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
Belongs to the DEAD box helicase family. DEAH subfamily. DDX11/CHL1 sub-subfamily.
Component of the PAN1 actin cytoskeleton-regulatory complex required for the internalization of endosomes during actin-coupled endocytosis. The complex links the site of endocytosis to the cell membrane-associated actin cytoskeleton. Mediates uptake of external molecules and vacuolar degradation of plasma membrane proteins. Plays a role in the proper organization of the cell membrane-associated actin cytoskeleton and promotes its destabilization.
Component of the PAN1 actin cytoskeleton-regulatory complex.
Binds specifically to the 3'-terminal U-tract of U6 snRNA.
Belongs to the velvet family. VelC subfamily.
Velvet-domain-containing protein that acts as a positive regulator of sexual development (By similarity). Dispensable for regulation of conidial size, hyphal hydrophobicity, fumonisin production, and oxidant resistance (PubMed:24792348).
ATPase component of the INO80 complex which remodels chromatin by shifting nucleosomes and is involved in DNA repair.
Component of the INO80 chromatin-remodeling complex.
The DBINO region is involved in binding to DNA.
Belongs to the HAD-like hydrolase superfamily. S-2-haloalkanoic acid dehalogenase family.
Belongs to the eukaryotic ribosomal protein eL8 family.
Required for the assembly of cytochrome c oxidase.
Exoribonuclease involved in ribosome biosynthesis. Involved in the processing of ITS1, the internal transcribed spacer localized between the 18S and 5.8S rRNAs.
Putative aldehyde dehydrogenase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C (PubMed:22652150). Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production (By similarity). The other FUS cluster members are not essential for fusarin C biosynthesis (By similarity).
Belongs to the eukaryotic ribosomal protein eL14 family.
Belongs to the bacterial ribosomal protein bL36 family.
The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
The glycine cleavage system is composed of four proteins: P, T, L and H.
Belongs to the RNA 3'-terminal cyclase family. Type 2 subfamily.
Second step of mRNA capping. Transfer of the GMP moiety of GTP to the 5'-end of RNA via an enzyme-GMP covalent reaction intermediate.
Highly specific D-xylulose kinase which participates in the catabolism of xylose. Xylose is a major component of hemicelluloses such as xylan. Most fungi utilize D-xylose via three enzymatic reactions, xylose reductase (XR), xylitol dehydrogenase (XDH), and xylulokinase, to form xylulose 5-phosphate, which enters pentose phosphate pathway.
In the 2nd section; belongs to the type-I 3-dehydroquinase family.
In the N-terminal section; belongs to the shikimate kinase family.
Involved in the 5-carboxymethylaminomethyl modification (mnm(5)s(2)U34) of the wobble uridine base in mitochondrial tRNAs.
Has a role in a nucleosome assembly pathway that is required for the integrity of heterochromatin and proper chromosome segregation.
Belongs to the asaB hydroxylase/desaturase family.
May associate with the eukaryotic translation initiation factor 3 (eIF-3) complex.
mRNA-binding protein involved in proper cytoplasmic distribution of mitochondria.
Neddylation of cullins play an essential role in the regulation of SCF-type complexes activity.
Belongs to the fungal hydrophobin family.
Ubiquitin-like protein involved in cytoplasm to vacuole transport (Cvt), autophagy vesicles formation, mitophagy, and nucleophagy.
Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN) coenzyme.
Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins.
Belongs to the eukaryotic ribosomal protein eS26 family.
Plays a role in maintaining the mitochondrial genome and in controlling the mtDNA escape. Involved in the regulation of mtDNA nucleotide structure and number. May have a dispensable role in early maturation of pre-rRNA.
Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains.
Component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes.
Essential component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins.
Belongs to the eukaryotic ribosomal protein eL28 family.
Belongs to the ALG6/ALG8 glucosyltransferase family.
Belongs to the nucleoporin NSP1/NUP62 family.
Belongs to the heat shock protein 90 family.
Belongs to the pseudouridine synthase TruB family.
Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX.
Catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols.
Belongs to the small GTPase superfamily. Arf family.
Belongs to the class I-like SAM-binding methyltransferase superfamily.
Produces fumonisins that lack one of the tricarballylic ester functions (PubMed:17147424).
Tricarboxylate transporter; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), and B4 (FB4), which are carcinogenic mycotoxins (PubMed:12620260, PubMed:17147424). On the basis of the chemical structures of fumonisins and precursor feeding studies, fumonisin biosynthesis is predicted to include at least five groups of biochemical reactions: synthesis of a linear polyketide with a single terminal carbonyl function and methyl groups at C-10 and C-14; condensation of the polyketide with alanine; reduction of the polyketide carbonyl to a hydroxyl; hydroxylation of 2-4 polyketide carbons; and esterification of six-carbon tricarboxylic acids to two of the hydroxyls (PubMed:12620260). The biosynthesis starts with the polyketide synthase FUM1-catalyzed carbon chain assembly from one molecule of acetyl CoA, eight molecules of malonyl CoA, and two molecules of methionine (PubMed:10413619). The C-18 polyketide chain is released from the enzyme by a nucleophilic attack of a carbanion, which is derived from R-carbon of alanine by decarboxylation, on the carbonyl carbon of polyketide acyl chain (PubMed:15137825, PubMed:12720383). This step is catalyzed by a pyridoxal 5'-phosphate-dependent aminoacyl transferase FUM8 (PubMed:15137825, PubMed:12720383). The resultant 3-keto intermediate 2-amino-3-oxo-12,16-dimethylicosane is then stereospecifically reduced to the 3-hydroxyl product 2-amino-3-hydroxy-12,16-dimethylicosane by reductase FUM13 (PubMed:12720383, PubMed:15137825). Subsequent oxidations at C-5, C-10, C-14 and C-15 followed by tricarballylic esterification of the hydroxyl groups on C-14 and C-15 furnish the biosynthesis of fumonisins (PubMed:15066782, PubMed:15137825, PubMed:16489749). The C-10 hydroxylation is performed by the cytochrome P450 monooxygenase FUM2 and occurs early in the biosynthesis (PubMed:16536629). The C-5 hydroxylation is performed by the dioxygenase FUM3 and occurs late in the biosynthesis (PubMed:20237561, PubMed:15066782, PubMed:15137825, PubMed:16536629). Cytochrome P450 monooxygenases FUM6 and FUM15 may be responsible for the two remaining hydroxylations at positions C-14 and C-15 (PubMed:12620260). The FUM11 tricarboxylate transporter makes a tricarboxylic acid precursor available for fumonisin biosynthesis via its export from the mitochondria (PubMed:12620260). If the precursor is citrate, the FUM7 dehydrogenase could remove the C-3 hydroxyl of citrate to form tricarballylic acid either before or after the CoA activation by the FUM10 acyl-CoA synthetase and FUM14 catalyzed esterification of CoA-activated tricarballylic acid to the C-14 and C-15 hydroxyls of the fumonisin backbone (PubMed:16489749, PubMed:17147424). Alternatively, if the precursor is cis-aconitate, FUM7 may function to reduce the double bond (PubMed:17147424). In this alternate proposal, feeding studies with tetradehydro-fumonisin B1 suggests that FUM7 cannot function on the tricarballylic ester and must therefore act before the FUM14-mediated esterification (PubMed:17147424).
Component of the ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme composed of 3 respiratory subunits cytochrome b, cytochrome c1 and Rieske protein, 2 core protein subunits, and additional low-molecular weight protein subunits.
Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Belongs to the archaeal Rpo11/eukaryotic RPB11/RPC19 RNA polymerase subunit family.
Belongs to the proteasome subunit p55 family.
Belongs to the carotenoid oxygenase family.
Belongs to the adaptor complexes small subunit family.
Component of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration.
Acyl-CoA transferase; part of the Fusarium detoxification of benzoxazolinone cluster 2 (FDB2) involved in the degradation of benzoxazolinones produced by the host plant (PubMed:19302487, PubMed:26808652). Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their inherent instability once released, spontaneously degrade to the more stable corresponding benzoxazolinones, 6-methoxy-2-benzoxazolinone (MBOA) and 2-benzoxazolinone (BOA), respectively (PubMed:11876429). The first step in the detoxification of benzoxazolinones involves the hydrolysis of the cyclic ester bond of benzoxazolinones by the FDB1 cluster gamma-lactamase MBL1 to aminophenols (PubMed:26808652, PubMed:12788712). MBL1 is able to convert BOA into 2-aminophenol (2-AP), as well as MBOA into 5-methoxy-2-aminophenol (2-AMP) (PubMed:26808652, PubMed:12788712). The FDB2 cluster N-malonyltransferase FDB2/NAT1 then metabolizes aminophenols via N-malonylation to non-toxic malonamic acids (PubMed:19302487, PubMed:12788712). FDB2/NAT1 converts 2-AP into N-(2-hydroxyphenyl) malonamic acid (HPMA) and 2-AMP into N-(2-hydroxy-4-methoxyphenyl) malonamic acid (HMPMA) (PubMed:19302487, PubMed:12788712). The duplicated dienlactone hydrolases DLH1 and DLH2 may provide redundant function for hydrolyzing the lactone moiety in the BOA molecule (Probable). The roles of the amidases an other enzymes encoded by the 2 FDB clusters have not been identified so far (Probable).
Belongs to the complex I NDUFA5 subunit family.
Belongs to the DODA-type extradiol aromatic ring-opening dioxygenase family.
Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing.
Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway.
Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner.
Belongs to the MsrA Met sulfoxide reductase family.
Ribosomal protein P0 is the functional equivalent of E.coli protein L10.
N-acetylglucosaminyltransferase involved in the Golgi-specific modification of N-linked glycans.
Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.
Homotetramer. Residues from neighboring subunits contribute catalytic and substrate-binding residues to each active site.
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.
Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane.
Component of the mitochondrial contact site and cristae organizing system (MICOS) complex.
Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.
Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade "E" sub-subfamily.
Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade 'E' sub-subfamily.
Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Belongs to the class II fructose-bisphosphate aldolase family.
Binds 2 Zn(2+) ions per subunit. One is catalytic and the other provides a structural contribution.
Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis.
Belongs to the eukaryotic RPC7 RNA polymerase subunit family.
Component of the RNA polymerase III (Pol III) complex.
Belongs to the MsrB Met sulfoxide reductase family.
Belongs to the GHMP kinase family. Mevalonate kinase subfamily.
Belongs to the cyclic nucleotide phosphodiesterase family.
Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions.
Belongs to the fungal Na(+)/H(+) exchanger family.
Belongs to the U2 small nuclear ribonucleoprotein A family.
Belongs to the eukaryotic ribosomal protein eS30 family.
In the N-terminal section; belongs to the cytochrome P450 family.
Sphingosine N-acyltransferase-like protein; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), and B4 (FB4), which are carcinogenic mycotoxins (PubMed:12620260). On the basis of the chemical structures of fumonisins and precursor feeding studies, fumonisin biosynthesis is predicted to include at least five groups of biochemical reactions: synthesis of a linear polyketide with a single terminal carbonyl function and methyl groups at C-10 and C-14; condensation of the polyketide with alanine; reduction of the polyketide carbonyl to a hydroxyl; hydroxylation of 2-4 polyketide carbons; and esterification of six-carbon tricarboxylic acids to two of the hydroxyls (PubMed:12620260). The biosynthesis starts with the polyketide synthase FUM1-catalyzed carbon chain assembly from one molecule of acetyl CoA, eight molecules of malonyl CoA, and two molecules of methionine (PubMed:10413619). The C-18 polyketide chain is released from the enzyme by a nucleophilic attack of a carbanion, which is derived from R-carbon of alanine by decarboxylation, on the carbonyl carbon of polyketide acyl chain (PubMed:15137825, PubMed:12720383). This step is catalyzed by a pyridoxal 5'-phosphate-dependent aminoacyl transferase FUM8 (PubMed:15137825, PubMed:12720383). The resultant 3-keto intermediate 2-amino-3-oxo-12,16-dimethylicosane is then stereospecifically reduced to the 3-hydroxyl product 2-amino-3-hydroxy-12,16-dimethylicosane by reductase FUM13 (PubMed:12720383, PubMed:15137825). Subsequent oxidations at C-5, C-10, C-14 and C-15 followed by tricarballylic esterification of the hydroxyl groups on C-14 and C-15 furnish the biosynthesis of fumonisins (PubMed:15066782, PubMed:15137825, PubMed:16489749). The C-10 hydroxylation is performed by the cytochrome P450 monooxygenase FUM2 and occurs early in the biosynthesis (PubMed:16536629). The C-5 hydroxylation is performed by the dioxygenase FUM3 and occurs late in the biosynthesis (PubMed:20237561, PubMed:15066782, PubMed:15137825, PubMed:16536629). Cytochrome P450 monooxygenases FUM6 and FUM15 may be responsible for the two remaining hydroxylations at positions C-14 and C-15 (PubMed:12620260). The FUM11 tricarboxylate transporter makes a tricarboxylic acid precursor available for fumonisin biosynthesis via its export from the mitochondria (PubMed:12620260). If the precursor is citrate, the FUM7 dehydrogenase could remove the C-3 hydroxyl of citrate to form tricarballylic acid either before or after the CoA activation by the FUM10 acyl-CoA synthetase and FUM14 catalyzed esterification of CoA-activated tricarballylic acid to the C-14 and C-15 hydroxyls of the fumonisin backbone (PubMed:16489749, PubMed:17147424). Alternatively, if the precursor is cis-aconitate, FUM7 may function to reduce the double bond (PubMed:17147424). In this alternate proposal, feeding studies with tetradehydro-fumonisin B1 suggests that FUM7 cannot function on the tricarballylic ester and must therefore act before the FUM14-mediated esterification (PubMed:17147424). FUM18 is not required for production of fumonosins but may have an indirect role such as self-protection (PubMed:12620260).
Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily.
Belongs to the lysine N-acyltransferase MbtK family.
Required for 3'-end cleavage and polyadenylation of pre-mRNAs.
Catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity.
Divalent metal cations. Prefers magnesium or manganese.
Belongs to the DASH complex ASK1 family.
Belongs to the GST superfamily. Zeta family.
Belongs to the cysteine synthase/cystathionine beta-synthase family.
E1-like activating enzyme involved in the 2 ubiquitin-like systems required for cytoplasm to vacuole transport (Cvt) and autophagy. Activates ATG12 for its conjugation with ATG5 and ATG8 for its conjugation with phosphatidylethanolamine. Both systems are needed for the ATG8 association to Cvt vesicles and autophagosomes membranes. Autophagy is essential for maintenance of amino acid levels and protein synthesis under nitrogen starvation. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production.
Belongs to the U1 small nuclear ribonucleoprotein C family.
Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. U1-C is directly involved in initial 5' splice-site recognition for both constitutive and regulated alternative splicing. The interaction with the 5' splice-site seems to precede base-pairing between the pre-mRNA and the U1 snRNA. Stimulates commitment or early (E) complex formation by stabilizing the base pairing of the 5' end of the U1 snRNA and the 5' splice-site region.
U1 snRNP is composed of the 7 core Sm proteins B/B', D1, D2, D3, E, F and G that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP, and at least 3 U1 snRNP-specific proteins U1-70K, U1-A and U1-C. U1-C interacts with U1 snRNA and the 5' splice-site region of the pre-mRNA.
Belongs to the sterol desaturase family. SCS7 subfamily.
Binds 2 Zn(2+) ions per subunit that likely form a catalytic dimetal center.
Ceramide hydroxylase involved in the hydroxylation of sphingolipid-associated very long chain fatty acids. Postulated to hydroxylate the very long chain fatty acid of dihydroceramides and phytoceramides at C-2.
ATP-independent protease that degrades mitochondrial transit peptides after their cleavage. Also degrades other unstructured peptides.
Belongs to the peptidase M16 family. PreP subfamily.
Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), and B4 (FB4), which are carcinogenic mycotoxins (PubMed:12620260). On the basis of the chemical structures of fumonisins and precursor feeding studies, fumonisin biosynthesis is predicted to include at least five groups of biochemical reactions: synthesis of a linear polyketide with a single terminal carbonyl function and methyl groups at C-10 and C-14; condensation of the polyketide with alanine; reduction of the polyketide carbonyl to a hydroxyl; hydroxylation of 2-4 polyketide carbons; and esterification of six-carbon tricarboxylic acids to two of the hydroxyls (PubMed:12620260). The biosynthesis starts with the polyketide synthase FUM1-catalyzed carbon chain assembly from one molecule of acetyl CoA, eight molecules of malonyl CoA, and two molecules of methionine (PubMed:10413619). The C-18 polyketide chain is released from the enzyme by a nucleophilic attack of a carbanion, which is derived from R-carbon of alanine by decarboxylation, on the carbonyl carbon of polyketide acyl chain (PubMed:15137825, PubMed:12720383). This step is catalyzed by a pyridoxal 5'-phosphate-dependent aminoacyl transferase FUM8 (PubMed:15137825, PubMed:12720383). The resultant 3-keto intermediate 2-amino-3-oxo-12,16-dimethylicosane is then stereospecifically reduced to the 3-hydroxyl product 2-amino-3-hydroxy-12,16-dimethylicosane by reductase FUM13 (PubMed:12720383, PubMed:15137825). Subsequent oxidations at C-5, C-10, C-14 and C-15 followed by tricarballylic esterification of the hydroxyl groups on C-14 and C-15 furnish the biosynthesis of fumonisins (PubMed:15066782, PubMed:15137825, PubMed:16489749). The C-10 hydroxylation is performed by the cytochrome P450 monooxygenase FUM2 and occurs early in the biosynthesis (PubMed:16536629). The C-5 hydroxylation is performed by the dioxygenase FUM3 and occurs late in the biosynthesis (PubMed:20237561, PubMed:15066782, PubMed:15137825, PubMed:16536629). Cytochrome P450 monooxygenases FUM6 and FUM15 may be responsible for the two remaining hydroxylations at positions C-14 and C-15 (PubMed:12620260). The FUM11 tricarboxylate transporter makes a tricarboxylic acid precursor available for fumonisin biosynthesis via its export from the mitochondria (PubMed:12620260). If the precursor is citrate, the FUM7 dehydrogenase could remove the C-3 hydroxyl of citrate to form tricarballylic acid either before or after the CoA activation by the FUM10 acyl-CoA synthetase and FUM14 catalyzed esterification of CoA-activated tricarballylic acid to the C-14 and C-15 hydroxyls of the fumonisin backbone (PubMed:16489749, PubMed:17147424). Alternatively, if the precursor is cis-aconitate, FUM7 may function to reduce the double bond (PubMed:17147424). In this alternate proposal, feeding studies with tetradehydro-fumonisin B1 suggests that FUM7 cannot function on the tricarballylic ester and must therefore act before the FUM14-mediated esterification (PubMed:17147424).
Required for nuclear membrane fusion during karyogamy.
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Belongs to the GatB/GatE family. GatB subfamily.
Subunit of the heterotrimeric GatCAB amidotransferase (AdT) complex, composed of A, B and C subunits.
Belongs to the complex I 20 kDa subunit family.
Belongs to the 40S cdc5-associated complex (or cwf complex), a spliceosome sub-complex reminiscent of a late-stage spliceosome.
Involved in mRNA splicing where it associates with cdc5 and the other cwf proteins as part of the spliceosome.
