Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
Catalyzes the formation of 4-(hydroxymethyl)-2-furancarboxaldehyde phosphate (4-HFC-P) from two molecules of glyceraldehyde-3-P (GA-3-P).
ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Degrades polypeptides processively (By similarity).
Belongs to the peptidase S16 family. Archaeal LonB subfamily.
Homohexamer. Organized in a ring with a central cavity (By similarity).
Tetramer of two alpha and two beta chains.
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Heterocomplex of the form (alpha(1)beta(1)gamma(1))(8).
Reduces the physiological low-potential two-electron acceptor coenzyme F420, and the artificial one-electron acceptor methylviologen.
There are 12-13 Fe atoms per alpha/beta/gamma unit of the FRH.
Belongs to the GTP cyclohydrolase IV family.
Converts GTP to 7,8-dihydro-D-neopterin 2',3'-cyclic phosphate, the first intermediate in the biosynthesis of coenzyme methanopterin.
Heterooctamer of four A and four B subunits.
Inhibited by ADP and alpha-ketoglutarate.
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.
Belongs to the purine/pyrimidine phosphoribosyltransferase family. Archaeal HPRT subfamily.
Catalyzes a salvage reaction resulting in the formation of IMP that is energically less costly than de novo synthesis.
Part of a complex that catalyzes the reversible reduction of CoM-S-S-CoB to the thiol-coenzymes H-S-CoM (coenzyme M) and H-S-CoB (coenzyme B).
The heterodisulfide reductase is composed of three subunits; HdrA, HdrB and HdrC. It forms a complex with the F420-non-reducing hydrogenase (Mvh), which provides the reducing equivalents to the heterodisulfide reductase.
Belongs to the V-ATPase D subunit family.
Produces ATP from ADP in the presence of a proton gradient across the membrane.
Belongs to the methyl-coenzyme M reductase gamma subunit family.
Binds 2 coenzyme F430 non-covalently per MCR complex. Coenzyme F430 is a yellow nickel porphinoid. Methyl-coenzyme-M reductase is activated when the enzyme-bound coenzyme F430 is reduced to the Ni(I) oxidation state.
Component of the methyl-coenzyme M reductase (MCR) I that catalyzes the reductive cleavage of methyl-coenzyme M (CoM-S-CH3 or 2-(methylthio)ethanesulfonate) using coenzyme B (CoB or 7-mercaptoheptanoylthreonine phosphate) as reductant which results in the production of methane and the mixed heterodisulfide of CoB and CoM (CoM-S-S-CoB). This is the final step in methanogenesis.
MCR is a hexamer of two alpha, two beta, and two gamma chains, forming a dimer of heterotrimers.
There are two MCR complexes in this bacteria. MCR II is expressed in the early growth phase. Late growth cells contain mostly MCR I.
Belongs to the LeuD family. LeuD type 2 subfamily.
Component of a hydro-lyase with broad substrate specificity for cis-unsaturated tricarboxylic acids. Catalyzes both the reversible dehydration of (R)-homocitrate ((R)-2-hydroxybutane-1,2,4-tricarboxylate) to produce cis-homoaconitate ((Z)-but-1-ene-1,2,4-tricarboxylate), and its hydration to homoisocitrate ((1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate). Is also able to hydrate the analogous longer chain substrates cis-homo(2)-aconitate, cis-homo(3)-aconitate. These reactions are part of the biosynthesis pathway of coenzyme B.
Functional assignment as methanogen HACN has been made based on the presence of the YLRT motif involved in substrate specificity as discussed in PubMed:20170198.
Heterotetramer of 2 HacA and 2 HacB proteins.
Belongs to the eukaryotic ribosomal protein eS24 family.
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). The GatDE system is specific for glutamate and does not act on aspartate.
Belongs to the asparaginase 1 family. GatD subfamily.
Catalyzes the condensation of formaldehyde with tetrahydromethanopterin (H(4)MPT) to 5,10-methylenetetrahydromethanopterin.
Catalyzes the reversible formation of ribulose-5-phosphate and formaldehyde from 3-hexulose-6-phosphate.
In the C-terminal section; belongs to the HPS/KGPDC family. HPS subfamily.
In the N-terminal section; belongs to the formaldehyde-activating enzyme family.
Probably functions as a manganese efflux pump.
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Catalyzes the synthesis of GMP from XMP.
Heterodimer composed of a glutamine amidotransferase subunit (A) and a GMP-binding subunit (B).
Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family.
Belongs to the activator 1 small subunits family. RfcL subfamily.
Heterohexamer composed of four small subunits (RfcS) and two large subunits (RfcL).
Part of the RFC clamp loader complex which loads the PCNA sliding clamp onto DNA. The complex possesses DNA-dependent ATPase activity which is further stimulated by PCNA. In conjunction with PCNA stimulates DNA synthesis by PolB, relieving inhibition by replication protein A (RPA).
Belongs to the eukaryotic ribosomal protein eS17 family.
Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Belongs to the homoserine dehydrogenase family.
Rubredoxin is a small nonheme, iron protein lacking acid-labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule.
Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases.
Belongs to the archaeal-type DHQ synthase family.
Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.
Belongs to the NifD/NifK/NifE/NifN family.
Binds 1 [8Fe-7S] cluster per heterodimer.
Tetramer of two alpha and two beta chains. Forms complex with the iron protein (nitrogenase component 2).
This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation.
Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase.
Forms an energy-coupling factor (ECF) transporter complex composed of an ATP-binding protein (A component, CbiO), a transmembrane protein (T component, CbiQ) and 2 possible substrate-capture proteins (S components, CbiM and CbiN) of unknown stoichimetry.
Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.
Belongs to the CbiX family. CbiXS subfamily.
Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis (PubMed:12686546). Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation (Potential). Catalyzes the insertion of Ni(2+) into sirohydrochlorin to yield Ni-sirohydrochlorin (Potential).
Belongs to the eukaryotic ribosomal protein eL39 family.
Belongs to the IPP isomerase type 2 family.
Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP).
Probably involved in the biogenesis of the ribosome.
Belongs to the eukaryotic ribosomal protein eL32 family.
Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.
Belongs to the eukaryotic/archaeal RNase P protein component 4 family.
Consists of a catalytic RNA component and at least 4-5 protein subunits.
Constitutively expressed (at protein level).
Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Belongs to the eukaryotic ribosomal protein eL18 family.
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).
Belongs to the purine/pyrimidine phosphoribosyltransferase family.
Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family.
Converts O-phospho-L-seryl-tRNA(Cys) (Sep-tRNA(Cys)) to L-cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)).
Homodimer. Heterotetramer of two Top6A and two Top6B chains.
Relaxes both positive and negative superturns and exhibits a strong decatenase activity.
Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 1 subfamily.
Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
Belongs to the phosphohexose mutase family.
Lacks the conserved Ser-Lys catalytic dyad essential for proteolytic activity. Its enzyme activity is therefore unsure.
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.
Belongs to the universal ribosomal protein uS13 family.
Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement.
Part of the 30S ribosomal subunit. Forms a loose heterodimer with protein S19. Forms two bridges to the 50S subunit in the 70S ribosome.
Catalyzes the cis-trans isomerization of peptidyl prolyl bonds and accelerates protein folding. Also exhibits chaperone-like activity (PubMed:10824098). In vitro, can use oligopeptides such as N-succinyl-Ala-Leu-Pro-Phe-p-nitroanilide and N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide as substrates. The PPIase activity is much lower than those of other FKBPs reported against oligopeptidyl substrates. As a chaperone, protects green fluorescent protein (GFP) and rhodanese from thermal denaturation or aggregation, and suppresses the aggregation of chemically unfolded rhodanese and elevates the yield of its refolding (PubMed:10824098).
Contains an N-terminal PPIase domain, an IF (Insert in the Flap) domain and a C-terminal domain (CTD). Aggregation suppressing activity against chemically unfolded protein is exerted mainly by the CTD while N- and C-terminal domains contribute to thermal protein aggregation suppression. The CTD probably contributes to hexamerization.
Belongs to the glutamate synthase family.
RNA-free RNase P that catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus.
Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ and 2 PurS subunits.
Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
This protein may play a role in the biosynthesis of the prosthetic group of nitrogenase (FeMo cofactor).
Belongs to the CDP-archaeol synthase family.
Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.
Belongs to the anthranilate synthase component I family.
Heterotetramer consisting of two non-identical subunits: a beta subunit (TrpG) and a large alpha subunit (TrpE).
Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia (By similarity).
Belongs to the helicase family. UvrD subfamily.
Belongs to the universal ribosomal protein uL30 family.
Belongs to the SAICAR synthetase family.
Belongs to the 2-phosphoglycerate kinase family.
Catalyzes the phosphorylation of 2-phosphoglycerate to 2,3-diphosphoglycerate. Involved in the biosynthesis of cyclic 2,3-bisphosphoglycerate, a thermoprotectant.
Belongs to the thymidylate kinase family.
Belongs to the class-I aminoacyl-tRNA synthetase 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 V-ATPase E subunit family.
Belongs to the FBP aldolase/phosphatase family.
Catalyzes two subsequent steps in gluconeogenesis: the aldol condensation of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (GA3P) to fructose-1,6-bisphosphate (FBP), and the dephosphorylation of FBP to fructose-6-phosphate (F6P).
Consists of a single catalytic domain, but remodels its active-site architecture via a large structural change to exhibit dual activities.
Heterotetramer of one alpha, one beta, one delta and one gamma chain.
Plays a role in the regulation of phosphate uptake.
Belongs to the eukaryotic ribosomal protein eL31 family.
Belongs to the binding-protein-dependent transport system permease family. CysTW subfamily.
Belongs to the glycosyltransferase 4 family. MraY subfamily.
Belongs to the complex I 51 kDa subunit family.
Belongs to the GTP cyclohydrolase I type 2/NIF3 family.
Part of a complex that catalyzes the formation of methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and methyl-tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step.
The complex is composed of 8 subunits; MtrA, MtrB, MtrC, MtrD, MtrE, MtrF, MtrG and MtrH.
Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
Heterooligomer of catalytic and regulatory chains.
Binds 2 [4Fe-4S] clusters. In this family the first cluster has a non-standard and varying [4Fe-4S] binding motif CX(2)CX(2)CX(4-5)CP.
Catalyzes the ferredoxin-dependent oxidative decarboxylation of arylpyruvates.
Heterodimer of the IorA and IorB subunits.
Belongs to the universal ribosomal protein uL11 family.