Involved in the initiation of assembly of the COPII coat required for the formation of transport vesicles from the endoplasmic reticulum (ER) and the selection of cargo molecules. Also involved in autophagy.
DNA polymerase II participates in chromosomal DNA replication.
Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Acts in association with DOCK1 and CRK. Was initially proposed to be required in complex with DOCK1 to activate Rac Rho small GTPases. May enhance the guanine nucleotide exchange factor (GEF) activity of DOCK1.
Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 2 subfamily.
Common component of the spliceosome and rRNA processing machinery.
Small GTPase required for proper nuclear import of RNA polymerase II (RNAPII). May act at an RNAP assembly step prior to nuclear import.
Catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second.
Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second.
Octamer of two non-identical subunits IDH1 and IDH2.
Belongs to the eukaryotic ribosomal protein eS8 family. Ribosome biogenesis protein NSA2 subfamily.
Component of the pre-66S ribosomal particle. Interacts with NOP7 and RRP1. Interacts with RSA4 (via WD repeats).
Involved in the biogenesis of the 60S ribosomal subunit. May play a part in the quality control of pre-60S particles.
Belongs to the ribose 5-phosphate isomerase family.
Belongs to the peroxiredoxin family. Prx6 subfamily.
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively.
Functions in both vacuole inheritance and protein targeting from the cytoplasm to vacuole.
Belongs to the PIGG/PIGN/PIGO family. PIGO subfamily.
Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.
Belongs to the pyridoxine kinase family.
Belongs to the nucleoporin Nup84/Nup107 family.
Functions as a component of the nuclear pore complex (NPC).
The GINS complex plays an essential role in the initiation of DNA replication.
Component of 250-400 kDa complexes called cytochrome oxidase assembly intermediates or COA complexes.
Required for assembly of cytochrome c oxidase (complex IV).
Belongs to the mitochondrion-specific ribosomal protein mL49 family.
Ubiquitin ligase protein which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation.
Belongs to the complex I 51 kDa subunit family.
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
Belongs to the eukaryotic/archaeal RNase P protein component 1 family.
Dienlactone hydrolase; part of the Fusarium detoxification of benzoxazolinone cluster 2 (FDB2) involved in the degradation of benzoxazolinones produced by the host plant (PubMed:19302487, PubMed:26808652). Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their inherent instability once released, spontaneously degrade to the more stable corresponding benzoxazolinones, 6-methoxy-2-benzoxazolinone (MBOA) and 2-benzoxazolinone (BOA), respectively (PubMed:11876429). The first step in the detoxification of benzoxazolinones involves the hydrolysis of the cyclic ester bond of benzoxazolinones by the FDB1 cluster gamma-lactamase MBL1 to aminophenols (PubMed:26808652, PubMed:12788712). MBL1 is able to convert BOA into 2-aminophenol (2-AP), as well as MBOA into 5-methoxy-2-aminophenol (2-AMP) (PubMed:26808652, PubMed:12788712). The FDB2 cluster N-malonyltransferase FDB2/NAT1 then metabolizes aminophenols via N-malonylation to non-toxic malonamic acids (PubMed:19302487, PubMed:12788712). FDB2/NAT1 converts 2-AP into N-(2-hydroxyphenyl) malonamic acid (HPMA) and 2-AMP into N-(2-hydroxy-4-methoxyphenyl) malonamic acid (HMPMA) (PubMed:19302487, PubMed:12788712). The duplicated dienlactone hydrolases DLH1 and DLH2 may provide redundant function for hydrolyzing the lactone moiety in the BOA molecule (Probable). The roles of the amidases and other enzymes encoded by the 2 FDB clusters have not been identified so far (Probable).
Belongs to the aspartate/glutamate racemases family.
Belongs to the major facilitator superfamily. Monocarboxylate porter (TC 2.A.1.13) family.
MFS-type transporter; part of the Fusarium detoxification of benzoxazolinone cluster 2 (FDB2) involved in the degradation of benzoxazolinones produced by the host plant (PubMed:26808652). Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their inherent instability once released, spontaneously degrade to the more stable corresponding benzoxazolinones, 6-methoxy-2-benzoxazolinone (MBOA) and 2-benzoxazolinone (BOA), respectively (PubMed:11876429).
Belongs to the mandelate racemase/muconate lactonizing enzyme family. GlucD subfamily.
Belongs to the complex I 24 kDa subunit family.
Belongs to the universal ribosomal protein uL23 family.
Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Functions as a sorting receptor in the Golgi compartment required for the intracellular sorting and delivery of soluble vacuolar proteins, like carboxypeptidase Y (CPY) and proteinase A. Executes multiple rounds of sorting by cycling between the late Golgi and a prevacuolar endosome-like compartment.
Belongs to the mitochondrion-specific ribosomal protein mL43 family.
Belongs to the reverse transcriptase family. Telomerase subfamily.
Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. It elongates telomeres. It is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme.
Belongs to the nucleoporin Nup133 family.
Belongs to the DASH complex SPC34 family.
Belongs to the GTR/RAG GTP-binding protein family.
GTPase involved in activation of the TORC1 signaling pathway, which promotes growth and represses autophagy in nutrient-rich conditions.
Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA (By similarity). The NAD-cap is present at the 5'-end of some RNAs and snoRNAs. In contrast to the canonical 5'-end N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay (By similarity). Also acts as a non-canonical decapping enzyme that removes the entire cap structure of m7G capped or incompletely capped RNAs (By similarity). Has decapping activity toward incomplete 5'-end m7G cap mRNAs such as unmethylated 5'-end-capped RNA (cap0), while it has no activity toward 2'-O-ribose methylated m7G cap (cap1).
Involved in amino sugar synthesis (formation of chitin, supplies the amino sugars of asparagine-linked oligosaccharides of glycoproteins).
Belongs to the eukaryotic ribosomal protein eL15 family.
Belongs to the heat shock protein 70 family.
Belongs to the clathrin light chain family.
Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of coenzyme Q (CoQ) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate.
Belongs to the eukaryotic ribosomal protein eS4 family.
Belongs to the queuine tRNA-ribosyltransferase family.
Catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming queuine, allowing a nucleophilic attack on the C1' of the ribose to form the product.
Heterodimer of a catalytic subunit and an accessory subunit.
Belongs to the velvet family. VelB subfamily.
Component of the heterotrimeric velvet complex composed of LAE1, VE1 and VELB; VE1 acting as a bridging protein between LAE1 and VEL2 (By similarity). Interacts with VE1 (PubMed:24792348). Forms a heterodimeric complex with VOS1; the formation of the VELB-VOS1 complex is light-dependent (By similarity).
Component of the velvet transcription factor complex that controls sexual/asexual developmental ratio in response to light, promoting sexual development in the darkness while stimulating asexual sporulation under illumination (PubMed:24792348). The velvet complex acts as a global regulator for secondary metabolite gene expression (By similarity). Component of the VELB-VOS1 heterodimeric complex that plays a dual role in activating genes associated with spore maturation and repressing certain development-associated genes (By similarity). The VELB-VOS1 complex binds DNA through the DNA-binding domain of VOS1 that recognizes an 11-nucleotide consensus sequence 5'-CTGGCCGCGGC-3' consisting of two motifs in the promoters of key developmental regulatory genes (By similarity). Controls the expression of the fumonisins gene cluster (PubMed:24792348). Involved in cell wall integrity, cell surface hydrophobicity, hyphal polarity and conidiation pattern (PubMed:24792348). Involved in oxidative stress resistance by positively regulating the transcription of the catalase-encoding gene CAT2 (PubMed:24792348).
Suppresses aerial hyphal growth,reduced colony surface hydrophobicity on solid media, and increases the ratio of macroconidia to microconidia (PubMed:24792348). Reduces the production of fumonisins (PubMed:24792348).
Probably involved in transcription regulation via its interaction with the INO80 complex, a chromatin remodeling complex.
Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent, however specific DNA sequences that define origins of replication have not been identified so far. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication.
Belongs to the metallo-beta-lactamase superfamily. Glyoxalase II family.
Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Component of the SMC5-SMC6 complex, that promotes sister chromatid alignment after DNA damage and facilitates double-stranded DNA breaks (DSBs) repair via homologous recombination between sister chromatids.
Essential component of the cytosolic iron-sulfur (Fe/S) protein assembly machinery. Required for the maturation of extramitochondrial Fe/S proteins.
Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides.
Belongs to the adenylosuccinate synthetase family.
Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first commited step in the biosynthesis of AMP from IMP.
Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Plays an important role in the de novo pathway of purine nucleotide biosynthesis.
Belongs to the WD repeat G protein beta family.
Belongs to the transcriptional coactivator PC4 family.
Belongs to the histidinol dehydrogenase family.
Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
Involved in the assembly of the cytochrome c oxidase complex.
Abolishes the expression of FUB1, FUB3 and FUB8, and impairs the production of fusaric acid (PubMed:25372119).
Transcription factor that regulates the expression of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties (PubMed:25372119).
Belongs to the nicotianamine synthase (NAS)-like family.
Involved in maceration and soft-rotting of plant tissue.
Belongs to the WD repeat CDC20/Fizzy family.
Belongs to the alkaline phosphatase family.
Belongs to the eukaryotic/archaeal RNase P protein component 2 family.
Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Acyl-CoA synthetase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), and B4 (FB4), which are carcinogenic mycotoxins (PubMed:12620260, PubMed:17147424). On the basis of the chemical structures of fumonisins and precursor feeding studies, fumonisin biosynthesis is predicted to include at least five groups of biochemical reactions: synthesis of a linear polyketide with a single terminal carbonyl function and methyl groups at C-10 and C-14; condensation of the polyketide with alanine; reduction of the polyketide carbonyl to a hydroxyl; hydroxylation of 2-4 polyketide carbons; and esterification of six-carbon tricarboxylic acids to two of the hydroxyls (PubMed:12620260). The biosynthesis starts with the polyketide synthase FUM1-catalyzed carbon chain assembly from one molecule of acetyl CoA, eight molecules of malonyl CoA, and two molecules of methionine (PubMed:10413619). The C-18 polyketide chain is released from the enzyme by a nucleophilic attack of a carbanion, which is derived from R-carbon of alanine by decarboxylation, on the carbonyl carbon of polyketide acyl chain (PubMed:15137825, PubMed:12720383). This step is catalyzed by a pyridoxal 5'-phosphate-dependent aminoacyl transferase FUM8 (PubMed:15137825, PubMed:12720383). The resultant 3-keto intermediate 2-amino-3-oxo-12,16-dimethylicosane is then stereospecifically reduced to the 3-hydroxyl product 2-amino-3-hydroxy-12,16-dimethylicosane by reductase FUM13 (PubMed:12720383, PubMed:15137825). Subsequent oxidations at C-5, C-10, C-14 and C-15 followed by tricarballylic esterification of the hydroxyl groups on C-14 and C-15 furnish the biosynthesis of fumonisins (PubMed:15066782, PubMed:15137825, PubMed:16489749). The C-10 hydroxylation is performed by the cytochrome P450 monooxygenase FUM2 and occurs early in the biosynthesis (PubMed:16536629). The C-5 hydroxylation is performed by the dioxygenase FUM3 and occurs late in the biosynthesis (PubMed:20237561, PubMed:15066782, PubMed:15137825, PubMed:16536629). Cytochrome P450 monooxygenases FUM6 and FUM15 may be responsible for the two remaining hydroxylations at positions C-14 and C-15 (PubMed:12620260). The FUM11 tricarboxylate transporter makes a tricarboxylic acid precursor available for fumonisin biosynthesis via its export from the mitochondria (PubMed:12620260). If the precursor is citrate, the FUM7 dehydrogenase could remove the C-3 hydroxyl of citrate to form tricarballylic acid either before or after the CoA activation by the FUM10 acyl-CoA synthetase and FUM14 catalyzed esterification of CoA-activated tricarballylic acid to the C-14 and C-15 hydroxyls of the fumonisin backbone (PubMed:16489749, PubMed:17147424). Alternatively, if the precursor is cis-aconitate, FUM7 may function to reduce the double bond (PubMed:17147424). In this alternate proposal, feeding studies with tetradehydro-fumonisin B1 suggests that FUM7 cannot function on the tricarballylic ester and must therefore act before the FUM14-mediated esterification (PubMed:17147424).
Impairs the ability to produce fumonisins, but accumulates two new metabolites, HFB3 and HFB4, which are biosynthetic precursors of fumonisins lacking the tricarballylic esters (PubMed:17147424).
Belongs to the transglutaminase-like superfamily. PNGase family.
Adenosyl-L-methionine (AdoMet)-dependent tRNA (uracil-O(2)-)-methyltransferase.
Involved in pre-mRNA splicing. Binds and is required for the stability of snRNA U1, U2, U4 and U5 which contain a highly conserved structural motif called the Sm binding site. Involved in cap modification.
Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.
Belongs to the complex I NDUFB7 subunit family.
Belongs to the XPG/RAD2 endonuclease family. XPG subfamily.
Required for the assembly of the V0 complex of the vacuolar ATPase (V-ATPase) in the endoplasmic reticulum.
Belongs to the ATP-dependent DNA ligase family.
Mediates GPI anchoring in the endoplasmic reticulum, by replacing a protein's C-terminal GPI attachment signal peptide with a pre-assembled GPI. During this transamidation reaction, the GPI transamidase forms a carbonyl intermediate with the substrate protein.
Component of the 7-subunit TFIIH core complex.
In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape.
Belongs to the adenylate kinase family. AK3 subfamily.
Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon GTP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent GTP hydrolysis.
Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Has GTP:AMP phosphotransferase and ITP:AMP phosphotransferase activities.
Belongs to the proteasome subunit p27 family.
Belongs to the mannose-6-phosphate isomerase type 1 family.
Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.
Belongs to the archaeal Rpo3/eukaryotic RPB3 RNA polymerase subunit family.
Acts as an adapter for the XPO1/CRM1-mediated export of the 60S ribosomal subunit.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. NifS/IscS subfamily.
Binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit to form the 80S initiation complex in the cytoplasm. Is also involved in ribosome biogenesis. Associates with pre-60S subunits in the nucleus and is involved in its nuclear export.
Monomer. Associates with the 60S ribosomal subunit.
Phosphorylation at Ser-174 and Ser-175 promotes nuclear export.
Belongs to the sirtuin family. Class I subfamily.
Belongs to the mitochondrion-specific ribosomal protein mL50 family.
Belongs to the F-actin-capping protein beta subunit family.
F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.
Belongs to the XPG/RAD2 endonuclease family. FEN1 subfamily.
Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Interacts with PCNA. Three molecules of FEN1 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity.
Phosphorylated. Phosphorylation upon DNA damage induces relocalization to the nuclear plasma.
Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA.
Alpha-L-arabinofuranosidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Releases L-arabinose from arabinoxylan.
Belongs to the glycosyl hydrolase 62 family.
Interacts with ODC and thereby sterically blocks ODC homodimerization.
Ornithine decarboxylase (ODC) antizyme protein that negatively regulates ODC activity and intracellular polyamine biosynthesis in response to increased intracellular polyamine levels. Binds to ODC monomers, inhibiting the assembly of the functional ODC homodimer, and targets the monomers for ubiquitin-independent proteolytic destruction by the 26S proteasome.
Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Abolishes synthesis of the polyketide mycotoxin fumonisin B1 (FB1), severely decreases macroconidia production, results in hydrogen peroxide sensitivity, and decreases virulence in maize kernels.
Expressed during growth on endosperm tissue (PubMed:20854112, PubMed:18705852). Repressed in conditions of high nitrogen (PubMed:20854112).
Transporter for myo-inositol (PubMed:27195938). Also appears to transport the polyketide mycotoxin fumonisin B1 (FB1) (PubMed:27195938, PubMed:20854112). Does not appear to transport hexose sugars (PubMed:18705852, PubMed:20854112).
Belongs to the ACC deaminase/D-cysteine desulfhydrase family.
Belongs to the glycosyltransferase 3 family.
Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan.
Belongs to the oxidase-dependent Fe transporter (OFeT) (TC 9.A.10.1) family.
Amidase; part of the Fusarium detoxification of benzoxazolinone cluster 2 (FDB2) involved in the degradation of benzoxazolinones produced by the host plant (PubMed:19302487, PubMed:26808652). Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their inherent instability once released, spontaneously degrade to the more stable corresponding benzoxazolinones, 6-methoxy-2-benzoxazolinone (MBOA) and 2-benzoxazolinone (BOA), respectively (PubMed:11876429). The first step in the detoxification of benzoxazolinones involves the hydrolysis of the cyclic ester bond of benzoxazolinones by the FDB1 cluster gamma-lactamase MBL1 to aminophenols (PubMed:26808652, PubMed:12788712). MBL1 is able to convert BOA into 2-aminophenol (2-AP), as well as MBOA into 5-methoxy-2-aminophenol (2-AMP) (PubMed:26808652, PubMed:12788712). The FDB2 cluster N-malonyltransferase FDB2/NAT1 then metabolizes aminophenols via N-malonylation to non-toxic malonamic acids (PubMed:19302487, PubMed:12788712). FDB2/NAT1 converts 2-AP into N-(2-hydroxyphenyl) malonamic acid (HPMA) and 2-AMP into N-(2-hydroxy-4-methoxyphenyl) malonamic acid (HMPMA) (PubMed:19302487, PubMed:12788712). The duplicated dienlactone hydrolases DLH1 and DLH2 may provide redundant function for hydrolyzing the lactone moiety in the BOA molecule (Probable). The roles of the amidases an other enzymes encoded by the 2 FDB clusters have not been identified so far (Probable).
Expression is not induced in response to 2-benzoxazolinone (BOA) exposure.
Belongs to the cyclophilin-type PPIase family. PPIase D subfamily.
Component of an histone acetyltransferase complex.
Component of an histone acetyltransferase complex. Interacts with H3K4me3 and to a lesser extent with H3K4me2.
The PHD-type zinc finger mediates the binding to H3K4me3.
Belongs to the glycosyltransferase 48 family.
Plays a role in determining ER morphology.
The C4-type zinc finger motif is necessary both for its ER three-way tubular junction localization and formation.
Golgi membrane protein involved in vesicular trafficking and spindle migration.
Belongs to the eukaryotic ribosomal protein eS8 family.
Belongs to the complex I NDUFA1 subunit family.
Belongs to the LDH/MDH superfamily. MDH type 1 family.
Aminocarboxypropyltransferase that catalyzes the aminocarboxypropyl transfer on pseudouridine at position 1191 (Psi1191) in 18S rRNA. It constitutes the last step in biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S rRNA.
Belongs to the TDD superfamily. TSR3 family.
Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35) family.
Required for synthesis of 60S ribosomal subunits and the transport of pre-ribosomes from the nucleoplasm to the cytoplasm.
Belongs to the ATPase gamma chain family.
F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c.
Mevalonate kinase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway. The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins.
May participate in the translocation of oligosaccharide from the cytoplasmic side to the lumenal side of the endoplasmic reticulum membrane.
Belongs to the transaldolase family. Type 1 subfamily.
Catalyzes the rate-limiting step of the non-oxidative phase in the pentose phosphate pathway. Catalyzes the reversible conversion of sedheptulose-7-phosphate and D-glyceraldehyde 3-phosphate into erythrose-4-phosphate and beta-D-fructose 6-phosphate.
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome.
RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
Probable acetyltransferase, which acetylates the inositol ring of phosphatidylinositol during biosynthesis of GPI-anchor.
5'->3' double-stranded DNA exonuclease which may also possess a cryptic 3'->5' double-stranded DNA exonuclease activity. Functions in DNA mismatch repair.
Belongs to the XPG/RAD2 endonuclease family. EXO1 subfamily.
Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
Belongs to the class I-like SAM-binding methyltransferase superfamily. Erg6/SMT family.
Catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of lanosterol to form eburicol.
Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37.
Belongs to the ATPase delta chain family.
Belongs to the adenosylhomocysteinase family.
Belongs to the nitrate reductase family.
Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria.
Belongs to the methyltransferase superfamily. Type-7 methyltransferase family.
Methyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C (PubMed:17121404, PubMed:22652150). Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production (By similarity). The roles of the other FUS members are yet undetermined (By similarity). The fusarin C synthetase FUS1 is responsible for the condensation of one acetyl-coenzyme A (CoA) unit with six malonyl-CoA units and the amide linkage of the arising heptaketide and homoserine, subsequently releasing the first intermediate, prefusarin, as an alcohol with an open ring structure (PubMed:17121404). The cytochrome P450 monooxygenase FUS8 participates in multiple oxidation processes at carbon C-20 and is able to use the FUS1 product as substrate, resulting in formation of 20-hydroxy-prefusarin (By similarity). This reaction seems to be essential before the 2-pyrrolidone ring closure can be catalyzed by FUS2, generating 20-hydroxy-fusarin (By similarity). FUS8 is able to further oxidizes carbon C-20 after ring closure, resulting in the formation of carboxy-fusarin C (By similarity). As the last step, FUS9 methylates the hydroxyl group at C-21 to generate fusarin C (By similarity). Fusarin C can then rearrange to epi-fusarin C, the (z)-isomers, and fusarin A and fusarin D (By similarity).
Belongs to the mitochondrion-specific ribosomal protein mS41 family.
Belongs to the thiolase-like superfamily. Chalcone/stilbene synthases family.
Belongs to the Mediator complex subunit 7 family.
Belongs to the HAD-like hydrolase superfamily. SerB family.
Belongs to the non-repetitive/WGA-negative nucleoporin family.
Component of the RIX1 complex required for processing of ITS2 sequences from 35S pre-rRNA.
Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase NEP1 family.
Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines.
Belongs to the iron-containing alcohol dehydrogenase family. Hydroxyacid-oxoacid transhydrogenase subfamily.
Belongs to the indoleamine 2,3-dioxygenase family.
Plays a central role as a glucosyl donor in cellular metabolic pathways.
Belongs to the eukaryotic ribosomal protein eS27 family.
Belongs to the aldolase class II family. MtnB subfamily.
Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).
Belongs to the lysophospholipase family.
Belongs to the NAD(P)-dependent epimerase/dehydratase family. UDP-glucuronic acid decarboxylase subfamily.
Involved in nuclear export, actin cytoskeleton organization and vesicular transport.
Belongs to the methyltransferase superfamily. RRP8 family.
S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(1) position of adenine in helix 25.1 in 25S rRNA. Required both for ribosomal 40S and 60S subunits biogenesis. Required for efficient pre-rRNA cleavage at site A2.
Belongs to the TFIIF beta subunit family.
Plays an important role in the elongation step of protein synthesis.
Belongs to the adenylate kinase family. AK2 subfamily.
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways.
Belongs to the DASH complex DAD3 family.
FUM14 encodes a nonribosomal peptide synthetasecontaining two domains, a peptidyl carrier protein domain and a condensation domain (PubMed:16489749). The condensation domain catalyzes a C-O bond (ester) formation and can convert HFB1, a precursor of fumonisin B1 lacking the tricarballylic ester, to fumonisin B1 (PubMed:16489749).
Loses the ability to produce fumonisins, but accumulates two new metabolites, HFB3 and HFB4, which are biosynthetic precursors of fumonisins lacking the tricarballylic esters (PubMed:16489749, PubMed:17147424).
Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), and B4 (FB4), which are carcinogenic mycotoxins (PubMed:12620260, PubMed:16489749, PubMed:17147424). On the basis of the chemical structures of fumonisins and precursor feeding studies, fumonisin biosynthesis is predicted to include at least five groups of biochemical reactions: synthesis of a linear polyketide with a single terminal carbonyl function and methyl groups at C-10 and C-14; condensation of the polyketide with alanine; reduction of the polyketide carbonyl to a hydroxyl; hydroxylation of 2-4 polyketide carbons; and esterification of six-carbon tricarboxylic acids to two of the hydroxyls (PubMed:12620260). The biosynthesis starts with the polyketide synthase FUM1-catalyzed carbon chain assembly from one molecule of acetyl CoA, eight molecules of malonyl CoA, and two molecules of methionine (PubMed:10413619). The C-18 polyketide chain is released from the enzyme by a nucleophilic attack of a carbanion, which is derived from R-carbon of alanine by decarboxylation, on the carbonyl carbon of polyketide acyl chain (PubMed:15137825, PubMed:12720383). This step is catalyzed by a pyridoxal 5'-phosphate-dependent aminoacyl transferase FUM8 (PubMed:15137825, PubMed:12720383). The resultant 3-keto intermediate 2-amino-3-oxo-12,16-dimethylicosane is then stereospecifically reduced to the 3-hydroxyl product 2-amino-3-hydroxy-12,16-dimethylicosane by reductase FUM13 (PubMed:12720383, PubMed:15137825). Subsequent oxidations at C-5, C-10, C-14 and C-15 followed by tricarballylic esterification of the hydroxyl groups on C-14 and C-15 furnish the biosynthesis of fumonisins (PubMed:15066782, PubMed:15137825, PubMed:16489749). The C-10 hydroxylation is performed by the cytochrome P450 monooxygenase FUM2 and occurs early in the biosynthesis (PubMed:16536629). The C-5 hydroxylation is performed by the dioxygenase FUM3 and occurs late in the biosynthesis (PubMed:20237561, PubMed:15066782, PubMed:15137825, PubMed:16536629). Cytochrome P450 monooxygenases FUM6 and FUM15 may be responsible for the two remaining hydroxylations at positions C-14 and C-15 (PubMed:12620260). The FUM11 tricarboxylate transporter makes a tricarboxylic acid precursor available for fumonisin biosynthesis via its export from the mitochondria (PubMed:12620260). If the precursor is citrate, the FUM7 dehydrogenase could remove the C-3 hydroxyl of citrate to form tricarballylic acid either before or after the CoA activation by the FUM10 acyl-CoA synthetase and FUM14 catalyzed esterification of CoA-activated tricarballylic acid to the C-14 and C-15 hydroxyls of the fumonisin backbone (PubMed:16489749, PubMed:17147424). Alternatively, if the precursor is cis-aconitate, FUM7 may function to reduce the double bond (PubMed:17147424). In this alternate proposal, feeding studies with tetradehydro-fumonisin B1 suggests that FUM7 cannot function on the tricarballylic ester and must therefore act before the FUM14-mediated esterification (PubMed:17147424).
Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family.
Belongs to the ferredoxin--NADP reductase type 1 family.
Catalyzes the hydration of cyanide to formamide. Degradation of cyanide may be important for plant pathogenic fungi in infection of cyanogenic plants.
Oligomer of dimers, forming left-handed helical fibers.
Belongs to the cytochrome c oxidase VIIc family.
Component of the cytochrome c oxidase (complex IV, CIV), a multisubunit enzyme composed of a catalytic core of 3 subunits and several supernumerary subunits. The complex exists as a monomer or a dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII).
Belongs to the proteasome subunit S14 family.
Belongs to the Mediator complex subunit 31 family.
Belongs to the uroporphyrinogen-III synthase family.
Belongs to the small GTPase superfamily. Rho family. CDC42 subfamily.
Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state.
In the C-terminal section; belongs to the trehalose phosphatase family.
In the N-terminal section; belongs to the glycosyltransferase 20 family.
Involved in cytoplasm to vacuole transport (Cvt), pexophagy, mitophagy and nucleophagy. Recruits mitochondria for their selective degradation via autophagy (mitophagy) during starvation. Works as scaffold proteins that recruit ATG proteins to the pre-autophagosome (PAS), the site of vesicle/autophagosome formation. Required for the Cvt vesicles completion.
Belongs to the universal ribosomal protein uL22 family.
Functions as actin-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks.
Cleaves the gamma-glutamyl peptide bond of glutathione and glutathione conjugates.
Belongs to the RNA cytidine acetyltransferase family. NAT10 subfamily.
RNA cytidine acetyltransferase with specificity toward both 18S rRNA and tRNAs. Catalyzes the formation of N(4)-acetylcytidine (ac4C) in 18S rRNA. Required for early nucleolar cleavages of precursor rRNA at sites A0, A1 and A2 during 18S rRNA synthesis. Catalyzes the formation of ac4C in serine and leucine tRNAs. Requires the tRNA-binding adapter protein TAN1 for full tRNA acetyltransferase activity but not for 18S rRNA acetylation.
Produces ATP from ADP in the presence of a proton gradient across the membrane.
Belongs to the transient receptor potential (TRP) ion channel family.
S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(1) position of an adenine present in helix 65 in 25S rRNA.
Belongs to the aerobic coproporphyrinogen-III oxidase family.
Belongs to the ribonucleoside diphosphate reductase large chain family.
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Belongs to the iron/manganese superoxide dismutase family.
Component of the ESCRT-I complex (endosomal sorting complex required for transport I), a regulator of vesicular trafficking process.
Adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man(5)GlcNAc(2)-PP-Dol.
Component of the ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme composed of 3 respiratory subunits cytochrome b, cytochrome c1 and Rieske protein, 2 core protein subunits, and additional low-molecular weight protein subunits. The complex exists as an obligatory dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with cytochrome c oxidase (complex IV, CIV).
Belongs to the calcium channel alpha-1 subunit (TC 1.A.1.11) family.
Belongs to the diphosphomevalonate decarboxylase family.
Nonessential protein required for the fusion of transport vesicles derived from the endocytic pathway with the Golgi complex.
Component of the endosomal sorting complex required for transport II (ESCRT-II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs.
Component of the endosomal sorting complex required for transport II (ESCRT-II).
In the C-terminal section; belongs to the AIR carboxylase family. Class I subfamily.
Belongs to the AB hydrolase superfamily. LDAH family.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type V subfamily.
Belongs to the complex I NDUFS5 subunit family.
20-hydroxy-prefusarin hydrolase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C (PubMed:17121404, PubMed:22652150). Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production (By similarity). The roles of the other FUS members are yet undetermined (By similarity). The fusarin C synthetase FUS1 is responsible for the condensation of one acetyl-coenzyme A (CoA) unit with six malonyl-CoA units and the amide linkage of the arising heptaketide and homoserine, subsequently releasing the first intermediate, prefusarin, as an alcohol with an open ring structure (PubMed:17121404). The cytochrome P450 monooxygenase FUS8 participates in multiple oxidation processes at carbon C-20 and is able to use the FUS1 product as substrate, resulting in formation of 20-hydroxy-prefusarin (By similarity). This reaction seems to be essential before the 2-pyrrolidone ring closure can be catalyzed by FUS2, generating 20-hydroxy-fusarin (By similarity). FUS8 is able to further oxidizes carbon C-20 after ring closure, resulting in the formation of carboxy-fusarin C (By similarity). As the last step, FUS9 methylates the hydroxyl group at C-21 to generate fusarin C (By similarity). Fusarin C can then rearrange to epi-fusarin C, the (z)-isomers, and fusarin A and fusarin D (By similarity).
Belongs to the AB hydrolase superfamily. FUS2 hydrolase family.
Belongs to the JHDM3 histone demethylase family.
This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand.
Components of the endosome-vacuole trafficking pathway that regulates nutrient transport. May be involved in processes which determine whether plasma membrane proteins are degraded or routed to the plasma membrane.
The glycine cleavage system catalyzes the degradation of glycine.
Belongs to the glycosyltransferase 22 family. PIGB subfamily.
Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the third mannose to Man2-GlcN-acyl-PI during GPI precursor assembly.
Belongs to the CDP-alcohol phosphatidyltransferase class-II family.
Functions in the biosynthesis of the anionic phospholipids phosphatidylglycerol and cardiolipin.
Belongs to the eukaryotic ribosomal protein eL6 family.
Belongs to the ribonucleoside diphosphate reductase small chain family.
Catalyzes the last step of tRNA splicing, the transfer of the splice junction 2'-phosphate from ligated tRNA to NAD to produce ADP-ribose 1''-2'' cyclic phosphate.
Belongs to the thymidylate kinase family.
Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with NCS6 that ligates sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. May also be involved in protein urmylation.
Belongs to the arylamine N-acetyltransferase family.
Belongs to the Dus family. Dus3 subfamily.
Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. Specifically modifies U47 in cytoplasmic tRNAs (By similarity). Catalyzes the synthesis of dihydrouridine in some mRNAs, thereby affecting their translation.
Component of the microsomal membrane bound fatty acid elongation system, which produces the 26-carbon very long-chain fatty acids (VLCFA) from palmitate. Catalyzes the reduction of the 3-ketoacyl-CoA intermediate that is formed in each cycle of fatty acid elongation. VLCFAs serve as precursors for ceramide and sphingolipids.
Belongs to the DHHC palmitoyltransferase family. PFA4 subfamily.
Mediates the reversible addition of palmitate to target proteins, thereby regulating their membrane association and biological function.
Belongs to the phosphoglycerate kinase family.
Belongs to the class-II aminoacyl-tRNA synthetase family. Alax-L subfamily.
Belongs to the eukaryotic ribosomal protein eS10 family.
Belongs to the DASH complex DUO1 family.
Belongs to the glycogen debranching enzyme family.
Multifunctional enzyme acting as 1,4-alpha-D-glucan:1,4-alpha-D-glucan 4-alpha-D-glycosyltransferase and amylo-1,6-glucosidase in glycogen degradation.
Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
Belongs to the band 7/mec-2 family. Flotillin subfamily.
Belongs to the PEP-utilizing enzyme family.
Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate.
Component of the proteasome, a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
Component of the ESCRT-II complex (endosomal sorting complex required for transport II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs.
Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria. Constitutes a pore-forming and calcium-conducting subunit. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cell death pathways.
Belongs to the palmitoyl-protein thioesterase family.
Belongs to the methyltransferase superfamily.
ATP-dependent DNA helicase involved in DNA damage repair by homologous recombination and in genome maintenance. Capable of unwinding D-loops. Plays a role in limiting crossover recombinants during mitotic DNA double-strand break (DSB) repair. Component of a FANCM-MHF complex which promotes gene conversion at blocked replication forks, probably by reversal of the stalled fork.
Belongs to the DEAD box helicase family. DEAH subfamily. FANCM sub-subfamily.
Interacts with the MHF histone-fold complex to form the FANCM-MHF complex.
Regulatory subunit of the dolichol-phosphate mannose (DPM) synthase complex; essential for the ER localization.
Belongs to the MICOS complex subunit Mic10 family.
Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-dependent O-methyltransferase family.
Has a role in promoting intracellular calcium ion sequestration via the exchange of calcium ions for hydrogen ions across the vacuolar membrane. Involved also in manganese ion homeostasis via its uptake into the vacuole.
Part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties (PubMed:22652150, PubMed:25372119). L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L-homoserine by cluster enzymes aspartate kinase FUB3 and homoserine O-acetyltransferase FUB5, as well as enzymes of the primary metabolism (By similarity). The polyketide synthase (PKS) FUB1 generates the triketide trans-2-hexenal which is presumptively released by the hydrolase FUB4 and linked to the NRPS-bound amino acid precursor by NAD(P)-dependent dehydrogenase FUB6 (By similarity). FUB1, FUB4, and the non-canonical NRPS Fub8 may form an enzyme complex (By similarity). Further processing of the NRPS-bound intermediate might be carried out by FUB6 and the sulfhydrylase FUB7, enabling a spontaneous electrocyclization to close the carbon backbone of fusaric acid (By similarity). Dihydrofusaric acid is likely to be released via reduction by the thioester reductase (TR) domain of FUB8 whereupon the final oxidation to fusaric acid may (also) be performed by the FMN-dependent dehydrogenase FUB9 (By similarity).
Belongs to the glycosyl hydrolase 38 family.
Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Confers resistance to H(2)O(2) in hyphae. May play an antioxidative role in fungal defense against the host-produced H(2)O(2) (oxidative burst) at the early stage of plant infection.
Belongs to the dihydroxyacetone kinase (DAK) family.
Catalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde.
Belongs to the velvet family. VeA subfamily.
Component of the heterotrimeric velvet complex composed of LAE1, VE1 and VELB; VE1 acting as a bridging protein between LAE1 and VELB (By similarity). Interacts with VELB and VELC (PubMed:24792348).
Component of the velvet transcription factor complex that controls sexual/asexual developmental ratio in response to light, promoting sexual development in the darkness while stimulating asexual sporulation under illumination (By similarity). The velvet complex hat acts as a global regulator for secondary metabolite gene expression (PubMed:22247572). Controls the expression of the cycotoxins fumonisins and fusarins gene cluster (PubMed:22247572, PubMed:19382792, PubMed:24792348). Involved in cell wall integrity, cell surface hydrophobicity, hyphal polarity and conidiation pattern (PubMed:17054442, PubMed:24792348). Required for pathogenicity against maize seedlings (PubMed:22247572). Involved in oxidative stress resistance by positively regulating the transcription of the catalase-encoding gene CAT2 (PubMed:24792348).
Suppresses aerial hyphal growth,reduced colony surface hydrophobicity on solid media, and increases the ratio of macroconidia to microconidia (PubMed:17054442, PubMed:24792348). Impairs production of fumonisins and fusarins, and reduces pathogenicity against maize seedlings (PubMed:22247572, PubMed:19382792, PubMed:24792348).
The C-terminal PEST domain is a region rich in proline, glutamic acid, serine and threonine residues that is required for the light-dependent regulation of development and secondary metabolism (By similarity).
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Belongs to the Mediator complex subunit 22 family.
Belongs to the acetyltransferase family. NAA40 subfamily.
Belongs to the glycosyl hydrolase 81 family.
Belongs to the ATG13 family. Fungi subfamily.
Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.
Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.
Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
Belongs to the Cu-Zn superoxide dismutase family.
Belongs to the eukaryotic RPA49/POLR1E RNA polymerase subunit family.
Nuclear serine protease which mediates apoptosis.
Catalyzes conversion of folates to polyglutamate derivatives allowing concentration of folate compounds in the cell and the intracellular retention of these cofactors, which are important substrates for most of the folate-dependent enzymes that are involved in one-carbon transfer reactions involved in purine, pyrimidine and amino acid synthesis.
Component of the small nucleolar ribonucleoprotein particles containing H/ACA-type snoRNAs (H/ACA snoRNPs).
Required for ribosome biogenesis. Part of a complex which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ("psi") residues may serve to stabilize the conformation of rRNAs.
Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
Belongs to the DASH complex DAM1 family.
Involved in nucleolar processing of pre-18S ribosomal RNA.
Belongs to the NADPH--cytochrome P450 reductase family.