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
Part of the ribosomal stalk of the 50S ribosomal subunit. Interacts with L10 and the large rRNA to form the base of the stalk. L10 forms an elongated spine to which L12 dimers bind in a sequential fashion forming a multimeric L10(L12)X complex.
Belongs to the NAGSA dehydrogenase family. Type 1 subfamily.
Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Belongs to the eukaryotic ribosomal protein eS19 family.
May be involved in maturation of the 30S ribosomal subunit.
Belongs to the archaeal RpoM/eukaryotic RPA12/RPB9/RPC11 RNA polymerase family.
Induces RNA cleavage activity in the RNA polymerase. In its presence, the cleavage activity of the RNA polymerase truncates the RNA back to position +15 in a stepwise manner by releasing mainly dinucleotides from the 3'-end of the nascent RNA. The truncated RNAs are able to continue elongation. Involved in transcriptional proofreading and fidelity. Misincorporation of nucleotides during elongation of transcription leads to arrested elongation complexes which are rescued by TFS-promoted removal of a dinucleotide from the 3'-end. TFS is able to induce a cleavage resynthesis cycle in stalled elongation complexes (resulting from the next missing nucleotide or a reduced incorporation rate of a wrong nucleotide) preventing misincorporation and enabling proofreading in a post-incorporation manner. Pausing of elongation complexes is the main determinant of TFS-induced RNA cleavage.
More similar by sequence similarity to the eukaryotic RNA polymerase subunits.
Belongs to the archaeal SPP-like hydrolase family.
Catalyzes the dephosphorylation of 2-phosphoglycolate.
Belongs to the radical SAM superfamily. Biotin synthase family.
Homodimer or monomer. The Ni-sirohydrochlorin a,c-diamide reductive cyclase complex is composed of a NifH homolog component CfbC and a NifD homolog component CfbD.
Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes both the six-electron reduction of the tetrahydroporphyrin ring system and the gamma-lactamization of the c-acetamide side chain of Ni-sirohydrochlorin a,c-diamide to yield 15,17(3)-seco-F430-17(3)-acid (seco-F430), the last intermediate in the biosynthesis of the coenzyme F430.
Belongs to the class-II aminoacyl-tRNA synthetase family. Type-2 seryl-tRNA synthetase subfamily.
Binds 1 Zn(2+) ion per subunit. This ion is coordinated with 2 cysteines, 1 glutamate and a water molecule that dissociates from the zinc ion to allow the coordination of the amino group of the serine substrate, which is essential for catalysis.
Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
Consists of two distinct domains, a catalytic core and a N-terminal extension that is presumably involved in tRNA binding.
Belongs to the triosephosphate isomerase family.
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalyzes the transfer of diphosphate from ATP to 6-hydroxymethyl-7,8-dihydropterin (6-HMD), leading to 6-hydroxymethyl-7,8-dihydropterin diphosphate (6-HMDP).
Homodimer. Forms a heterotetramer composed of two Mre11 subunits and two Rad50 subunits.
Nuclease activity is regulated by Rad50.
Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Mre11 binds to DSB ends and has both double-stranded 3'-5' exonuclease activity and single-stranded endonuclease activity.
Belongs to the AIR carboxylase family. Class I subfamily.
Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR).
Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.
Catalyzes two reactions in de novo purine nucleotide biosynthesis. Catalyzes the breakdown of 5-aminoimidazole- (N-succinylocarboxamide) ribotide (SAICAR or 2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate) to 5-aminoimidazole-4-carboxamide ribotide (AICAR or 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide) and fumarate, and of adenylosuccinate (ADS or N(6)-(1,2-dicarboxyethyl)-AMP) to adenosine monophosphate (AMP) and fumarate.
Homotetramer. Residues from neighboring subunits contribute catalytic and substrate-binding residues to each active site (By similarity).
Belongs to the thymidylate synthase family. Archaeal-type ThyA subfamily.
May catalyze the biosynthesis of dTMP using an unknown cosubstrate.
Binds 1 thiamine pyrophosphate per subunit.
Heterododecamer composed of 6 subunits alpha and 6 subunits beta.
Involved in the biosynthesis of the coenzyme M (2-mercaptoethanesulfonic acid). Catalyzes the decarboxylation of sulfopyruvate to sulfoacetaldehyde.
Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 subfamily.
Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile).
IleRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated valine is translocated from the active site to the editing site, which sterically excludes the correctly activated isoleucine. The single editing site contains two valyl binding pockets, one specific for each substrate (Val-AMP or Val-tRNA(Ile)).
Belongs to the FPP/GGPP synthase family.
There seems to be a sequencing error that fuses together porC and porD. We have cut the ORF into its two constituents.
Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
Belongs to the ATPase alpha/beta chains family.
Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal alpha chain is a catalytic subunit (By similarity).
Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit family.
There are 12-13 Fe atoms/(alpha(1)beta(1)gamma(1)) unit of the FRH.
Homodimer. Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ and 2 PurS subunits (By similarity).
Belongs to the DNA photolyase class-2 family.
Binds 1 coenzyme F420 non-covalently per subunit.
Involved in repair of UV radiation-induced DNA damage. Catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl pyrimidine dimers (in cis-syn configuration), which are formed between adjacent bases on the same DNA strand upon exposure to ultraviolet radiation.
Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 2 subfamily.
Tetramer of two alpha and two beta subunits.