In the N-terminal section; belongs to the flavodoxin family.
This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. Involved in ergosterol biosynthesis.
Belongs to the SMC family. SMC6 subfamily.
Belongs to the Mediator complex subunit 6 family.
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery.
Belongs to the TAF9 family. CENP-S/MHF1 subfamily.
Belongs to the archaeal/bacterial/fungal opsin family.
Belongs to the protein disulfide isomerase family.
Participates in the folding of proteins containing disulfide bonds, may be involved in glycosylation, prolyl hydroxylation and triglyceride transfer.
Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.
Mycophenolic acid (MPA) is a non-competitive inhibitor that prevents formation of the closed enzyme conformation by binding to the same site as the amobile flap. In contrast, mizoribine monophosphate (MZP) is a competitive inhibitor that induces the closed conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of bacterial IMPDH.
Required for retention of late Golgi membrane proteins. Component of the retrieval machinery that functions by direct interaction with the cytosolic tails of certain TGN membrane proteins during the sorting/budding process at the prevacuolar compartment. Binds phosphatidylinositol 3-phosphate (PtdIns(P3)).
Catalyzes the intermembrane transfer of phosphatidylglycerol and phosphatidylinositol.
Dioxygenase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), and B4 (FB4), which are carcinogenic mycotoxins (PubMed:11728154, PubMed:12620260, PubMed:14602658, PubMed:15066782, PubMed:16536629). On the basis of the chemical structures of fumonisins and precursor feeding studies, fumonisin biosynthesis is predicted to include at least five groups of biochemical reactions: synthesis of a linear polyketide with a single terminal carbonyl function and methyl groups at C-10 and C-14; condensation of the polyketide with alanine; reduction of the polyketide carbonyl to a hydroxyl; hydroxylation of 2-4 polyketide carbons; and esterification of six-carbon tricarboxylic acids to two of the hydroxyls (PubMed:12620260). The biosynthesis starts with the polyketide synthase FUM1-catalyzed carbon chain assembly from one molecule of acetyl CoA, eight molecules of malonyl CoA, and two molecules of methionine (PubMed:10413619). The C-18 polyketide chain is released from the enzyme by a nucleophilic attack of a carbanion, which is derived from R-carbon of alanine by decarboxylation, on the carbonyl carbon of polyketide acyl chain (PubMed:15137825, PubMed:12720383). This step is catalyzed by a pyridoxal 5'-phosphate-dependent aminoacyl transferase FUM8 (PubMed:15137825, PubMed:12720383). The resultant 3-keto intermediate 2-amino-3-oxo-12,16-dimethylicosane is then stereospecifically reduced to the 3-hydroxyl product 2-amino-3-hydroxy-12,16-dimethylicosane by reductase FUM13 (PubMed:12720383, PubMed:15137825). Subsequent oxidations at C-5, C-10, C-14 and C-15 followed by tricarballylic esterification of the hydroxyl groups on C-14 and C-15 furnish the biosynthesis of fumonisins (PubMed:15066782, PubMed:15137825, PubMed:16489749). The C-10 hydroxylation is performed by the cytochrome P450 monooxygenase FUM2 and occurs early in the biosynthesis (PubMed:16536629). The C-5 hydroxylation is performed by the dioxygenase FUM3 and occurs late in the biosynthesis (PubMed:20237561, PubMed:15066782, PubMed:15137825, PubMed:16536629). Cytochrome P450 monooxygenases FUM6 and FUM15 may be responsible for the two remaining hydroxylations at positions C-14 and C-15 (PubMed:12620260). The FUM11 tricarboxylate transporter makes a tricarboxylic acid precursor available for fumonisin biosynthesis via its export from the mitochondria (PubMed:12620260). If the precursor is citrate, the FUM7 dehydrogenase could remove the C-3 hydroxyl of citrate to form tricarballylic acid either before or after the CoA activation by the FUM10 acyl-CoA synthetase and FUM14 catalyzed esterification of CoA-activated tricarballylic acid to the C-14 and C-15 hydroxyls of the fumonisin backbone (PubMed:16489749, PubMed:17147424). Alternatively, if the precursor is cis-aconitate, FUM7 may function to reduce the double bond (PubMed:17147424). In this alternate proposal, feeding studies with tetradehydro-fumonisin B1 suggests that FUM7 cannot function on the tricarballylic ester and must therefore act before the FUM14-mediated esterification (PubMed:17147424).
Produces only fumonisins B3 and B4 (PubMed:14602658, PubMed:16536629).
Acts as component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover. The NOT protein subcomplex negatively regulates the basal and activated transcription of many genes. Preferentially affects TC-type TATA element-dependent transcription. Could directly or indirectly inhibit component(s) of the general transcription machinery.
In the C-terminal section; belongs to the NAD synthetase family.
Has kinase activity and phosphorylates inositol-1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5) to produce 1,2,3,4,5,6-hexakisphosphate (InsP6), also known as phytate.
Phosphorylates Ins(1,3,4,5,6)P5 at position 2 to form Ins(1,2,3,4,5,6)P6 (InsP6 or phytate).
The EXKPK motif is conserved in inositol-pentakisphosphate 2-kinases of both family 1 and 2.
Belongs to the adenylate kinase family. AK6 subfamily.
Broad-specificity nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Has also ATPase activity. May be involved in rRNA maturation and transcription regulation.
Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily.
Belongs to the peptidase C19 family. PAN2 subfamily.
Binds 2 metal cations per subunit in the catalytic exonuclease domain.
Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein PAB1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails.
Contains a pseudo-UCH domain. This ubiquitin C-terminal hydrolase (UCH)-like or ubiquitin specific protease (USP)-like domain is predicted to be catalytically inactive because it lacks the active site catalytic triad characteristic of thiol proteases, with residues at the equivalent structural positions that are incompatible with catalysis, and it cannot bind ubiquitin. It functions as a structural scaffold for intra- and intermolecular interactions in the complex.
Forms a heterotrimer with an asymmetric homodimer of the regulatory subunit PAN3 to form the poly(A)-nuclease (PAN) deadenylation complex.
Positively regulated by the regulatory subunit PAN3.
The linker, or PAN3 interaction domain (PID), between the WD40 repeats and the pseudo-UCH domain mediates interaction with PAN3.
Belongs to the complex I NDUFA8 subunit family.
Belongs to the Nudix hydrolase family. DCP2 subfamily.
Belongs to the Mrp/NBP35 ATP-binding proteins family. NUBP1/NBP35 subfamily.
Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable clusters in the N-termini of NBP35 and two labile, bridging clusters between subunits of the NBP35-CFD1 heterotetramer.
Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NBP35-CFD1 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins.
Heterotetramer of 2 NBP35 and 2 CFD1 chains.
Belongs to the DPH1/DPH2 family. DPH2 subfamily.
Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising DPH3 and a NADH-dependent reductase. Facilitates the reduction of the catalytic iron-sulfur cluster found in the DPH1 subunit.
Does not affect 2-benzoxazolinone (BOA) degradation.
Transmembrane transporter; part of the Fusarium detoxification of benzoxazolinone cluster 1 (FDB1) involved in the degradation of benzoxazolinones produced by the host plant (PubMed:26808652). Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their inherent instability once released, spontaneously degrade to the more stable corresponding benzoxazolinones, 6-methoxy-2-benzoxazolinone (MBOA) and 2-benzoxazolinone (BOA), respectively (PubMed:11876429). Might be involved in the transport of metabolites of benzoxazolinone degradation (Probable).
Belongs to the glutamate--cysteine ligase type 3 family.
Belongs to the bacterial ribosomal protein bL33 family.
TFIIA is a component of the transcription machinery of RNA polymerase II and plays an important role in transcriptional activation. TFIIA in a complex with TBP mediates transcriptional activity.
Belongs to the small GTPase superfamily. SAR1 family.
Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released.
In the C-terminal section; belongs to the MoeA family.
Belongs to the glycosyl hydrolase 53 family.
NAD(+)-dependent glutamate dehydrogenase which degrades glutamate to ammonia and alpha-ketoglutarate.
Belongs to the DNA mismatch repair MutL/HexB family.
Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes.
Belongs to the universal ribosomal protein uL4 family.
Belongs to the eukaryotic ribosomal protein eL32 family.
Belongs to the eukaryotic ribosomal protein eS28 family.
Non-classical phosphatidylinositol (PtdIns) transfer protein (PITP), which exhibits PtdIns-binding/transfer activity in the absence of detectable PtdCho-binding/transfer activity. Regulates PtdIns(4,5)P2 homeostasis at the plasma membrane. Heme-binding protein that may play a role in organic oxidant-induced stress responses.
Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic type 2 subfamily.
Belongs to the acetyltransferase family. GNAT subfamily.
Belongs to the eukaryotic ATPase epsilon family.
Belongs to the DASH complex DAD2 family.
Belongs to the Mediator complex subunit 17 family.
Belongs to the RecA family. RAD51 subfamily.
Required both for recombination and for the repair of DNA damage caused by X-rays.
Key enzyme involved in DNA replication and DNA repair. Involved in Okazaki fragments processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA and becomes a substrate for FEN1. Also involved in 5'-end resection of DNA during double-strand break (DSB) repair by mediating the cleavage of 5'-ssDNA.
Aminotransferase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), and B4 (FB4), which are carcinogenic mycotoxins (PubMed:11728154, PubMed:15137825). On the basis of the chemical structures of fumonisins and precursor feeding studies, fumonisin biosynthesis is predicted to include at least five groups of biochemical reactions: synthesis of a linear polyketide with a single terminal carbonyl function and methyl groups at C-10 and C-14; condensation of the polyketide with alanine; reduction of the polyketide carbonyl to a hydroxyl; hydroxylation of 2-4 polyketide carbons; and esterification of six-carbon tricarboxylic acids to two of the hydroxyls (PubMed:12620260). The biosynthesis starts with the polyketide synthase FUM1-catalyzed carbon chain assembly from one molecule of acetyl CoA, eight molecules of malonyl CoA, and two molecules of methionine (PubMed:10413619). The C-18 polyketide chain is released from the enzyme by a nucleophilic attack of a carbanion, which is derived from R-carbon of alanine by decarboxylation, on the carbonyl carbon of polyketide acyl chain (PubMed:15137825, PubMed:12720383). This step is catalyzed by a pyridoxal 5'-phosphate-dependent aminoacyl transferase FUM8 (PubMed:15137825, PubMed:12720383). The resultant 3-keto intermediate 2-amino-3-oxo-12,16-dimethylicosane is then stereospecifically reduced to the 3-hydroxyl product 2-amino-3-hydroxy-12,16-dimethylicosane by reductase FUM13 (PubMed:12720383, PubMed:15137825). Subsequent oxidations at C-5, C-10, C-14 and C-15 followed by tricarballylic esterification of the hydroxyl groups on C-14 and C-15 furnish the biosynthesis of fumonisins (PubMed:15066782, PubMed:15137825, PubMed:16489749). The C-10 hydroxylation is performed by the cytochrome P450 monooxygenase FUM2 and occurs early in the biosynthesis (PubMed:16536629). The C-5 hydroxylation is performed by the dioxygenase FUM3 and occurs late in the biosynthesis (PubMed:20237561, PubMed:15066782, PubMed:15137825, PubMed:16536629). Cytochrome P450 monooxygenases FUM6 and FUM15 may be responsible for the two remaining hydroxylations at positions C-14 and C-15 (PubMed:12620260). The FUM11 tricarboxylate transporter makes a tricarboxylic acid precursor available for fumonisin biosynthesis via its export from the mitochondria (PubMed:12620260). If the precursor is citrate, the FUM7 dehydrogenase could remove the C-3 hydroxyl of citrate to form tricarballylic acid either before or after the CoA activation by the FUM10 acyl-CoA synthetase and FUM14 catalyzed esterification of CoA-activated tricarballylic acid to the C-14 and C-15 hydroxyls of the fumonisin backbone (PubMed:16489749, PubMed:17147424). Alternatively, if the precursor is cis-aconitate, FUM7 may function to reduce the double bond (PubMed:17147424). In this alternate proposal, feeding studies with tetradehydro-fumonisin B1 suggests that FUM7 cannot function on the tricarballylic ester and must therefore act before the FUM14-mediated esterification (PubMed:17147424).
Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. BioF subfamily.
Expression correlates with fuminisins production (PubMed:11728154). Expression is positively regulated by the fumonisin gene cluster-specific transcription regulator FUM21 (PubMed:17483290).
Impairs the production of fumonisins (PubMed:11728154, PubMed:15137825).
Has a role in nuclear-cytoplasmic transport of proteins and mRNAs.
First step of mRNA capping. Converts the 5'-triphosphate end of a nascent mRNA chain into a diphosphate end.
Heterodimer. The mRNA-capping enzyme is composed of two separate chains alpha and beta, respectively a mRNA guanylyltransferase and an mRNA 5'-triphosphate monophosphatase.
Belongs to the MIP/aquaporin (TC 1.A.8) family.
Involved in ds DNA break repair. Has a role in non-homologous integration (NHI) pathways where it is required in the final step of non-homologous end-joining.
Belongs to the eukaryotic RPA43 RNA polymerase subunit family.
Belongs to the universal ribosomal protein uL29 family.
In the C-terminal section; belongs to the histidinol dehydrogenase family.
Belongs to the actin family. ARP3 subfamily.
Belongs to the type IA topoisomerase family.
Introduces a single-strand break via transesterification at a target site in duplex DNA. Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand.
Interacts with EME1 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication fork intermediates. May be required in meiosis for the repair of meiosis-specific double strand breaks subsequent to single-end invasion (SEI).
Belongs to the PC-esterase family. CASD1 subfamily.
Belongs to the metallo-beta-lactamase superfamily.
Gamma-lactamase; part of the Fusarium detoxification of benzoxazolinone cluster 2 (FDB2) involved in the degradation of benzoxazolinones produced by the host plant (PubMed:19302487, PubMed:26808652). Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their inherent instability once released, spontaneously degrade to the more stable corresponding benzoxazolinones, 6-methoxy-2-benzoxazolinone (MBOA) and 2-benzoxazolinone (BOA), respectively (PubMed:11876429). The first step in the detoxification of benzoxazolinones involves the hydrolysis of the cyclic ester bond of benzoxazolinones by the FDB1 cluster gamma-lactamase MBL1 to aminophenols (PubMed:26808652, PubMed:12788712). MBL1 is able to convert BOA into 2-aminophenol (2-AP), as well as MBOA into 5-methoxy-2-aminophenol (2-AMP) (PubMed:26808652, PubMed:12788712). The FDB2 cluster N-malonyltransferase FDB2/NAT1 then metabolizes aminophenols via N-malonylation to non-toxic malonamic acids (PubMed:19302487, PubMed:12788712). FDB2/NAT1 converts 2-AP into N-(2-hydroxyphenyl) malonamic acid (HPMA) and 2-AMP into N-(2-hydroxy-4-methoxyphenyl) malonamic acid (HMPMA) (PubMed:19302487, PubMed:12788712). The duplicated dienlactone hydrolases DLH1 and DLH2 may provide redundant function for hydrolyzing the lactone moiety in the BOA molecule (Probable). The roles of the amidases and other enzymes encoded by the 2 FDB clusters have not been identified so far (Probable).
In the central section; belongs to the inositol 1,4,5-trisphosphate 5-phosphatase family.
Required for the assembly of the mitochondrial respiratory chain complex IV (CIV), also known as cytochrome c oxidase. May participate in merging the COX1 and COX2 assembly lines.
Esterase; part of the Fusarium detoxification of benzoxazolinone cluster 2 (FDB2) involved in the degradation of benzoxazolinones produced by the host plant (PubMed:19302487, PubMed:26808652). Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their inherent instability once released, spontaneously degrade to the more stable corresponding benzoxazolinones, 6-methoxy-2-benzoxazolinone (MBOA) and 2-benzoxazolinone (BOA), respectively (PubMed:11876429). The first step in the detoxification of benzoxazolinones involves the hydrolysis of the cyclic ester bond of benzoxazolinones by the FDB1 cluster gamma-lactamase MBL1 to aminophenols (PubMed:26808652, PubMed:12788712). MBL1 is able to convert BOA into 2-aminophenol (2-AP), as well as MBOA into 5-methoxy-2-aminophenol (2-AMP) (PubMed:26808652, PubMed:12788712). The FDB2 cluster N-malonyltransferase FDB2/NAT1 then metabolizes aminophenols via N-malonylation to non-toxic malonamic acids (PubMed:19302487, PubMed:12788712). FDB2/NAT1 converts 2-AP into N-(2-hydroxyphenyl) malonamic acid (HPMA) and 2-AMP into N-(2-hydroxy-4-methoxyphenyl) malonamic acid (HMPMA) (PubMed:19302487, PubMed:12788712). The duplicated dienlactone hydrolases DLH1 and DLH2 may provide redundant function for hydrolyzing the lactone moiety in the BOA molecule (Probable). The roles of the amidases an other enzymes encoded by the 2 FDB clusters have not been identified so far (Probable).
Belongs to the SLC29A/ENT transporter (TC 2.A.57) family.
Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
Belongs to the PHP hydrolase family. HisK subfamily.
Belongs to the metallo-dependent hydrolases superfamily. NagA family.
In the N-terminal section; belongs to the MoaB/Mog family.
Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II.
Belongs to the WD repeat DCAF13/WDSOF1 family.
Belongs to the class VI-like SAM-binding methyltransferase superfamily. CHO2 family.
Catalyzes the first step of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine (PMME).
Belongs to the transthyretin family. 5-hydroxyisourate hydrolase subfamily.
Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome.
Belongs to the eukaryotic-type primase small subunit family.
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily.
Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. CGI121 acts as an allosteric effector that regulates the t(6)A activity of the complex. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators. CGI121 is not required for tRNA modification.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family.
Binds to the catalytic subunit of the cyclin dependent kinases and is essential for their biological function.
Belongs to the queuosine salvage protein family.
Belongs to the deoxyhypusine synthase family.
Adenine glycosylase active on G-A mispairs.
Belongs to the Mrp/NBP35 ATP-binding proteins family. NUBP2/CFD1 subfamily.
Belongs to the phosphatase 2A regulatory subunit B family.
Belongs to the NAD(P)-dependent epimerase/dehydratase family.
Phosphorylated in response to DNA damage.
Regulatory subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA.
Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family.
The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin.
Involved in ubiquitin-mediated protein degradation. Regulatory factor in the ubiquitin/proteasome pathway that controls the turnover of proteasome substrates. Targets proteasomes to the nucleus and facilitates the degradation of nuclear proteins.
Belongs to the universal ribosomal protein uS11 family.
In the C-terminal section; belongs to the NRP synthetase family.
Belongs to the glycosyl hydrolases 36 family.
Functions as a dosage-dependent inducer in mitotic control. Tyrosine protein phosphatase required for progression of the cell cycle.
Expression is regulated by the upstream regulator ada1 (PubMed:24161731).
Results in near absence of conidia production (PubMed:24161731).
Transcription factor that regulates asexual reproduction (PubMed:24161731). Binds the StuA-response elements (StRE) with the consensus sequence 5'-(A/T)CGCG(T/A)N(A/C)-3' at the promoters of target genes (By similarity).
Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine). The elongator complex catalyzes formation of carboxymethyluridine in the wobble base at position 34 in tRNAs.
Belongs to the methyltransferase superfamily. METL family.
S-adenosyl-L-methionine-dependent methyltransferase.
Belongs to the glycosyl hydrolase 18 family.
Belongs to the NADPH-dependent diflavin oxidoreductase NDOR1 family.
Interacts with DRE2; as part of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery.
NADPH-dependent reductase which is a central component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Transfers electrons from NADPH via its FAD and FMN prosthetic groups to the [2Fe-2S] cluster of DRE2, another key component of the CIA machinery. In turn, this reduced cluster provides electrons for assembly of cytosolic iron-sulfur cluster proteins. Positively controls H(2)O(2)-induced cell death.
Belongs to the vitamin-B12 independent methionine synthase family.
Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
Belongs to the eukaryotic ribosomal protein eL22 family.
Belongs to the proteasome subunit S9 family.
Belongs to the cytidine and deoxycytidylate deaminase family.
Plasma membrane osmosensor that activates the high osmolarity glycerol (HOG) MAPK signaling pathway in response to high osmolarity.
Catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to dihydrosphingosine (DHS).
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. IF-2 subfamily.
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
Substantially reduces production of fusaric acid (PubMed:25372119).
Transcription factor that is involved in the formation of the two Fusaric acid derivatives, dehydrofusaric acid and fusarinolic acid, serving as a detoxification mechanism (By similarity).
Belongs to the BPG-independent phosphoglycerate mutase family.
Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. YchF/OLA1 subfamily.
Hydrolyzes ATP, and can also hydrolyze GTP with lower efficiency. Has lower affinity for GTP.
Belongs to the V-ATPase 116 kDa subunit family.
Essential component of the vacuolar proton pump (V-ATPase), a multimeric enzyme that catalyzes the translocation of protons across the membranes. Required for assembly and activity of the V-ATPase.
Belongs to the class-II DAHP synthase family.
Belongs to the universal ribosomal protein uS19 family.
Belongs to the eukaryotic ribosomal protein eS6 family.
Belongs to the eukaryotic ribosomal protein eL18 family.
Belongs to the NAD(P)-dependent epimerase/dehydratase family. Dihydroflavonol-4-reductase subfamily.
Leads to a strong reduction by at least 90% of the production of fumonisins B1, B2, B3 and B4, and accumulates 3-keto homologs of fumonisins B3 and B4 (PubMed:12720383).
NAD-dependent epimerase/dehydratase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), and B4 (FB4), which are carcinogenic mycotoxins (PubMed:12620260, PubMed:12720383, PubMed:15969533). On the basis of the chemical structures of fumonisins and precursor feeding studies, fumonisin biosynthesis is predicted to include at least five groups of biochemical reactions: synthesis of a linear polyketide with a single terminal carbonyl function and methyl groups at C-10 and C-14; condensation of the polyketide with alanine; reduction of the polyketide carbonyl to a hydroxyl; hydroxylation of 2-4 polyketide carbons; and esterification of six-carbon tricarboxylic acids to two of the hydroxyls (PubMed:12620260). The biosynthesis starts with the polyketide synthase FUM1-catalyzed carbon chain assembly from one molecule of acetyl CoA, eight molecules of malonyl CoA, and two molecules of methionine (PubMed:10413619). The C-18 polyketide chain is released from the enzyme by a nucleophilic attack of a carbanion, which is derived from R-carbon of alanine by decarboxylation, on the carbonyl carbon of polyketide acyl chain (PubMed:15137825, PubMed:12720383). This step is catalyzed by a pyridoxal 5'-phosphate-dependent aminoacyl transferase FUM8 (PubMed:15137825, PubMed:12720383). The resultant 3-keto intermediate 2-amino-3-oxo-12,16-dimethylicosane is then stereospecifically reduced to the 3-hydroxyl product 2-amino-3-hydroxy-12,16-dimethylicosane by reductase FUM13 (PubMed:12720383, PubMed:15137825). Subsequent oxidations at C-5, C-10, C-14 and C-15 followed by tricarballylic esterification of the hydroxyl groups on C-14 and C-15 furnish the biosynthesis of fumonisins (PubMed:15066782, PubMed:15137825, PubMed:16489749). The C-10 hydroxylation is performed by the cytochrome P450 monooxygenase FUM2 and occurs early in the biosynthesis (PubMed:16536629). The C-5 hydroxylation is performed by the dioxygenase FUM3 and occurs late in the biosynthesis (PubMed:20237561, PubMed:15066782, PubMed:15137825, PubMed:16536629). Cytochrome P450 monooxygenases FUM6 and FUM15 may be responsible for the two remaining hydroxylations at positions C-14 and C-15 (PubMed:12620260). The FUM11 tricarboxylate transporter makes a tricarboxylic acid precursor available for fumonisin biosynthesis via its export from the mitochondria (PubMed:12620260). If the precursor is citrate, the FUM7 dehydrogenase could remove the C-3 hydroxyl of citrate to form tricarballylic acid either before or after the CoA activation by the FUM10 acyl-CoA synthetase and FUM14 catalyzed esterification of CoA-activated tricarballylic acid to the C-14 and C-15 hydroxyls of the fumonisin backbone (PubMed:16489749, PubMed:17147424). Alternatively, if the precursor is cis-aconitate, FUM7 may function to reduce the double bond (PubMed:17147424). In this alternate proposal, feeding studies with tetradehydro-fumonisin B1 suggests that FUM7 cannot function on the tricarballylic ester and must therefore act before the FUM14-mediated esterification (PubMed:17147424).
Belongs to the peptidase M24 family. SPT16 subfamily.
Essential for the assembly of ubiquinol-cytochrome c reductase. It has a direct effect on the correct occurrence of the Rieske protein, core 4, core 5 and apocytochrome b.
Belongs to the HAD-like hydrolase superfamily. MasA/MtnC family.
Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Belongs to the universal ribosomal protein uL13 family.
Belongs to the proteasome subunit S3 family.
Required for mitochondrial cytochrome c oxidase (COX) assembly and respiration.
Belongs to the dynactin subunits 5/6 family. Dynactin subunit 6 subfamily.
Belongs to the AAA ATPase family. RarA/MGS1/WRNIP1 subfamily.
Belongs to the fructosamine kinase family.
Belongs to the SRP receptor beta subunit family.
Belongs to the bleomycin resistance protein family.
Belongs to the metallo-beta-lactamase superfamily. RNA-metabolizing metallo-beta-lactamase-like family. CPSF2/YSH1 subfamily.
Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to cysteines occuring in specific C-terminal amino acid sequences.
Heterohexamer; composed of 3 copies of TIM8 and 3 copies of TIM13, named soluble 70 kDa complex. Associates with the TIM22 complex, whose core is composed of TIM22 and TIM54. Interacts with the transmembrane regions of multi-pass transmembrane proteins in transit.
Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. The TIM8-TIM13 complex is non essential and only mediates the import of few proteins, while the predominant TIM9-TIM10 70 kDa complex is crucial and mediates the import of much more proteins.
The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space.
Belongs to the complex I NDUFS4 subunit family.
This promotes the activity of RNA polymerase II.
Component of the ribosome quality control complex (RQC).
E3 ubiquitin-protein ligase. Component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation.
Belongs to the IPP isomerase type 1 family.
Required for pre-18S rRNA processing. May bind microtubules.
Hydrolase that can remove conjugated ubiquitin from proteins and may therefore play an important regulatory role at the level of protein turnover by preventing degradation.
Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.
Belongs to the WD repeat WDR12/YTM1 family.
Component of the SWR1 chromatin remodeling complex.
Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. Involved in chromosome stability.
Belongs to the ketol-acid reductoisomerase family.
Belongs to the DNA repair enzymes AP/ExoA family.
Belongs to the proteasome inhibitor PI31 family.
Plays an important role in control of proteasome function. Inhibits the hydrolysis of protein and peptide substrates by the 20S proteasome. Also inhibits the activation of the proteasome by the proteasome regulatory proteins PA700 and PA28.
In the N-terminal section; belongs to the HesA/MoeB/ThiF family. UBA4 subfamily.
Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers urm1 and MOCS2A. Its N-terminus first activates urm1 and MOCS2A as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to urm1 and MOCS2A to form thiocarboxylation (-COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards urm1 and MOCS2A. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; nfs1 probably acting as a sulfur donor for thiocarboxylation reactions.
In the C-terminal section; belongs to the DHPS family.
Belongs to the very long-chain fatty acids dehydratase HACD family.
Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.
Expression is positively regulated by the fumonisin gene cluster-specific transcription regulator FUM21 (PubMed:17483290). Expression is increased under histone deacetylase (HDAC)-inhibiting conditions (PubMed:22117026). Expression is strongly reduced by benomyl (PubMed:25217721).
Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), and B4 (FB4), which are carcinogenic mycotoxins (PubMed:10413619, PubMed:12620260). On the basis of the chemical structures of fumonisins and precursor feeding studies, fumonisin biosynthesis is predicted to include at least five groups of biochemical reactions: synthesis of a linear polyketide with a single terminal carbonyl function and methyl groups at C-10 and C-14; condensation of the polyketide with alanine; reduction of the polyketide carbonyl to a hydroxyl; hydroxylation of 2-4 polyketide carbons; and esterification of six-carbon tricarboxylic acids to two of the hydroxyls (PubMed:12620260). The biosynthesis starts with the polyketide synthase FUM1-catalyzed carbon chain assembly from one molecule of acetyl CoA, eight molecules of malonyl CoA, and two molecules of methionine (PubMed:10413619). The C-18 polyketide chain is released from the enzyme by a nucleophilic attack of a carbanion, which is derived from R-carbon of alanine by decarboxylation, on the carbonyl carbon of polyketide acyl chain (PubMed:15137825, PubMed:12720383). This step is catalyzed by a pyridoxal 5'-phosphate-dependent aminoacyl transferase FUM8 (PubMed:15137825, PubMed:12720383). The resultant 3-keto intermediate 2-amino-3-oxo-12,16-dimethylicosane is then stereospecifically reduced to the 3-hydroxyl product 2-amino-3-hydroxy-12,16-dimethylicosane by reductase FUM13 (PubMed:12720383, PubMed:15137825). Subsequent oxidations at C-5, C-10, C-14 and C-15 followed by tricarballylic esterification of the hydroxyl groups on C-14 and C-15 furnish the biosynthesis of fumonisins (PubMed:15066782, PubMed:15137825, PubMed:16489749). The C-10 hydroxylation is performed by the cytochrome P450 monooxygenase FUM2 and occurs early in the biosynthesis (PubMed:16536629). The C-5 hydroxylation is performed by the dioxygenase FUM3 and occurs late in the biosynthesis (PubMed:20237561, PubMed:15066782, PubMed:15137825, PubMed:16536629). Cytochrome P450 monooxygenases FUM6 and FUM15 may be responsible for the two remaining hydroxylations at positions C-14 and C-15 (PubMed:12620260). The FUM11 tricarboxylate transporter makes a tricarboxylic acid precursor available for fumonisin biosynthesis via its export from the mitochondria (PubMed:12620260). If the precursor is citrate, the FUM7 dehydrogenase could remove the C-3 hydroxyl of citrate to form tricarballylic acid either before or after the CoA activation by the FUM10 acyl-CoA synthetase and FUM14 catalyzed esterification of CoA-activated tricarballylic acid to the C-14 and C-15 hydroxyls of the fumonisin backbone (PubMed:16489749, PubMed:17147424). Alternatively, if the precursor is cis-aconitate, FUM7 may function to reduce the double bond (PubMed:17147424). In this alternate proposal, feeding studies with tetradehydro-fumonisin B1 suggests that FUM7 cannot function on the tricarballylic ester and must therefore act before the FUM14-mediated esterification (PubMed:17147424).
Impairs the production of fumonisins but does not affect maize ear rot and ear infection (PubMed:10413619, PubMed:12423021, PubMed:15137825).
Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.
Belongs to the proteasome subunit S2 family.
Belongs to the WD repeat striatin family.
Belongs to the bacterial ribosomal protein bL12 family.
Acts as component of the peripheral membrane COG complex that is involved in intra-Golgi protein trafficking. COG is located at the cis-Golgi, and regulates tethering of retrograde intra-Golgi vesicles and possibly a number of other membrane trafficking events.
Component of the conserved oligomeric Golgi complex.
Belongs to the Mediator complex subunit 14 family.
Belongs to the V-ATPase F subunit family.
Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments.
V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'', d, e, f and VOA1).
V-ATPase is a heteromultimeric enzyme made up of two complexes: the ATP-hydrolytic V1 complex and the proton translocation V0 complex.
Belongs to the TtcA family. CTU1/NCS6/ATPBD3 subfamily.
Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. It is unclear whether it acts as a sulfurtransferase that transfers sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. May also be involved in protein urmylation.
Belongs to the plant rapid alkalinization factor (RALF) family.
Part of a SCF (SKP1-cullin-F-box) protein ligase complex.
Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis.
Belongs to the glutamate synthase family.
Belongs to the scytalone dehydratase family.
Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), and B4 (FB4), which are carcinogenic mycotoxins (PubMed:16536629, PubMed:12620260). On the basis of the chemical structures of fumonisins and precursor feeding studies, fumonisin biosynthesis is predicted to include at least five groups of biochemical reactions: synthesis of a linear polyketide with a single terminal carbonyl function and methyl groups at C-10 and C-14; condensation of the polyketide with alanine; reduction of the polyketide carbonyl to a hydroxyl; hydroxylation of 2-4 polyketide carbons; and esterification of six-carbon tricarboxylic acids to two of the hydroxyls (PubMed:12620260). The biosynthesis starts with the polyketide synthase FUM1-catalyzed carbon chain assembly from one molecule of acetyl CoA, eight molecules of malonyl CoA, and two molecules of methionine (PubMed:10413619). The C-18 polyketide chain is released from the enzyme by a nucleophilic attack of a carbanion, which is derived from R-carbon of alanine by decarboxylation, on the carbonyl carbon of polyketide acyl chain (PubMed:15137825, PubMed:12720383). This step is catalyzed by a pyridoxal 5'-phosphate-dependent aminoacyl transferase FUM8 (PubMed:15137825, PubMed:12720383). The resultant 3-keto intermediate 2-amino-3-oxo-12,16-dimethylicosane is then stereospecifically reduced to the 3-hydroxyl product 2-amino-3-hydroxy-12,16-dimethylicosane by reductase FUM13 (PubMed:12720383, PubMed:15137825). Subsequent oxidations at C-5, C-10, C-14 and C-15 followed by tricarballylic esterification of the hydroxyl groups on C-14 and C-15 furnish the biosynthesis of fumonisins (PubMed:15066782, PubMed:15137825, PubMed:16489749). The C-10 hydroxylation is performed by the cytochrome P450 monooxygenase FUM2 and occurs early in the biosynthesis (PubMed:16536629). The C-5 hydroxylation is performed by the dioxygenase FUM3 and occurs late in the biosynthesis (PubMed:20237561, PubMed:15066782, PubMed:15137825, PubMed:16536629). Cytochrome P450 monooxygenases FUM6 and FUM15 may be responsible for the two remaining hydroxylations at positions C-14 and C-15 (PubMed:12620260). The FUM11 tricarboxylate transporter makes a tricarboxylic acid precursor available for fumonisin biosynthesis via its export from the mitochondria (PubMed:12620260). If the precursor is citrate, the FUM7 dehydrogenase could remove the C-3 hydroxyl of citrate to form tricarballylic acid either before or after the CoA activation by the FUM10 acyl-CoA synthetase and FUM14 catalyzed esterification of CoA-activated tricarballylic acid to the C-14 and C-15 hydroxyls of the fumonisin backbone (PubMed:16489749, PubMed:17147424). Alternatively, if the precursor is cis-aconitate, FUM7 may function to reduce the double bond (PubMed:17147424). In this alternate proposal, feeding studies with tetradehydro-fumonisin B1 suggests that FUM7 cannot function on the tricarballylic ester and must therefore act before the FUM14-mediated esterification (PubMed:17147424).
Produces only fumonisins B2 and B4, both of which lack the C-10 hydroxyl (PubMed:16536629).
Belongs to the splicing factor SR family.
This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
Assembly factor required for Rieske Fe-S protein RIP1 incorporation into the cytochrome b-c1 (CIII) complex. Functions as a chaperone, binding to this subunit within the mitochondrial matrix and stabilizing it prior to its translocation and insertion into the late CIII dimeric intermediate within the mitochondrial inner membrane. Modulates the mitochondrial matrix zinc pool.
Belongs to the complex I LYR family. MZM1 subfamily.
Belongs to the proteasome subunit S5A family.
Component of the SPT4-SPT5 complex. Interacts with RNA polymerase II.
IMP-specific 5'-nucleotidase involved in IMP (inositol monophosphate) degradation.
Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PDPK1 subfamily.
Belongs to the deoxyhypusine hydroxylase family.
Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-lysine intermediate to form hypusine, an essential post-translational modification only found in mature eIF-5A factor.
Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.
Belongs to the cyclin family. Cyclin C subfamily.
The GINS complex plays an essential role in the initiation of DNA replication. Has a role in chromosome segregation.
Belongs to the eukaryotic ribosomal protein eL20 family.
Adds the second glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(1)Man(9)GlcNAc(2)-PP-Dol.
Belongs to the mitochondrion-specific ribosomal protein mS29 family.
Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. MOCOS subfamily.
Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form.
Belongs to the thiamine pyrophosphokinase family.
Belongs to the eukaryotic ribosomal protein eS1 family.
Component of the small ribosomal subunit. Mature ribosomes consist of a small (40S) and a large (60S) subunit. The 40S subunit contains about 33 different proteins and 1 molecule of RNA (18S). The 60S subunit contains about 49 different proteins and 3 molecules of RNA (25S, 5.8S and 5S).
Belongs to the 2H phosphoesterase superfamily. USB1 family.
Phosphodiesterase responsible for the U6 snRNA 3' end processing. Acts as an exoribonuclease (RNase) responsible for trimming the poly(U) tract of the last nucleotides in the pre-U6 snRNA molecule, leading to the formation of mature U6 snRNA.
Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3.
DEAD-box RNA helicase-like protein required for pre-18S rRNA processing, specifically at sites A0, A1, and A2.
Belongs to the galactose-1-phosphate uridylyltransferase type 1 family.
Ubiquitin-protein ligase which is mainly involved pre-mRNA splicing and DNA repair. Required for pre-mRNA splicing as component of the spliceosome.
Belongs to the V-ATPase H subunit family.
Belongs to the complex I 23 kDa subunit family.
Belongs to the MPDU1 (TC 2.A.43.3) family.
Belongs to the eIF-2B alpha/beta/delta subunits family.
Component of the small ribosomal subunit, ribosomal RNA processing complex (SSU RRP complex).
Required for small ribosomal subunit (SSU) synthesis. Has a role in the processing of early nucleolar and late cytoplasmic pre-RNA species.
Component of the ER-mitochondria encounter structure (ERMES) or MDM complex, composed of MMM1, MDM10, MDM12 and MDM34. Associates with the mitochondrial outer membrane sorting assembly machinery SAM(core) complex.
Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. MDM10 is involved in the late assembly steps of the general translocase of the mitochondrial outer membrane (TOM complex). Functions in the TOM40-specific route of the assembly of outer membrane beta-barrel proteins, including the association of TOM40 with the receptor TOM22 and small TOM proteins. Can associate with the SAM(core) complex as well as the MDM12-MMM1 complex, both involved in late steps of the major beta-barrel assembly pathway, that is responsible for biogenesis of all outer membrane beta-barrel proteins. May act as a switch that shuttles between both complexes and channels precursor proteins into the TOM40-specific pathway. Plays a role in mitochondrial morphology and in the inheritance of mitochondria.
Lacks alpha-helical transmembrane segments, suggesting that it resides in the membrane via beta-sheet conformations similar to those predicted for other outer membrane proteins and porin.
Belongs to the eukaryotic ribosomal protein eL38 family.
Belongs to the class I-like SAM-binding methyltransferase superfamily. EFM5 family.
S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that trimethylates elongation factor 1-alpha at 'Lys-79'.
Belongs to the NiCoT transporter (TC 2.A.52) family.
Belongs to the enhancer of polycomb family.
Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair. Involved in gene silencing by neighboring heterochromatin, blockage of the silencing spreading along the chromosome, and required for cell cycle progression through G2/M.
Belongs to the myo-inositol oxygenase family.
Recruits the lipid transfer protein VPS13 to endosomal and vacuolar membranes.
Functions as a component of the DNA-binding general transcription factor complex TFIID and the transcription regulatory histone acetylation (HAT) complexes SAGA and SLIK. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation), facilitation of DNA opening and initiation of transcription. SAGA is required for recruitment of the basal transcription machinery. SLIK is proposed to have partly overlapping functions with SAGA.
Involved in the regulation of telomere length, clustering and has a specific role in telomere position effect (TPE).
Has a role in transport between endoplasmic reticulum and Golgi.
Intracellular phospholipase B that catalyzes the double deacylation of phosphatidylcholine (PC) to glycerophosphocholine (GroPCho). Plays an important role in membrane lipid homeostasis. Responsible for the rapid PC turnover in response to inositol, elevated temperatures, or when choline is present in the growth medium.
Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily.
Binds 1 thiamine pyrophosphate per subunit.
Belongs to the DNA polymerase type-Y family.
Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents.
Belongs to the fungal fatty acid synthetase subunit beta family.
The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex.
Belongs to the glycosyltransferase group 1 family.
Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate.
Belongs to the uroporphyrinogen decarboxylase family.
Belongs to the complex I NDUFA2 subunit family.
Heterodimer with ALG14 to form a functional enzyme.
Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway.
Plays a role in U6 snRNP assembly and function. Binds to the 3' end of U6 snRNA.
Belongs to the alpha-acetolactate decarboxylase family.
Belongs to the terpene cyclase/mutase family.
Belongs to the V-ATPase E subunit family.
Belongs to the DNA mismatch repair MutS family.
Belongs to the complex I 30 kDa subunit family.
Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C (PubMed:17121404, PubMed:22652150). Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production (By similarity). The roles of the other FUS members are yet undetermined (By similarity). The fusarin C synthetase FUS1 is responsible for the condensation of one acetyl-coenzyme A (CoA) unit with six malonyl-CoA units and the amide linkage of the arising heptaketide and homoserine, subsequently releasing the first intermediate, prefusarin, as an alcohol with an open ring structure (PubMed:17121404). The cytochrome P450 monooxygenase FUS8 participates in multiple oxidation processes at carbon C-20 and is able to use the FUS1 product as substrate, resulting in formation of 20-hydroxy-prefusarin (By similarity). This reaction seems to be essential before the 2-pyrrolidone ring closure can be catalyzed by FUS2, generating 20-hydroxy-fusarin (By similarity). FUS8 is able to further oxidizes carbon C-20 after ring closure, resulting in the formation of carboxy-fusarin C (By similarity). As the last step, FUS9 methylates the hydroxyl group at C-21 to generate fusarin C (By similarity). Fusarin C can then rearrange to epi-fusarin C, the (z)-isomers, and fusarin A and fusarin D (By similarity).
Component of the general transcription and DNA repair factor IIH (TFIIH) core complex which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA.
Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module TFIIK controls the initiation of transcription.
May function both as a monomer and a homodimer.
Fusarium verticillioides possesses 2 unlinked loci, FDB1 and FDB2, necessary for detoxification of antimicrobial compounds produced by maize, including 2-benzoxazolinone (BOA) (PubMed:26808652). The FDB2 cluster arose as a duplication of the FDB1 cluster with rearrangement and expansion by incorporating additional genes (Probable).
Gamma-lactamase; part of the Fusarium detoxification of benzoxazolinone cluster 1 (FDB1) involved in the degradation of benzoxazolinones produced by the host plant (PubMed:19302487, PubMed:26808652). Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their inherent instability once released, spontaneously degrade to the more stable corresponding benzoxazolinones, 6-methoxy-2-benzoxazolinone (MBOA) and 2-benzoxazolinone (BOA), respectively (PubMed:11876429). The first step in the detoxification of benzoxazolinones involves the hydrolysis of the cyclic ester bond of benzoxazolinones by the FDB1 cluster gamma-lactamase MBL1 to aminophenols (PubMed:26808652, PubMed:12788712). MBL1 is able to convert BOA into 2-aminophenol (2-AP), as well as MBOA into 5-methoxy-2-aminophenol (2-AMP) (PubMed:26808652, PubMed:12788712). The FDB2 cluster N-malonyltransferase FDB2/NAT1 then metabolizes aminophenols via N-malonylation to non-toxic malonamic acids (PubMed:19302487, PubMed:12788712). FDB2/NAT1 converts 2-AP into N-(2-hydroxyphenyl) malonamic acid (HPMA) and 2-AMP into N-(2-hydroxy-4-methoxyphenyl) malonamic acid (HMPMA) (PubMed:19302487, PubMed:12788712). The duplicated dienlactone hydrolases DLH1 and DLH2 may provide redundant function for hydrolyzing the lactone moiety in the BOA molecule (Probable). The roles of the amidases and other enzymes encoded by the 2 FDB clusters have not been identified so far (Probable).
Impairs the ability to of metabolize 2-benzoxazolinone (BOA) and thus growth BOA-amended media.
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex.
Involved in the small subunit (SSU) processome assembly and function, and in the 18S rRNA synthesis. Required for the early cleavages at sites A0, A1 and A2.
Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB) and recruits ESCRT-I to the MVB outer membrane.
Belongs to the glycosyl hydrolase 13 family.
Involved in the organization of the mitochondrial membranes and the global structure of the mitochondria. Also required for mitochondrial distribution and mobility as well as for the maintenance of mitochondrial DNA nucleoids structures.
Belongs to the eukaryotic/archaeal RNase P protein component 3 family.
Transcriptional coactivator that stimulates transcriptional activity by bridging regulatory proteins and TBP, thereby recruiting TBP to promoters occupied by DNA-binding regulators.
Involved in the lipid remodeling steps of GPI-anchor maturation.
Belongs to the bacterial ribosomal protein bS6 family.
Belongs to the Mediator complex subunit 9 family.
Belongs to the neutral sphingomyelinase family.
Belongs to the membrane magnesium transporter (TC 1.A.67) family.
May be involved in calcium-mediated signal transduction.
Belongs to the purine/pyrimidine phosphoribosyltransferase family.
Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks.
Belongs to the bacterial ribosomal protein bS16 family.
Belongs to the clathrin heavy chain family.
Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins.
Belongs to the cAMP-dependent kinase regulatory chain family.
Tetramer, composed of 2 regulatory (R) and 2 catalytic (C) subunits. In the presence of cAMP it dissociates into 2 active monomeric C subunits and an R dimer.
Belongs to the glycerate kinase type-1 family.
Belongs to the NFYB/HAP3 subunit family.
Belongs to the snRNP Sm proteins family. SmF/LSm6 subfamily.
Component of the peroxisomal translocation machinery.
Belongs to the SMC family. SMC1 subfamily.
Belongs to the acetyl-CoA hydrolase/transferase family.
Belongs to the major facilitator superfamily.
MFS-type transporter; part of the Fusarium detoxification of benzoxazolinone cluster 1 (FDB1) involved in the degradation of benzoxazolinones produced by the host plant (PubMed:19302487, PubMed:26808652). Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their inherent instability once released, spontaneously degrade to the more stable corresponding benzoxazolinones, 6-methoxy-2-benzoxazolinone (MBOA) and 2-benzoxazolinone (BOA), respectively (PubMed:11876429).
DNA helicase participates in several chromatin remodeling complexes, including the SWR1 and the INO80 complexes.
Belongs to the ubiquitin conjugation factor E4 family.
Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly.
Interacts with histone H3 and histone H4.
Belongs to the ETF beta-subunit/FixA family.
Belongs to the PpiC/parvulin rotamase family. PIN4 subfamily.
Belongs to the complex I 49 kDa subunit family.
Component of the homotypic vacuole fusion and vacuole protein sorting (HOPS) complex. Component of the class C core vacuole/endosome tethering (CORVET) complex.
Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER). The SRP complex interacts with the signal sequence in nascent secretory and membrane proteins and directs them to the membrane of the ER.
Responsible for the formation of the pyrimidine heterocycle in the thiamine biosynthesis pathway. Catalyzes the formation of hydroxymethylpyrimidine phosphate (HMP-P) from histidine and pyridoxal phosphate (PLP). The protein uses PLP and the active site histidine to form HMP-P, generating an inactive enzyme. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme.
Component of the cleavage factor I (CF I) involved in pre-mRNA 3'-end processing.
Component of the coenzyme Q biosynthetic pathway. May play a role in organizing a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis. Required for steady-state levels of other COQ polypeptides.
Belongs to the V-ATPase e1/e2 subunit family.
Belongs to the universal ribosomal protein uS3 family.
Belongs to the bacterial ribosomal protein bL28 family.
FUS1 is an unusual polyketide synthase (PKS) fused to a non-ribosomal peptide synthetase (NRPS) module to form a megasynthetase.
Fusarin C synthetase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C (PubMed:17121404, PubMed:22652150). Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production (By similarity). The roles of the other FUS members are yet undetermined (By similarity). The fusarin C synthetase FUS1 is responsible for the condensation of one acetyl-coenzyme A (CoA) unit with six malonyl-CoA units and the amide linkage of the arising heptaketide and homoserine, subsequently releasing the first intermediate, prefusarin, as an alcohol with an open ring structure (PubMed:17121404). The cytochrome P450 monooxygenase FUS8 participates in multiple oxidation processes at carbon C-20 and is able to use the FUS1 product as substrate, resulting in formation of 20-hydroxy-prefusarin (By similarity). This reaction seems to be essential before the 2-pyrrolidone ring closure can be catalyzed by FUS2, generating 20-hydroxy-fusarin (By similarity). FUS8 is able to further oxidizes carbon C-20 after ring closure, resulting in the formation of carboxy-fusarin C (By similarity). As the last step, FUS9 methylates the hydroxyl group at C-21 to generate fusarin C (By similarity). Fusarin C can then rearrange to epi-fusarin C, the (z)-isomers, and fusarin A and fusarin D (By similarity).
Impairs the production of fusarin C (PubMed:22652150).
Autophagy-specific protein that functions in response to autophagy-inducing signals as a scaffold to recruit other ATG proteins to organize preautophagosomal structure (PAS) formation. Modulates the timing and magnitude of the autophagy response, such as the size of the sequestering vesicles. Plays particularly a role in pexophagy and nucleophagy.
Accepts electrons from ETF and reduces ubiquinone.
Belongs to the PPP phosphatase family. PP-5 (PP-T) subfamily.
Belongs to the mitochondrial Rho GTPase family.
Mitochondrial GTPase involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution.
Belongs to the protein kinase superfamily. ADCK protein kinase family.
Necessary for the splicing of pre-mRNA. Has a role in the recognition of the branch site (5'-UACUAAC-3'), the pyrimidine tract and the 3'-splice site at the 3'-end of introns.
Non-catalytic subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments.
V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex attached to an integral membrane V0 proton pore complex.
Involved in cell fusion during mating by stabilizing the plasma membrane fusion event.
Belongs to the eukaryotic AdoMetDC family.
Required for multiple vacuole delivery pathways including the cytoplasm to vacuole transport (Cvt), autophagy, pexophagy and endocytosis.
Belongs to the eukaryotic release factor 1 family.
Belongs to the Rieske iron-sulfur protein family.
The Rieske protein is a high potential 2Fe-2S protein.
Catalytic subunit in the complex catalyzing the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis.
Component of the mitochondrial large ribosomal subunit. Mature mitochondrial ribosomes consist of a small (37S) and a large (54S) subunit. The 37S subunit contains at least 33 different proteins and 1 molecule of RNA (15S). The 54S subunit contains at least 45 different proteins and 1 molecule of RNA (21S).
Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. GSK-3 subfamily.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIIA subfamily.
The plasma membrane ATPase of plants and fungi is a hydrogen ion pump. The proton gradient it generates drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses.
Belongs to the universal ribosomal protein uL14 family.
Belongs to the WD repeat IPI3/WDR18 family.
Component of the RIX1 complex, composed of IPI1, RIX1/IPI2 and IPI3 in a 1:2:2 stoichiometry. The complex interacts (via RIX1) with MDN1 (via its hexameric AAA ATPase ring) and the pre-60S ribosome particles.
Required for correct functioning of the GINS complex, a complex that plays an essential role in the initiation of DNA replication, and progression of DNA replication forks. GINS complex seems to bind preferentially to single-stranded DNA.
Belongs to the PPP phosphatase family. PP-2B subfamily.
Composed of two components (A and B), the A component is the catalytic subunit and the B component confers calcium sensitivity.
Belongs to the eukaryotic ribosomal protein eL37 family.
Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Belongs to the phosphosulfolactate synthase family.
Belongs to the mitochondrion-specific ribosomal protein mL46 family.
Belongs to the LIMR family. LMBRD1 subfamily.
Probable lysosomal cobalamin transporter. Required to export cobalamin from lysosomes allowing its conversion to cofactors.
Adds the eighth mannose residue in an alpha-1,6 linkage onto the dolichol-PP-oligosaccharide precursor (dolichol-PP-Man(7)GlcNAc(2)) required for protein glycosylation.
May act as a negative regulator of salt tolerance.
Required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus.
Belongs to the WD repeat LIS1/nudF family.
Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for nuclear migration during vegetative growth as well as development. Required for retrograde early endosome (EE) transport from the hyphal tip. Required for localization of dynein to the mitotic spindle poles. Recruits additional proteins to the dynein complex at SPBs.
Self-associates. Interacts with NDL1 and dynein.
Glutathione S-transferase-like protein; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C (PubMed:22652150). Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production (By similarity). The other FUS cluster members are not essential for fusarin C biosynthesis (By similarity).
Belongs to the GTP cyclohydrolase I type 2/NIF3 family.
Belongs to the FAD-dependent glycerol-3-phosphate dehydrogenase family.
Required for proper folding and/or the stability of a subset of proteins in the endoplasmic reticulum. Component of glycosylphosphatidylinositol-mannosyltransferase 1 which transfers the first of the 4 mannoses in the GPI-anchor precursors during GPI-anchor biosynthesis. Probably acts by stabilizing the mannosyltransferase GPI14.
Belongs to the aldo/keto reductase family. Glutamate--cysteine ligase light chain subfamily.
Heterodimer of a catalytic heavy chain and a regulatory light chain.
Component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner.
Belongs to the myo-inositol 1-phosphate synthase family.
Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.
Belongs to the ubiquitin-conjugating enzyme family. UEV subfamily.
Belongs to the eukaryotic ribosomal protein eL31 family.
Nuclear chaperone required for maturation and nuclear export of pre-60S ribosome subunits.
Belongs to the prefoldin subunit alpha family.
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Involved in ribosomal large subunit assembly.
Belongs to the glycosyltransferase 8 family.
Belongs to the Tim17/Tim22/Tim23 family.
Essential core component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. In the TIM22 complex, it constitutes the voltage-activated and signal-gated channel. Forms a twin-pore translocase that uses the membrane potential as external driving force in 2 voltage-dependent steps.
Belongs to the actin-binding proteins ADF family. GMF subfamily.
Belongs to the fatty acid desaturase type 1 family.
Expected to bind 2 Fe(2+) ions per subunit.
Stearoyl-CoA desaturase that utilizes O(2) and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates.
Belongs to the diphthine synthase family.
S-adenosyl-L-methionine-dependent methyltransferase that catalyzes four methylations of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine methyl ester. The four successive methylation reactions represent the second step of diphthamide biosynthesis.
Belongs to the GTP cyclohydrolase I family.
In the C-terminal section; belongs to the formate--tetrahydrofolate ligase family.
In the N-terminal section; belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.
Belongs to the uracil-DNA glycosylase (UDG) superfamily. UNG family.
Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
Belongs to the acid sphingomyelinase family.
Belongs to the eukaryotic NMN adenylyltransferase family.
Belongs to the histone deacetylase family. HD type 2 subfamily.
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events.
Belongs to the chaperonin (HSP60) family.
Belongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. Eukaryotic type I sub-subfamily.
Binds 1 pyruvoyl group covalently per subunit.
Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine.
Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit.
Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase.
Mitogen-activated protein kinase involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment. Controls osmotic regulation of transcription of target genes.
Belongs to the SMC family. SMC2 subfamily.
Belongs to the glycosyl hydrolase 54 family.
Required for the first step of diphthamide biosynthesis, the transfer of 3-amino-3-carboxypropyl from S-adenosyl-L-methionine to a histidine residue. Diphthamide is a post-translational modification of histidine which occurs in elongation factor 2.
Belongs to the HMG-CoA reductase family.
Belongs to the carotenoid/retinoid oxidoreductase family.
Belongs to the CWC16 family. YJU2 subfamily.
Component of the spliceosome. Present in the activated B complex, the catalytically activated B* complex which catalyzes the branching, the catalytic step 1 C complex catalyzing the exon ligation, and the postcatalytic P complex containing the ligated exons (mRNA) and the excised lariat intron.
Part of the spliceosome which catalyzes two sequential transesterification reactions, first the excision of the non-coding intron from pre-mRNA and then the ligation of the coding exons to form the mature mRNA. Plays a role in stabilizing the structure of the spliceosome catalytic core and docking of the branch helix into the active site, producing 5'-exon and lariat intron-3'-intermediates.
Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3. Interacts with snoRNA U3. Interacts with MPP10, KRI1 and with ribosomal proteins RPS1A, RPS4A, RPS4B, RPS8A, RPS8B, RPS11A, RPS11B, RPS13, RPS24, RPS25, RPL4A, RPL7B, RPL8, RPL23, RPL25 and RPL28.
Required for 40S ribosome biogenesis. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly. Essential for vegetative growth.
Belongs to the STE12 transcription factor family.
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
Belongs to the aromatic-ring hydroxylase family. KMO subfamily.
Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid.
Impairs the production of fusaric acid (PubMed:22652150).
Multidomain protein; including a starter unit:ACP transacylase (SAT) that selects the starter unit; a ketosynthase (KS) that catalyzes repeated decarboxylative condensation to elongate the polyketide backbone; a malonyl-CoA:ACP transacylase (MAT) that selects and transfers the extender unit malonyl-CoA; a product template (PT) domain that controls the immediate cyclization regioselectivity of the reactive polyketide backbone; and an acyl-carrier protein (ACP) that serves as the tether of the growing and completed polyketide via its phosphopantetheinyl arm.
Reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties (PubMed:22652150, PubMed:25372119). L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L-homoserine by cluster enzymes aspartate kinase FUB3 and homoserine O-acetyltransferase FUB5, as well as enzymes of the primary metabolism (By similarity). The polyketide synthase (PKS) FUB1 generates the triketide trans-2-hexenal which is presumptively released by the hydrolase FUB4 and linked to the NRPS-bound amino acid precursor by NAD(P)-dependent dehydrogenase FUB6 (By similarity). FUB1, FUB4, and the non-canonical NRPS Fub8 may form an enzyme complex (By similarity). Further processing of the NRPS-bound intermediate might be carried out by FUB6 and the sulfhydrylase FUB7, enabling a spontaneous electrocyclization to close the carbon backbone of fusaric acid (By similarity). Dihydrofusaric acid is likely to be released via reduction by the thioester reductase (TR) domain of FUB8 whereupon the final oxidation to fusaric acid may (also) be performed by the FMN-dependent dehydrogenase FUB9 (By similarity).
Bifunctional cytochrome P450/NADPH--P450 reductase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), and B4 (FB4), which are carcinogenic mycotoxins (PubMed:11728154, PubMed:15137825). On the basis of the chemical structures of fumonisins and precursor feeding studies, fumonisin biosynthesis is predicted to include at least five groups of biochemical reactions: synthesis of a linear polyketide with a single terminal carbonyl function and methyl groups at C-10 and C-14; condensation of the polyketide with alanine; reduction of the polyketide carbonyl to a hydroxyl; hydroxylation of 2-4 polyketide carbons; and esterification of six-carbon tricarboxylic acids to two of the hydroxyls (PubMed:12620260). The biosynthesis starts with the polyketide synthase FUM1-catalyzed carbon chain assembly from one molecule of acetyl CoA, eight molecules of malonyl CoA, and two molecules of methionine (PubMed:10413619). The C-18 polyketide chain is released from the enzyme by a nucleophilic attack of a carbanion, which is derived from R-carbon of alanine by decarboxylation, on the carbonyl carbon of polyketide acyl chain (PubMed:15137825, PubMed:12720383). This step is catalyzed by a pyridoxal 5'-phosphate-dependent aminoacyl transferase FUM8 (PubMed:15137825, PubMed:12720383). The resultant 3-keto intermediate 2-amino-3-oxo-12,16-dimethylicosane is then stereospecifically reduced to the 3-hydroxyl product 2-amino-3-hydroxy-12,16-dimethylicosane by reductase FUM13 (PubMed:12720383, PubMed:15137825). Subsequent oxidations at C-5, C-10, C-14 and C-15 followed by tricarballylic esterification of the hydroxyl groups on C-14 and C-15 furnish the biosynthesis of fumonisins (PubMed:15066782, PubMed:15137825, PubMed:16489749). The C-10 hydroxylation is performed by the cytochrome P450 monooxygenase FUM2 and occurs early in the biosynthesis (PubMed:16536629). The C-5 hydroxylation is performed by the dioxygenase FUM3 and occurs late in the biosynthesis (PubMed:20237561, PubMed:15066782, PubMed:15137825, PubMed:16536629). Cytochrome P450 monooxygenases FUM6 and FUM15 may be responsible for the two remaining hydroxylations at positions C-14 and C-15 (PubMed:12620260). The FUM11 tricarboxylate transporter makes a tricarboxylic acid precursor available for fumonisin biosynthesis via its export from the mitochondria (PubMed:12620260). If the precursor is citrate, the FUM7 dehydrogenase could remove the C-3 hydroxyl of citrate to form tricarballylic acid either before or after the CoA activation by the FUM10 acyl-CoA synthetase and FUM14 catalyzed esterification of CoA-activated tricarballylic acid to the C-14 and C-15 hydroxyls of the fumonisin backbone (PubMed:16489749, PubMed:17147424). Alternatively, if the precursor is cis-aconitate, FUM7 may function to reduce the double bond (PubMed:17147424). In this alternate proposal, feeding studies with tetradehydro-fumonisin B1 suggests that FUM7 cannot function on the tricarballylic ester and must therefore act before the FUM14-mediated esterification (PubMed:17147424).
Belongs to the Mediator complex subunit 16 family.
Delta(8)-fatty-acid desaturase which introduces a double bond at the 8-position in the long-chain base (LCB) of ceramides. Required for the formation of the di-unsaturated sphingoid base (E,E)-sphinga-4,8-dienine during glucosylceramide (GluCer) biosynthesis.
Involved in degradation of plant cell walls. Hydrolyzes the feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl-galactose ester bond in pectin. Active against paranitrophenyl-acetate, methyl ferulate and wheat arabinoxylan.
Belongs to the nucleoporin interacting component (NIC) family.
Belongs to the PIGG/PIGN/PIGO family. PIGG subfamily.
Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the GPI second mannose.
Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily.
Dehydrogenase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties (PubMed:25372119). L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L-homoserine by cluster enzymes aspartate kinase FUB3 and homoserine O-acetyltransferase FUB5, as well as enzymes of the primary metabolism (By similarity). The polyketide synthase (PKS) FUB1 generates the triketide trans-2-hexenal which is presumptively released by the hydrolase FUB4 and linked to the NRPS-bound amino acid precursor by NAD(P)-dependent dehydrogenase FUB6 (By similarity). FUB1, FUB4, and the non-canonical NRPS Fub8 may form an enzyme complex (By similarity). Further processing of the NRPS-bound intermediate might be carried out by FUB6 and the O-acetylhomoserine FUB7, enabling a spontaneous electrocyclization to close the carbon backbone of fusaric acid (By similarity). Dihydrofusaric acid is likely to be released via reduction by the thioester reductase (TR) domain of FUB8 whereupon the final oxidation to fusaric acid may (also) be performed by the FMN-dependent dehydrogenase FUB9 (By similarity).
Reductase; part of the Fusarium detoxification of benzoxazolinone cluster 2 (FDB2) involved in the degradation of benzoxazolinones produced by the host plant (PubMed:19302487, PubMed:26808652). Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their inherent instability once released, spontaneously degrade to the more stable corresponding benzoxazolinones, 6-methoxy-2-benzoxazolinone (MBOA) and 2-benzoxazolinone (BOA), respectively (PubMed:11876429). The first step in the detoxification of benzoxazolinones involves the hydrolysis of the cyclic ester bond of benzoxazolinones by the FDB1 cluster gamma-lactamase MBL1 to aminophenols (PubMed:26808652, PubMed:12788712). MBL1 is able to convert BOA into 2-aminophenol (2-AP), as well as MBOA into 5-methoxy-2-aminophenol (2-AMP) (PubMed:26808652, PubMed:12788712). The FDB2 cluster N-malonyltransferase FDB2/NAT1 then metabolizes aminophenols via N-malonylation to non-toxic malonamic acids (PubMed:19302487, PubMed:12788712). FDB2/NAT1 converts 2-AP into N-(2-hydroxyphenyl) malonamic acid (HPMA) and 2-AMP into N-(2-hydroxy-4-methoxyphenyl) malonamic acid (HMPMA) (PubMed:19302487, PubMed:12788712). The duplicated dienlactone hydrolases DLH1 and DLH2 may provide redundant function for hydrolyzing the lactone moiety in the BOA molecule (Probable). The roles of the amidases an other enzymes encoded by the 2 FDB clusters have not been identified so far (Probable).
FAD-dependent monooxygenase required for the C5-ring hydroxylation during ubiquinone biosynthesis. Catalyzes the hydroxylation of 3-polyprenyl-4-hydroxybenzoic acid to 3-polyprenyl-4,5-dihydroxybenzoic acid. The electrons required for the hydroxylation reaction may be funneled indirectly from NADPH via a ferredoxin/ferredoxin reductase system to COQ6.
Belongs to the class VI-like SAM-binding methyltransferase superfamily. PEMT/PEM2 methyltransferase family.
Catalyzes the second two steps of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylmonomethylethanolamine (PMME) to phosphatidyldimethylethanolamine (PDME) and of PDME to phosphatidylcholine (PC).
Belongs to the eukaryotic-type primase large subunit family.
DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication.
Belongs to the eukaryotic ribosomal protein eS24 family.
Belongs to the class I-like SAM-binding methyltransferase superfamily. mRNA cap 0 methyltransferase family.
In the N-terminal section; belongs to the dsDNA virus mRNA guanylyltransferase family.
Responsible for methylating the 5'-cap structure of mRNAs.
Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome.
Belongs to the eukaryotic ribosomal protein eS12 family.
Belongs to the glucosamine/galactosamine-6-phosphate isomerase family. 6-phosphogluconolactonase subfamily.
Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
Belongs to the methyltransferase superfamily. Fibrillarin family.
Belongs to the 5'-3' exonuclease family.
Multifunctional protein that exhibits several independent functions at different levels of the cellular processes. 5'-3' exonuclease component of the nonsense-mediated mRNA decay (NMD) which is a highly conserved mRNA degradation pathway, an RNA surveillance system whose role is to identify and rid cells of mRNA with premature termination codons and thus prevents accumulation of potentially harmful truncated proteins.
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network.
Belongs to the GTP cyclohydrolase II family.
Belongs to the SSU72 phosphatase family.
Component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. SSU72 is required for 3'-end formation of snoRNAs.
Component of the cleavage and polyadenylation factor (CPF) complex.
Processively dephosphorylates Ser-5 of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit (RPB1).
Belongs to the class I-like SAM-binding methyltransferase superfamily. EFM7 family.
S-adenosyl-L-methionine-dependent protein methyltransferase that trimethylates the N-terminal glycine 'Gly-2' of elongation factor 1-alpha, before also catalyzing the mono- and dimethylation of 'Lys-3'.
Heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter.
Belongs to the mitochondrion-specific ribosomal protein mL53 family.
Component of the ER membrane protein complex (EMC).
Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins.
Belongs to the CND1 (condensin subunit 1) family.
Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases.
Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 2 subfamily.
Belongs to the cytochrome c oxidase subunit 6A family.
Belongs to the F-actin-capping protein alpha subunit family.
Belongs to the mitochondrion-specific ribosomal protein mS33 family.
Belongs to the nonaspanin (TM9SF) (TC 9.A.2) family.
Key component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into apoproteins specifically involved in DNA metabolism and genomic integrity. In the CIA complex, MMS19 acts as an adapter between early-acting CIA components and a subset of cellular target iron-sulfur proteins.
Lipid-binding protein involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration.
Belongs to the eukaryotic ribosomal protein eL27 family.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RMT2 methyltransferase family.
S-adenosyl-L-methionine-dependent protein-arginine N-methyltransferase that methylates the delta-nitrogen atom of arginine residues to form N5-methylarginine (type IV) in target proteins. Monomethylates ribosomal protein L12.
Belongs to the class I-like SAM-binding methyltransferase superfamily. EFM4 family.
S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that mono- and dimethylates elongation factor 1-alpha at 'Lys-316'. May play a role in intracellular transport.
Associates with the pre-60S ribosomal particle.
Component of the ribosome assembly machinery. Nuclear paralog of the ribosomal protein P0, it binds pre-60S subunits at an early stage of assembly in the nucleolus, and is replaced by P0 in cytoplasmic pre-60S subunits and mature 80S ribosomes.
Belongs to the enoyl-CoA hydratase/isomerase family.
Belongs to the oligoribonuclease family.
Belongs to the complex I LYR family. SDHAF1 subfamily.
Stabilizer subunit of the dolichol-phosphate mannose (DPM) synthase complex; tethers catalytic subunit to the ER.
Belongs to the glutaminase PdxT/SNO family.
Sulfhydrylase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties (PubMed:25372119). L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L-homoserine by cluster enzymes aspartate kinase FUB3 and homoserine O-acetyltransferase FUB5, as well as enzymes of the primary metabolism (By similarity). The polyketide synthase (PKS) FUB1 generates the triketide trans-2-hexenal which is presumptively released by the hydrolase FUB4 and linked to the NRPS-bound amino acid precursor by NAD(P)-dependent dehydrogenase FUB6 (By similarity). FUB1, FUB4, and the non-canonical NRPS Fub8 may form an enzyme complex (By similarity). Further processing of the NRPS-bound intermediate might be carried out by FUB6 and the O-acetylhomoserine FUB7, enabling a spontaneous electrocyclization to close the carbon backbone of fusaric acid (By similarity). Dihydrofusaric acid is likely to be released via reduction by the thioester reductase (TR) domain of FUB8 whereupon the final oxidation to fusaric acid may (also) be performed by the FMN-dependent dehydrogenase FUB9 (By similarity).
Small GTPase required for proper nuclear import of RNA polymerase II and III (RNAPII and RNAPIII). May act at an RNAP assembly step prior to nuclear import.
Belongs to the imidazoleglycerol-phosphate dehydratase family.
Belongs to the homoserine dehydrogenase family.
Adaptor protein complex 3 (AP-3) is a heterotetramer.
Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane.
Belongs to the glycosyltransferase 4 family.
Belongs to the phytoene/squalene synthase family.
Catalyzes the condensation of 2 farnesyl pyrophosphate (FPP) moieties to form squalene.
Belongs to the amidase family. GatA subfamily.
Belongs to the UPL family. K-HECT subfamily.
Belongs to the glycosyl hydrolase family 6.
Belongs to the arsenical resistance-3 (ACR3) (TC 2.A.59) family.
Putative RNA polymerase II subunit B1 C-terminal domain (CTD) phosphatase involved in RNA polymerase II transcription regulation.
Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. SETD6 subfamily.
S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that monomethylates 60S ribosomal protein L42.
Belongs to the DNA polymerase type-X family.
Belongs to the peroxisomal targeting signal receptor family.
Binds to the C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type) and plays an essential role in peroxisomal protein import.
Belongs to the universal ribosomal protein uL1 family.
Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family.
Belongs to the gluconokinase GntK/GntV family.
Regulates the cell cycle in a nutrient dependent manner.
Belongs to the Mediator complex subunit 4 family.
Belongs to the protoporphyrinogen/coproporphyrinogen oxidase family. Protoporphyrinogen oxidase subfamily.
Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.
Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations.
Occurs in many kinds of cells as a complex with monomeric actin in a 1:1 ratio.
Belongs to the metallo-dependent hydrolases superfamily. Hydantoinase/dihydropyrimidinase family.
Carbamylation allows a single lysine to coordinate two divalent metal cations.
GTP-binding protein involved in protein trafficking; modulates vesicle budding and uncoating within the Golgi apparatus.
In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.
Allosterically inhibited by 3'-phosphoadenosine 5'-phosphosulfate (PAPS).
Catalyzes the first intracellular reaction of sulfate assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic sulfate and ATP. Plays an important role in sulfate activation as a component of the biosynthesis pathway of sulfur-containing amino acids.
In the C-terminal section; belongs to the APS kinase family.
In the C-terminal section; belongs to the sulfate adenylyltransferase family.
In the N-terminal section; belongs to the APS kinase family.
In the N-terminal section; belongs to the sulfate adenylyltransferase family.
The adenylyl-sulfate kinase (APS kinase) is non-functional. It is involved in allosteric regulation by PAPS. PAPS binding induces a large rotational rearrangement of domains lowering the substrate affinity of the enzyme.
Component of the SWR1 chromatin-remodeling complex and of the NuA4 histone acetyltransferase complex.
Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for an H2A variant leading to transcriptional regulation of selected genes by chromatin remodeling. Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4 and H2A. The NuA4 complex is also involved in DNA repair. Yaf9 may also be required for viability in conditions in which the structural integrity of the spindle is compromised.
The coiled-coil domain is required for assembly into the NuA4 complex.
Belongs to the DNA polymerase epsilon subunit B family.
Required for proper 27S pre-rRNA processing and 60S ribosome subunit assembly.
Component of the ER-mitochondria encounter structure (ERMES) or MDM complex, composed of MMM1, MDM10, MDM12 and MDM34. A MMM1 homodimer associates with one molecule of MDM12 on each side in a pairwise head-to-tail manner, and the SMP-LTD domains of MMM1 and MDM12 generate a continuous hydrophobic tunnel for phospholipid trafficking.
Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. MDM12 is required for the interaction of the ER-resident membrane protein MMM1 and the outer mitochondrial membrane-resident beta-barrel protein MDM10. The MDM12-MMM1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all mitochondrial outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The MDM10-MDM12-MMM1 subcomplex further acts in the TOM40-specific pathway after the action of the MDM12-MMM1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids.
Non-catalytic component of the proteasome.
Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family.
Mediates the transfer of lipids between membranes at organelle contact sites. May play a role in mitochondrial lipid homeostasis.
Essential role in pre-mRNA splicing. Also essential for entry into mitosis (G2/M progression) as well as for chromosome segregation during mitosis.
In the C-terminal section; belongs to the eukaryotic ribosomal protein eL40 family.
In the N-terminal section; belongs to the ubiquitin family.
Belongs to the DEAD box helicase family. DEAH subfamily. DDX15/PRP43 sub-subfamily.
Proteolytically removes the C-terminal three residues of farnesylated proteins.
Belongs to the methyltransferase superfamily. Trimethylguanosine synthase family.
Belongs to the methyltransferase superfamily. L-isoaspartyl/D-aspartyl protein methyltransferase family.
Belongs to the DASH complex DAD4 family.
Belongs to the bacterial ribosomal protein bL32 family.
Belongs to the eukaryotic ribosomal protein eL24 family.
Belongs to the alternative oxidase family.
Catalyzes cyanide-resistant oxygen consumption. May increase respiration when the cytochrome respiratory pathway is restricted, or in response to low temperatures.
Belongs to the complex I NDUFB11 subunit family.
During the catalytic reaction, a sulfide is transferred from Cys-209 to a reaction intermediate, generating a dehydroalanine residue.
During the catalytic reaction, a sulfide is transferred from Cys-316 to a reaction intermediate, generating a dehydroalanine residue.
Involved in biosynthesis of the thiamine precursor thiazole. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid (ADT), an adenylated thiazole intermediate. The reaction includes an iron-dependent sulfide transfer from a conserved cysteine residue of the protein to a thiazole intermediate. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme. May have additional roles in adaptation to various stress conditions and in DNA damage tolerance.
Belongs to the WD repeat G protein beta family. Ribosomal protein RACK1 subfamily.
Acts as one of several non-catalytic accessory components of the cytoplasmic dynein complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures.
Belongs to the dynein light chain family.
Cytoplasmic dynein consists of two catalytic heavy chains (HCs) and a number of non-catalytic subunits which present intermediate chains (ICs), light intermediate chains (LICs) and light chains (LCs).
Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily.
Required for N-linked oligosaccharide assembly. Has a role in the last step of the synthesis of the Man(5)GlcNAc(2)-PP-dolichol core oligosaccharide on the cytoplasmic face of the endoplasmic reticulum.
ATP-dependent RNA helicase involved in 40S ribosomal subunit biogenesis. Required for the processing and cleavage of 35S pre-rRNA at sites A0, A1, and A2, leading to mature 18S rRNA.
Belongs to the DEAD box helicase family. DDX52/ROK1 subfamily.