Contains two rhodanese domains with different primary structures but with near identical secondary structure conformations suggesting a common evolutionary origin. Only the C-terminal rhodanese domain contains the catalytic cysteine residue (By similarity).
Belongs to the radical SAM superfamily. MoaA family.
Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 [4Fe-4S] cluster coordinated with 3 cysteines and the GTP-derived substrate.
Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate.
Required for formate dehydrogenase (FDH) activity. Acts as a sulfur carrier protein that transfers sulfur from IscS to the molybdenum cofactor prior to its insertion into FDH.
Belongs to the AdoMet synthase 2 family.
Catalyzes the formation of S-adenosylmethionine from methionine and ATP.
Belongs to the aspartate-semialdehyde dehydrogenase family.
Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate.
Catalyzes the reversible reduction of methenyl-H(4)MPT(+) to methylene-H(4)MPT.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA methyltransferase RlmE family.
Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
Catalyzes the oxidation of F420H(2) with O(2) (By similarity). May be involved in O(2) detoxification, reducing the intracellular O(2) concentration to a level allowing growth at the expense of methane formation (By similarity).
In the N-terminal section; belongs to the zinc metallo-hydrolase group 3 family.
Was originally thought to be a subunit of methylviologen hydrolase II.
Belongs to the universal ribosomal protein uL24 family.
Located at the polypeptide exit tunnel on the outside of the subunit.
One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
Belongs to the eukaryotic ribosomal protein eL8 family.
Multifunctional RNA-binding protein that recognizes the K-turn motif in ribosomal RNA, the RNA component of RNase P, box H/ACA, box C/D and box C'/D' sRNAs.
Part of the 50S ribosomal subunit. Probably part of the RNase P complex.
Belongs to the V-ATPase V0D/AC39 subunit family.
Belongs to the type-I restriction system S methylase family.
Belongs to the alpha-IPM synthase/homocitrate synthase family.
Catalyzes the condensation of pyruvate and acetyl-coenzyme A to form (R)-citramalate.
Belongs to the metallo-dependent hydrolases superfamily. DHOase family. Class I DHOase subfamily.
Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Belongs to the universal ribosomal protein uL23 family.
Binds to 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome.
Part of the 50S ribosomal subunit. Contacts protein L29.
Catalyzes the reversible transfer of a formyl group from formylmethanofuran (formyl-MFR) to tetrahydromethanopterin (H(4)MPT) to produce 5-formyl tetrahydromethanopterin (5-formyl-H(4)MPT) and methanofuran (MFR).
Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 2 subfamily.
Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
ValRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated threonine is translocated from the active site to the editing site.
Belongs to the eukaryotic ribosomal protein eL14 family.
Belongs to the helicase family. Hel308 subfamily.
DNA-dependent ATPase and 3'-5' DNA helicase that may be involved in repair of stalled replication forks. Helicase with 3'-to 5'- polarity; able to unwind over 100 bp of DNA at 50 degrees Celsius. Unwinds forked DNA, preferentially on lagging strand forks; has weaker activity on Holliday junctions. Displaces the invading strand in DNA D-loops. Unwinds short oligonucleotides from dsDNA with 3'- but not blunt ends or 5'-ssDNA tails in an ATP-dependent manner. ATPase activity is stimulated by ssDNA but not dsDNA, protein binds ssDNA, dsDNA with 5'- or 3'-overhangs but not blunt ended dsDNA and replication forks. Replication forks bind both this protein and RPA. RPA does not stimulate the helicase activity of this protein.
Monomer (By similarity). Binds replication protein A (RPA), in presence and absence of DNA.
The C-terminal region (about 633-690) acts as a brake for ATP hydrolysis (PubMed:17991488) and interacts with RPA (PubMed:21195035).
The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein and the molybdenum-iron protein.
The reversible ADP-ribosylation of Arg-94 inactivates the nitrogenase reductase and regulates nitrogenase activity.
Belongs to the RNA 3'-terminal cyclase family. Type 1 subfamily.
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 (By similarity).
Belongs to the universal ribosomal protein uS19 family.
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
Belongs to the tRNA methyltransferase O family.
Catalyzes the first step of diphthamide biosynthesis, i.e. the transfer of the 3-amino-3-carboxypropyl group from S-adenosyl-L-methionine (SAM) to the C2 position of the imidazole ring of the target histidine residue in translation elongation factor 2 (EF-2).
DNA repair enzyme that incises DNA at 8-oxoG residues. Excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine (FAPY) from damaged DNA. Has a beta-lyase activity that nicks DNA 3' to the lesion (By similarity).
Belongs to the transcriptional regulatory CopG/NikR family.
Belongs to the precorrin-6x reductase family.
Catalyzes the reduction of the macrocycle of cobalt-precorrin-6A to cobalt-precorrin-6B.
Belongs to the dTDP-4-dehydrorhamnose 3,5-epimerase family.
Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.
Belongs to the NAD(P)-dependent epimerase/dehydratase family. GDP-mannose 4,6-dehydratase subfamily.
Catalyzes the conversion of GDP-D-mannose to GDP-4-dehydro-6-deoxy-D-mannose.
Lacks conserved residue(s) required for the propagation of feature annotation.
Belongs to the eukaryotic ribosomal protein eS6 family.
Belongs to the eukaryotic ribosomal protein eL19 family.