Interacts with the U3 snoRNA and is associated with the 90S and 40S pre-ribosomes.
Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. KAE1 likely plays a direct catalytic role in this reaction, but requires other protein(s) of the complex to fulfill this activity. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Interacts with the flavoprotein subunit within the SDH catalytic dimer.
Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Required for flavinylation (covalent attachment of FAD) of the flavoprotein subunit of the SDH catalytic dimer.
Catalyzes the synthesis of activated sulfate.
Belongs to the eukaryotic ribosomal protein eL19 family.
Functions as component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and ADA. SAGA is involved in RNA polymerase II-dependent transcriptional regulation.
Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the scaffold complex CFD1-NBP35. Electrons are transferred to DRE2 from NADPH via the FAD- and FMN-containing protein TAH18. TAH18-DRE2 are also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit RNR2.
Monomer. Interacts with TAH18. Interacts with MIA40.
The C-terminal domain binds 2 Fe-S clusters but is otherwise mostly in an intrinsically disordered conformation.
The N-terminal domain has structural similarity with S-adenosyl-L-methionine-dependent methyltransferases, but does not bind S-adenosyl-L-methionine. It is required for correct assembly of the 2 Fe-S clusters.
The twin Cx2C motifs are involved in the recognition by the mitochondrial MIA40-ERV1 disulfide relay system. The formation of 2 disulfide bonds in the Cx2C motifs through dithiol/disulfide exchange reactions effectively traps the protein in the mitochondrial intermembrane space.
Forms a one-to-one complex with ATPase to inhibit the enzyme activity completely.
Belongs to the protein kinase superfamily. PAN3 family.
Contains a pseudokinase domain. The protein kinase domain is predicted to be catalytically inactive because some of the residues important for catalytic activity are substituted and it lacks the equivalent of the binding site for a peptide substrate. However, it has retained an ATP-binding site and ATP-binding is required for mRNA degradation, stimulating the activity of the PAN2 nuclease in vitro. The nucleotide-binding site is juxtaposed to the RNase active site of PAN2 in the complex and may actually bind nucleosides of a poly(A) RNA rather than ATP, feeding the poly(A)-tail to the active site of the deadenylase and thus increasing the efficiency with which this distributive enzyme degrades oligo(A) RNAs.
Homodimer. Forms a heterotrimer with a catalytic subunit PAN2 to form the poly(A)-nuclease (PAN) deadenylation complex. Interacts (via PAM-2 motif) with poly(A)-binding protein PAB1 (via PABC domain), conferring substrate specificity of the enzyme complex.
Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein PAB1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails. PAN3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit PAN2 to mRNA via its interaction with RNA and with PAB1.
The N-terminal zinc finger binds to poly(A) RNA.
The pseudokinase domain, the coiled-coil (CC), and C-terminal knob domain (CK) form a structural unit (PKC) that forms an extensive high-affinity interaction surface for PAN2.
Involved in pre-mRNA splicing. Facilitates the cooperative formation of U2/U6 helix II in association with stem II in the spliceosome. Binds to RNA.
Exhibits ester hydrolase activity on the substrate p-nitrophenyl acetate.
Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.
As part of the replication protein A (RPA/RP-A), a single-stranded DNA-binding heterotrimeric complex, may play an essential role in DNA replication, recombination and repair. Binds and stabilizes single-stranded DNA intermediates, preventing complementary DNA reannealing and recruiting different proteins involved in DNA metabolism.
Belongs to the replication factor A protein 1 family.
Component of the heterotrimeric canonical replication protein A complex (RPA).
Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. The MDM12-MMM1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The MDM10-MDM12-MMM1 subcomplex further acts in the TOM40-specific pathway after the action of the MDM12-MMM1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids.
Homodimer. Component of the ER-mitochondria encounter structure (ERMES) or MDM complex, composed of MMM1, MDM10, MDM12 and MDM34. A MMM1 homodimer associates with one molecule of MDM12 on each side in a pairwise head-to-tail manner, and the SMP-LTD domains of MMM1 and MDM12 generate a continuous hydrophobic tunnel for phospholipid trafficking.
Belongs to the NUP186/NUP192/NUP205 family.
Belongs to the bacterial ribosomal protein bL17 family.
Belongs to the SNF2/RAD54 helicase family. SWR1 subfamily.
Component of the SWR1 chromatin-remodeling complex.
Belongs to the steroid 5-alpha reductase family. Polyprenol reductase subfamily.
Plays a key role in early steps of protein N-linked glycosylation by being required for the conversion of polyprenol into dolichol. Dolichols are required for the synthesis of dolichol-linked monosaccharides and the oligosaccharide precursor used for N-glycosylation. Acts as a polyprenol reductase that promotes the reduction of the alpha-isoprene unit of polyprenols into dolichols in a NADP-dependent mechanism.
Belongs to the damage-control phosphatase family. Sugar phosphate phosphatase III subfamily.
Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate. Its preference for fructose-1-phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-control function in hexose phosphate metabolism.
Subfamily III proteins have a conserved RTxK motif about 40-50 residues from the C-terminus; the threonine may be replaced by serine or cysteine.
Adds the third glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(2)Man(9)GlcNAc(2)-PP-Dol.
Belongs to the ALG10 glucosyltransferase family.
Forms a heterodimer with the catalytic subunit TRM8.
Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit.
Belongs to the thiolase-like superfamily. Fungal fatty acid synthetase subunit alpha family.
May play a role in anterograde transport of membrane proteins from the endoplasmic reticulum to the Golgi.
Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. FDH subfamily.
Catalyzes the NAD(+)-dependent oxidation of formate to carbon dioxide. Formate oxidation is the final step in the methanol oxidation pathway in methylotrophic microorganisms. Has a role in the detoxification of exogenous formate in non-methylotrophic organisms.
Belongs to the V-ATPase V0D/AC39 subunit family.
Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments. This subunit is a non-integral membrane component of the membrane pore domain and is required for proper assembly of the V0 sector. Might be involved in the regulated assembly of V1 subunits onto the membrane sector or alternatively may prevent the passage of protons through V0 pores.
Belongs to the class I-like SAM-binding methyltransferase superfamily. TrmB family.
Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
The complex LTO1:YAE1 may function as a target specific adapter that probably recruits apo-RPLI1 to the cytosolic iron-sulfur protein assembly (CIA) complex machinery. May be required for biogenesis of the large ribosomal subunit and initiation of translation.
The RNA gate region regulates mRNA cap recognition to prevent promiscuous mRNA-binding before assembly of eif3d into the full eukaryotic translation initiation factor 3 (eIF-3) complex.
mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. In the eIF-3 complex, eif3d specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs.
Belongs to the acetyltransferase family. ARD1 subfamily.
Belongs to the complex I LYR family. SDHAF3 subfamily.
Interacts with the iron-sulfur protein subunit within the SDH catalytic dimer.
Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Promotes maturation of the iron-sulfur protein subunit of the SDH catalytic dimer, protecting it from the deleterious effects of oxidants. May act together with SDHAF1.
Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.
Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Catalytic subunit of an S-adenosyl-L-methionine-dependent tRNA methyltransferase complex that mediates the methylation of the guanosine nucleotide at position 10 (m2G10) in tRNAs.
Belongs to the 5'-AMP-activated protein kinase beta subunit family.
Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation.
Glucosidase involved in the degradation of cellulosic biomass. Has both alpha- and beta-glucosidase activity.
Belongs to the V-ATPase G subunit family.
Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment.
Belongs to the class I-like SAM-binding methyltransferase superfamily. UbiG/COQ3 family.
O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
Catalyzes the synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP.
Transiently phosphorylated on a His residue during the reaction cycle. Phosphorylation strongly increases the affinity for substrates and increases the rate of nicotinate D-ribonucleotide production. Dephosphorylation regenerates the low-affinity form of the enzyme, leading to product release.
Nuclease required for the repair of DNA interstrand cross-links (ICL). Acts as a 5'-3' exonuclease that anchors at a cut end of DNA and cleaves DNA successively at every third nucleotide, allowing to excise an ICL from one strand through flanking incisions.
Belongs to the peroxidase family. Ligninase subfamily.
Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Belongs to the RNase HII family. Eukaryotic subfamily.
Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Belongs to the chromate ion transporter (CHR) (TC 2.A.51) family.
Catalytic component of the histone acetylase B (HAT-B) complex. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. Involved in DNA double-strand break repair.
Component of the HAT-B complex composed of at least HAT1 and HAT2. The HAT-B complex binds to histone H4 tail.
Carbamylation allows a single lysine to coordinate two nickel ions.
In the C-terminal section; belongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family.
Belongs to the metallo-dependent hydrolases superfamily. Adenosine and AMP deaminases family. Adenine deaminase type 2 subfamily.
Catalyzes the hydrolytic deamination of adenine to hypoxanthine. Plays an important role in the purine salvage pathway and in nitrogen catabolism.
Belongs to the queuine tRNA-ribosyltransferase family. QTRT2 subfamily.
Non-catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Acts as a membrane receptor for soluble GET3, which recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol.
Belongs to the ATPase epsilon chain family.
Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Involved in nucleotide excision repair.
Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. Alanine aminotransferase subfamily.
Component of the ER-mitochondria encounter structure (ERMES) or MDM complex, composed of MMM1, MDM10, MDM12 and MDM34.
Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. MDM34 is required for the interaction of the ER-resident membrane protein MMM1 and the outer mitochondrial membrane-resident beta-barrel protein MDM10.
Belongs to the cyclophilin-type PPIase family. PPIL2 subfamily.
May catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides thereby assisting the folding of proteins. May also function as a chaperone, playing a role in intracellular transport of proteins. May also have a protein ubiquitin ligase activity acting as an E3 ubiquitin protein ligase or as a ubiquitin-ubiquitin ligase promoting elongation of ubiquitin chains on proteins.
Component of the 66S pre-ribosomal particle.
Required for efficient assembly and nuclear export of the 60S ribosomal subunit.
Belongs to the class I-like SAM-binding methyltransferase superfamily. gTMT family.
Belongs to the MICOS complex subunit Mic12 family.
Belongs to the TRAFAC class dynamin-like GTPase superfamily. GB1/RHD3 GTPase family. RHD3 subfamily.
Cooperates with the reticulon proteins and tubule-shaping DP1 family proteins to generate and maintain the structure of the tubular endoplasmic reticulum network. Has GTPase activity, which is required for its function in ER organization.
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. The coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.
In the C-terminal section; belongs to the eukaryotic ribosomal protein eS31 family.
Belongs to the ubiquitin-activating E1 family. UBA3 subfamily.
Catalytic subunit of the dimeric E1 enzyme, which activates NEDD8.
Belongs to the cyclophilin-type PPIase family. PPIL4 subfamily.
Belongs to the eukaryotic ribosomal protein eL36 family.
Esterase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C (PubMed:22652150). Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production (By similarity). The other FUS cluster members are not essential for fusarin C biosynthesis (By similarity).
Associates in the nucleolus with the 60S and pre-60S ribosomal subunits.
Belongs to the DEAD box helicase family. DDX18/HAS1 subfamily.
Belongs to the serine/threonine dehydratase family.
Belongs to the small GTPase superfamily. Ran family.
GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Involved in chromatin condensation and control of cell cycle.
Belongs to the eukaryotic ribosomal protein eL21 family.
DNA polymerase that functions in several pathways of DNA repair. Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Also contributes to DNA double-strand break repair by non-homologous end joining and homologous recombination. Has both template-dependent and template-independent (terminal transferase) DNA polymerase activities. Has also a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity.
Belongs to the dolichyldiphosphatase family.
Required for efficient N-glycosylation. Necessary for maintaining optimal levels of dolichol-linked oligosaccharides. Hydrolyzes dolichyl pyrophosphate at a very high rate and dolichyl monophosphate at a much lower rate. Does not act on phosphatidate.
Eliminates the ability to metabolize BOA.
N-malonyltransferase; part of the Fusarium detoxification of benzoxazolinone cluster 2 (FDB2) involved in the degradation of benzoxazolinones produced by the host plant (PubMed:19302487, PubMed:26808652). Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their inherent instability once released, spontaneously degrade to the more stable corresponding benzoxazolinones, 6-methoxy-2-benzoxazolinone (MBOA) and 2-benzoxazolinone (BOA), respectively (PubMed:11876429). The first step in the detoxification of benzoxazolinones involves the hydrolysis of the cyclic ester bond of benzoxazolinones by the FDB1 cluster gamma-lactamase MBL1 to aminophenols (PubMed:26808652, PubMed:12788712). MBL1 is able to convert BOA into 2-aminophenol (2-AP), as well as MBOA into 5-methoxy-2-aminophenol (2-AMP) (PubMed:26808652, PubMed:12788712). The FDB2 cluster N-malonyltransferase FDB2/NAT1 then metabolizes aminophenols via N-malonylation to non-toxic malonamic acids (PubMed:19302487, PubMed:12788712). FDB2/NAT1 converts 2-AP into N-(2-hydroxyphenyl) malonamic acid (HPMA) and 2-AMP into N-(2-hydroxy-4-methoxyphenyl) malonamic acid (HMPMA) (PubMed:19302487, PubMed:12788712). The duplicated dienlactone hydrolases DLH1 and DLH2 may provide redundant function for hydrolyzing the lactone moiety in the BOA molecule (Probable). The roles of the amidases an other enzymes encoded by the 2 FDB clusters have not been identified so far (Probable).
Belongs to the UTP23/FCF1 family. FCF1 subfamily.
Belongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. Eukaryotic type II sub-subfamily.
Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit. Interacts with pstB2. This interaction may be a means to structurally tether the donor membrane (ER) harboring PstB2 to acceptor membranes (Golgi/endosomes) harboring PSD2 during PtdSer transport to the site of PtdEtn synthesis.
The C2 domains have an essential, but non-catalytic function. They may facilitate interactions with other proteins and are required for lipid transport function.
Binds 1 potassium ion per subunit. The potassium ion interacts primarily with the substrate.
Binds 2 magnesium ions per subunit. The magnesium ions interact primarily with the substrate.
Catalyzes the formation of S-adenosylmethionine from methionine and ATP.
Involved in the second step of GPI biosynthesis. De-N-acetylation of N-acetylglucosaminyl-phosphatidylinositol.
Belongs to the PAPS reductase family. CysH subfamily.
Belongs to the eukaryotic ribosomal protein eL33 family.
Belongs to the AP endonuclease 2 family.
Belongs to the calcineurin regulatory subunit family.
Composed of a catalytic subunit (A) and a regulatory subunit (B).
Regulatory subunit of calcineurin, a calcium-dependent, calmodulin stimulated protein phosphatase. Confers calcium sensitivity.
In the 2nd section; belongs to the EPSP synthase family.
In the 3rd section; belongs to the shikimate kinase family.
In the 4th section; belongs to the type-I 3-dehydroquinase family.
In the C-terminal section; belongs to the shikimate dehydrogenase family.
In the N-terminal section; belongs to the dehydroquinate synthase family.
In the N-terminal section; belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family.
The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis.
Belongs to the class I-like SAM-binding methyltransferase superfamily. DOT1 family.
Histone methyltransferase that specifically trimethylates histone H3 to form H3K79me3. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histone.
Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
Component of the 7-subunit TFIIH core complex composed of XPB/SSL2, XPD/RAD3, SSL1, TFB1, TFB2, TFB4 and TFB5, which is active in NER. The core complex associates with the 3-subunit CTD-kinase module TFIIK composed of CCL1, KIN28 and TFB3 to form the 10-subunit holoenzyme (holo-TFIIH) active in transcription.
Scaffold protein for the de novo synthesis of iron-sulfur (Fe-S) clusters within mitochondria, which is required for maturation of both mitochondrial and cytoplasmic [2Fe-2S] and [4Fe-4S] proteins.
Belongs to the major facilitator superfamily. DHA1 family. Polyamines/proton antiporter (TC 2.A.1.2.16) subfamily.
Efflux pump involved in export of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties (PubMed:25372119). Constitutes a self-protecting mechanism of the fungus against critical levels of FSA within the cell (By similarity).
Putative mitochondrial redox protein which could be involved in the reduction of small toxic molecules.
Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis.
Belongs to the GcvT family. CAF17 subfamily.
Belongs to the AB hydrolase superfamily.
Demethylates proteins that have been reversibly carboxymethylated. Demethylates the phosphatase PP2A catalytic subunit.
Catalytic tRNA acetyltransferase subunit of the elongator complex, which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine). In the elongator complex, acts as a tRNA uridine(34) acetyltransferase by mediating formation of carboxymethyluridine in the wobble base at position 34 in tRNAs.
Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrE subfamily.
Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Required for the import and folding of small cysteine-containing proteins (small Tim) in the mitochondrial intermembrane space (IMS). Forms a redox cycle with ERV1 that involves a disulfide relay system. Precursor proteins to be imported into the IMS are translocated in their reduced form into the mitochondria. The oxidized form of MIA40 forms a transient intermolecular disulfide bridge with the reduced precursor protein, resulting in oxidation of the precursor protein that now contains an intramolecular disulfide bond and is able to undergo folding in the IMS.
Hydrolase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties (PubMed:22652150, PubMed:25372119). L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L-homoserine by cluster enzymes aspartate kinase FUB3 and homoserine O-acetyltransferase FUB5, as well as enzymes of the primary metabolism (By similarity). The polyketide synthase (PKS) FUB1 generates the triketide trans-2-hexenal which is presumptively released by the hydrolase FUB4 and linked to the NRPS-bound amino acid precursor by NAD(P)-dependent dehydrogenase FUB6 (By similarity). FUB1, FUB4, and the non-canonical NRPS Fub8 may form an enzyme complex (By similarity). Further processing of the NRPS-bound intermediate might be carried out by FUB6 and the sulfhydrylase FUB7, enabling a spontaneous electrocyclization to close the carbon backbone of fusaric acid (By similarity). Dihydrofusaric acid is likely to be released via reduction by the thioester reductase (TR) domain of FUB8 whereupon the final oxidation to fusaric acid may (also) be performed by the FMN-dependent dehydrogenase FUB9 (By similarity).
Impairs the production of fusaric acid (PubMed:25372119).
Belongs to the PPP phosphatase family. PP-Z subfamily.
Belongs to the complex I NDUFB3 subunit family.
Belongs to the EF-1-beta/EF-1-delta family.
Belongs to the methyltransferase superfamily. NTM1 family.
Small GTPase required for proper localization of RNA polymerase II and III (RNAPII and RNAPIII). May act at an RNAP assembly step prior to nuclear import.
Belongs to the protein-tyrosine phosphatase family. Non-receptor class myotubularin subfamily.
Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-acyl-PI during GPI precursor assembly. Required for cell wall integrity.
Belongs to the complex I NDUFA13 subunit family.
Complex I functions in the transfer of electrons from NADH to the respiratory chain. Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis.
Belongs to the nucleoporin Nup85 family.
Component of the nuclear pore complex (NPC).
Binds 1 5,10-methenyltetrahydrofolate (MTHF) per subunit.
Belongs to the class IV-like SAM-binding methyltransferase superfamily.
Belongs to the MICOS complex subunit Mic60 family.
Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Plays a role in keeping cristae membranes connected to the inner boundary membrane. Also promotes protein import via the mitochondrial intermembrane space assembly (MIA) pathway.