Inhibited by charybdotoxin (CTX), a protein from scorpion venom.
It is not known whether calcium is the physiological ligand.
The channel is composed of 4 repeated units, each containing a transmembrane pore part and a gating ring part. The gating ring is composed of eight identical RCK (Regulators of K conductance) domains, in an alternating arrangement of one domain from each of the four subunits and four from the intracellular solution. Two protein interfaces between dimers of RCK domains from the pore-forming subunit and from the intracellular solution hold the ring together. One is called the fixed interface and the other the flexible interface. The flexible interface forms a cleft where calcium binds. Upon calcium binding the gating ring undergoes a conformational change that enables it to pull open the inner helices of the pore, allowing ion conduction.
Belongs to the eukaryotic ribosomal protein eS8 family.
Belongs to the universal ribosomal protein uL14 family.
Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome.
Part of the 50S ribosomal subunit. Forms a cluster with proteins L3 and L24e, part of which may contact the 16S rRNA in 2 intersubunit bridges.
Belongs to the eukaryotic ribosomal protein eS1 family.
Belongs to the SurE nucleotidase family.
Binds 1 divalent metal cation per subunit.
Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Belongs to the GTP-binding SRP family. SRP54 subfamily.
Composed of three domains: the N-terminal N domain, which is responsible for interactions with the ribosome, the central G domain, which binds GTP, and the C-terminal M domain, which binds the RNA and the signal sequence of the RNC.
Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY.
Part of the signal recognition particle protein translocation system, which is composed of SRP and FtsY. Archaeal SRP consists of a 7S RNA molecule of 300 nucleotides and two protein subunits: SRP54 and SRP19.
Belongs to the glucose-1-phosphate thymidylyltransferase family.
Catalyzes the reversible oxidation of malate to oxaloacetate.
Belongs to the archaeal Rpo11/eukaryotic RPB11/RPC19 RNA polymerase subunit family.
DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
Belongs to the 'phage' integrase family. XerA subfamily.
Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules.
A structure-specific endonuclease that resolves Holliday junction (HJ) intermediates during genetic recombination. Cleaves 4-way DNA junctions introducing paired nicks in opposing strands, leaving a 5'-terminal phosphate and a 3'-terminal hydroxyl group that are ligated to produce recombinant products. Cleaves both mobile and immobile junctions. Converts a synthetic Hj to nicked duplex products. Binds a variety of branched DNA structures but linear dsDNA poorly; cleaves only 4-way junctions. Confers UV and mitomycin C resistance to E.coli cells lacking the endogenous Hj machinery RuvABC.
Belongs to the Holliday junction resolvase Hjc family.
Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity.
Belongs to the histone-like Alba family.
Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.
Interacts with UvrB in an incision complex.
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
Belongs to the metallo-dependent hydrolases superfamily. MTA/SAH deaminase family.
Catalyzes the deamination of three SAM-derived enzymatic products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-methylthioadenosine, to produce the inosine analogs. Can also deaminate adenosine. The preferred substrate for this enzyme is 5'-deoxyadenosine, but all these substrates are efficiently deaminated. Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions. May also be involved in the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens.
SAH is a product of SAM methyltransferases and is known to be a feedback inhibitor of these enzymes. As a result of this inhibition, organisms have evolved efficient enzymes to metabolize SAH via different pathways. The pathway found in methanogens differs from the canonical pathway, it uses the deamination of S-adenosyl-L-homocysteine to form S-inosyl-L-homocysteine for the regeneration of SAM from S-adenosyl-L-homocysteine. 5'-deoxyadenosine is a radical SAM enzyme reaction product which strongly inhibits radical SAM enzymes. A pathway for removing this product must be present in methanogens where the MTA/SAH nucleosidase which normally metabolizes this compound is absent.
Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. LL-diaminopimelate aminotransferase subfamily.
Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate. Is also able to catalyze the reverse reaction in vitro, i.e. the transamination of LL-diaminopimelate with 2-oxoglutarate to produce 2-oxo-6-aminopimelate (in equilibrium with tetrahydrodipicolinate) and glutamate. Has maximal aminotransferase activity using 2-oxoglutarate as an amino group acceptor, and cannot use oxaloacetate instead of 2-oxoglutarate, although 2-oxoadipate can substitute with 21% relative activity. Cannot use m-DAP, lysine or ornithine as the amino-group donor, when using 2-oxoglutarate as the amino-group acceptor.
Belongs to the archaeal histone HMF family.
Binds and compact DNA (95 to 150 base pairs) to form nucleosome-like structures that contain positive DNA supercoils.
Homodimer or heterodimer with HmtA1 or HmtA2 (PubMed:1459937). Dimers then assemble into higher oligomers, with the DNA wrapped around the protein core (By similarity).
Part of a complex that provides reducing equivalents for heterodisulfide reductase. MvhD may form the contact site to heterodisulfide reductase (By similarity).
The F420-non-reducing hydrogenase is composed of three subunits; MvhA, MvhD and MvhG. It forms a complex with the heterodisulfide reductase (hdr) (By similarity).
Belongs to the heat shock protein 70 family.
Binds to the 50S ribosomal subunit and prevents its association with the 30S ribosomal subunit to form the 70S initiation complex.
Autophosphorylated on a serine. Phosphorylation is stimulated by binding to MCM. Both single-stranded DNA and double-stranded DNA inhibit the phosphorylation reaction.
Involved in regulation of DNA replication. May play an essential role in origin recognition. Binds to DNA, with a preference for origin-specific double-stranded sequences. Does not bind single-stranded DNA. Inhibits MCM helicase activity but does not affect its oligomeric state.
Monomer. Interacts with MCM via the WH domain.
The N-terminal AAA+ ATPase domain and the C-terminal winged-helix (WH) domain are both required for DNA binding.
Belongs to the eukaryotic ribosomal protein eL42 family.
Belongs to the eukaryotic ribosomal protein eL34 family.
Belongs to the eukaryotic RecA-like protein family.
Involved in DNA repair and in homologous recombination. Binds and assemble on single-stranded DNA to form a nucleoprotein filament. Hydrolyzes ATP in a ssDNA-dependent manner and promotes DNA strand exchange between homologous DNA molecules (By similarity).
Belongs to the pseudouridine synthase TruD family.
Could be responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
Belongs to the eukaryotic ribosomal protein eS28 family.
Belongs to the GTP-binding SRP family. FtsY subfamily.
Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC).
Part of the signal recognition particle protein translocation system, which is composed of SRP and FtsY.
Forms a Heterooligomeric complex of two stacked eight-membered rings.
Molecular chaperone; binds unfolded polypeptides in vitro, and has a weak ATPase activity.
Belongs to the geranylgeranyl reductase family. DGGGPL reductase subfamily.
Is involved in the reduction of 2,3-digeranylgeranylglycerophospholipids (unsaturated archaeols) into 2,3-diphytanylglycerophospholipids (saturated archaeols) in the biosynthesis of archaeal membrane lipids. Catalyzes the formation of archaetidic acid (2,3-di-O-phytanyl-sn-glyceryl phosphate) from 2,3-di-O-geranylgeranylglyceryl phosphate (DGGGP) via the hydrogenation of each double bond of the isoprenoid chains.
Reduction reaction proceeds via syn addition of hydrogen for double bonds.
Belongs to the thiolase-like superfamily. UPF0219 family.
Belongs to the methyltransferase superfamily. Archaeal-type CbiT family.
Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.
Was originally thought to be a precorrin-8w decarboxylase.
Belongs to the Orn/Lys/Arg decarboxylase class-II family. LysA subfamily.
Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine.
Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB.
Belongs to the isocitrate and isopropylmalate dehydrogenases family.
Belongs to the universal ribosomal protein uL22 family.
The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.
This protein binds specifically to 23S rRNA. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.
Belongs to the universal ribosomal protein uL4 family.
Forms part of the polypeptide exit tunnel.
One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.
Belongs to the universal ribosomal protein uL3 family.
One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
Part of the 50S ribosomal subunit. Forms a cluster with proteins L14 and L24e.
ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
Belongs to the ABC transporter superfamily. Energy-coupling factor EcfA family.
Forms a stable energy-coupling factor (ECF) transporter complex composed of 2 membrane-embedded substrate-binding proteins (S component), 2 ATP-binding proteins (A component) and 2 transmembrane proteins (T component).
Belongs to the MsrB Met sulfoxide reductase family.
Binds 1 zinc ion per subunit. The zinc ion is important for the structural integrity of the protein.
Belongs to the DeoC/FbaB aldolase family. ADHS subfamily.
Catalyzes a transaldol reaction between 6-deoxy-5-ketofructose 1-phosphate (DKFP) and L-aspartate semialdehyde (ASA) with an elimination of hydroxypyruvaldehyde phosphate to yield 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate (ADH). Plays a key role in an alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ), which is involved in the canonical pathway for the biosynthesis of aromatic amino acids.
Belongs to the archaeal adenylate kinase family.
Belongs to the RNA polymerase beta chain family.
DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. The Rpo2 subunit (Rpo2N and Rpo2C in this organism) is implicated in DNA promoter recognition and in nucleotide binding.
Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Belongs to the class-II aminoacyl-tRNA synthetase family.
Component of the KEOPS complex that consists of Kae1, Bud32, Cgi121 and Pcc1; the whole complex dimerizes.
In the C-terminal section; belongs to the protein kinase superfamily. Tyr protein kinase family. BUD32 subfamily.
In the N-terminal section; belongs to the KAE1 / TsaD family.
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is a component of the KEOPS complex that is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. The Kae1 domain likely plays a direct catalytic role in this reaction. The Bud32 domain probably displays kinase activity that regulates Kae1 function.
Belongs to the precorrin methyltransferase family.
Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.
Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
Inhibited by NaCl, KCl, ATP, ADP, GTP and aspartate. Unlike E.coli, not regulated by acetyl-CoA.
Belongs to the universal ribosomal protein uS4 family.
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit.
Part of the 30S ribosomal subunit. Contacts protein S5. The interaction surface between S4 and S5 is involved in control of translational fidelity.
With S5 and S12 plays an important role in translational accuracy.
Autophosphorylated on a serine. Phosphorylation is inhibited by binding to MCM. Both single-stranded DNA and double-stranded DNA inhibit the phosphorylation reaction.
Involved in regulation of DNA replication. Dissociates the MCM complex and inhibits the MCM helicase activity, suggesting that it may function as a helicase loader. Binds to both specific and random double-stranded or single-stranded DNA.
Belongs to the archaeal Rpo5/eukaryotic RPB5 RNA polymerase subunit family.
Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source.
Comprises of two domains. The C-terminal domain contains the binding site for glutamine and catalyzes the hydrolysis of this substrate to glutamate and ammonia. The N-terminal domain is anticipated to bind ATP, and cobyrinate or Ni-sirohydrochlorin, and catalyzes the ultimate synthesis of the diamide product. The ammonia produced via the glutaminase domain is probably translocated to the adjacent domain via a molecular tunnel, where it reacts with an activated intermediate.
The a and c carboxylates of cobyrinate and Ni-sirohydrochlorin are activated for nucleophilic attack via formation of a phosphorylated intermediate by ATP. CbiA catalyzes first the amidation of the c-carboxylate, and then that of the a-carboxylate.
Catalyzes the reversible interconversion of 5-formyl-H(4)MPT to methenyl-H(4)MPT(+).
Belongs to the universal ribosomal protein uL6 family.
This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.
Belongs to the glutaminase PdxT/SNO family.
Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
In the presence of PdxS, forms a dodecamer of heterodimers. Only shows activity in the heterodimer.
Belongs to the type-I 3-dehydroquinase family.
Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.
Belongs to the DNA polymerase delta/II small subunit family.
Heterodimer of a large subunit and a small subunit.
Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3' to 5' direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).
Anion-transporting ATPase. Catalyzes the extrusion of arsenite (By similarity).
Despite a certain similarity to selA, this is not selA (see AC Q57622).
Belongs to the carbohydrate kinase PfkB family.
Catalyzes the phosphorylation of a wide range of nucleosides to yield nucleoside monophosphates, using ATP, ITP or GTP as phosphate donor.
Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.
Belongs to the universal ribosomal protein uL2 family.
One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome.
Part of the 50S ribosomal subunit. Forms a bridge to the 30S subunit in the 70S ribosome.
Belongs to the GatB/GatE family. GatE subfamily.
Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
The covalent binding to the substrate causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein.
Belongs to the universal ribosomal protein uL15 family.
Belongs to the archaeal DnaG primase family.
Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.
RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.
Belongs to the Mg-chelatase subunits D/I family.
Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate.
Belongs to the radical SAM superfamily. NifB family.
Belongs to the histone deacetylase family.
Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.
Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.
Belongs to the anthranilate phosphoribosyltransferase family.
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
Belongs to the CobB/CobQ family. CobQ subfamily.
Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation (By similarity).
Belongs to the universal ribosomal protein uS11 family.
Located on the platform of the 30S subunit.
Belongs to the metallophosphoesterase superfamily. YfcE family.
Binds 2 divalent metal cations per subunit. The ions could be magnesium and/or manganese.
Catalyzes the GTP-dependent successive addition of two or more gamma-linked L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form coenzyme F420-0-glutamyl-glutamate (F420-2) or polyglutamated F420 derivatives.
Monovalent cation. The ion could be potassium.
Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction.
Belongs to the eukaryotic-type primase large subunit family.
Heterodimer of a small subunit (PriS) and a large subunit (PriL).
Regulatory subunit of DNA primase, an RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Stabilizes and modulates the activity of the small subunit, increasing the rate of DNA synthesis, and conferring RNA synthesis capability. The DNA polymerase activity may enable DNA primase to also catalyze primer extension after primer synthesis. May also play a role in DNA repair.
Belongs to the archaeal Rpo3/eukaryotic RPB3 RNA polymerase subunit family.
X-ray crystallography in other archaea shows this protein binds a 3Fe-4S cluster, although a 4Fe-4S cluster has been suggested to be present in this protein.
MCR is composed of three subunits: alpha, beta, and gamma. The function of proteins C and D is not known.
There are two MCR complexes in this bacteria. MCR II is expressed in the early growth phase. Late growth cells contains mostly MCR I.
Belongs to the phosphosulfolactate synthase family.
Catalyzes the addition of sulfite to phosphoenolpyruvate (PEP) to yield (2R)-phospho-3-sulfolactate (PSL).
Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction.
Belongs to the CRISPR-associated Csm5 family.
This subunit might be involved in maturation of a crRNA intermediate to its mature form.
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Binds 3 Mg(2+) cations per subunit. The strongest magnesium site (Mg1) is bound to the beta- and gamma-phosphates of ATP and four water molecules complete its coordination sphere.
Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Belongs to the archaeal phosphopantothenate synthetase family.
Catalyzes the condensation of (R)-4-phosphopantoate and beta-alanine to 4'-phosphopantothenate in the CoA biosynthesis pathway.
Belongs to the eukaryotic release factor 1 family. Pelota subfamily.
May function in recognizing stalled ribosomes, interact with stem-loop structures in stalled mRNA molecules, and effect endonucleolytic cleavage of the mRNA. May play a role in the release non-functional ribosomes and degradation of damaged mRNAs. Has endoribonuclease activity.
The N-terminal domain has the RNA-binding Sm fold. It harbors the endoribonuclease activity.
MCR is composed of three subunits: alpha, beta, and gamma. The function of protein D is not known.
Heterotrimer of the VorA, VorB and VorC subunits.
Belongs to the group II decarboxylase family. MfnA subfamily.
Catalyzes the decarboxylation of L-tyrosine to produce tyramine for methanofuran biosynthesis. Can also catalyze the decarboxylation of L-aspartate to produce beta-alanine for coenzyme A (CoA) biosynthesis.
Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
The N-terminal domain is an archaea-specific tRNA-editing domain that hydrolyzes incorrectly charged L-seryl-tRNA(Thr). Catalysis of tRNA editing is performed by the charged tRNA itself.
Essential for tRNA splicing and maturation. Acts by directly joining spliced tRNA halves to mature-sized tRNAs. Joins RNA with 2',3'-cyclic-phosphate or 3'-phosphate ends to RNA with 5'-hydroxy ends.
Ligation proceeds through 3 nucleotidyl transfer steps, with 2',3'-cyclic phosphate termini being hydrolyzed to 3'-P termini in a step that precedes 3'-P activation with GMP. In the first nucleotidyl transfer step, RtcB reacts with GTP to form a covalent RtcB-histidine-GMP intermediate with release of PPi; in the second step, the GMP moiety is transferred to the RNA 3'-P; in the third step, the 5'-OH from the opposite RNA strand attacks the activated 3'-P to form a 3',5'-phosphodiester bond and release GMP.
Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
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 Ser-tRNA(Ala) and Gly-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.
DNA polymerase is inhibited by replication protein A (RPA), while 3'-5' exonuclease activity is not. Polymerase inhibition can be overcome by replication factor C (RFC) and PCNA.
Formed of a complex between PolB1 and PolB2; the exonuclease activity is associated with subunit 1. Probably binds replication protein A (RPA).
In addition to polymerase activity, this DNA polymerase exhibits 3'-5' exonuclease activity.
In some Methanobacteriaceae the PolB protein is split over 2 genes.
Belongs to the eukaryotic ribosomal protein eL21 family.
In the C-terminal section; belongs to the transferase hexapeptide repeat family.
In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family.
Belongs to the thiamine-monophosphate kinase family.
Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.
Reaction mechanism of ThiL seems to utilize a direct, inline transfer of the gamma-phosphate of ATP to TMP rather than a phosphorylated enzyme intermediate.
Component of the archaeal exosome complex. Forms a trimer of Rrp4 and/or Csl4 subunits. The trimer associates with an hexameric ring-like arrangement composed of 3 Rrp41-Rrp42 heterodimers. Interacts with DnaG.
Non-catalytic component of the exosome, which is a complex involved in RNA degradation. Increases the RNA binding and the efficiency of RNA degradation. Helpful for the interaction of the exosome with A-poor RNAs.
Belongs to the ketol-acid reductoisomerase family.
Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
Monomer. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).
Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon complex generates CO from CO(2), while the beta subunit (this protein) combines the CO with CoA and a methyl group to form acetyl-CoA. The methyl group, which is incorporated into acetyl-CoA, is transferred to the beta subunit by a corrinoid iron-sulfur protein (the gamma-delta complex).
Belongs to the V-ATPase proteolipid subunit family.
Belongs to the eukaryotic RPB7/RPC8 RNA polymerase subunit family.
Forms 2 domains with an elongated structure; Rpo4 packs into the hinge region between the 2 domains.
Part of the RNA polymerase complex. Forms a stalk with Rpo4 that extends from the main structure.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. IF-2 subfamily.
Function in general translation initiation by promoting the binding of the formylmethionine-tRNA to ribosomes. Seems to function along with eIF-2 (By similarity).
Belongs to the universal ribosomal protein uL18 family.
Part of the 50S ribosomal subunit. Contacts the 5S and 23S rRNAs.
This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.
Belongs to the archaeal riboflavin kinase family.
Catalyzes the CTP-dependent phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN).
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF (By similarity).
Belongs to the eukaryotic ribosomal protein P1/P2 family.
Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.
Part of the 50S ribosomal subunit. Homodimer, it forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Forms a heptameric L10(L12)2(L12)2(L12)2 complex, where L10 forms an elongated spine to which the L12 dimers bind in a sequential fashion.
Belongs to the archaeal NMN adenylyltransferase family.
The reversible ADP-ribosylation of Arg-100 inactivates the nitrogenase reductase and regulates nitrogenase activity.
Belongs to the phosphatidylserine decarboxylase family. PSD-A subfamily.
Binds 1 pyruvoyl group covalently per subunit.
Catalyzes the formation of archaetidylethanolamine (PtdEtn) from archaetidylserine (PtdSer).
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 post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, 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.
Belongs to the aspartate/ornithine carbamoyltransferase superfamily. OTCase family.
Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline.
Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily.
Binds 1 pyridoxal phosphate per subunit.
May also have succinyldiaminopimelate aminotransferase activity, thus carrying out the corresponding step in lysine biosynthesis.
Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA).
Belongs to the MIP/aquaporin (TC 1.A.8) family.
Channel that permits osmotically driven movement of water in both directions. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity. Exhibits also a transient but reproducible increase in the initial glycerol flux (By similarity).
Belongs to the inositol monophosphatase superfamily. FBPase class 4 family.
Phosphatase with broad specificity; it can dephosphorylate fructose 1,6-bisphosphate, and both D and L isomers of inositol-1-phosphate (I-1-P).
Belongs to the adenosylhomocysteinase family.
Catalyzes the hydrolysis of S-inosyl-L-homocysteine (SIH) to L-homocysteine (Hcy) and inosine. Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions. Can also catalyze the reverse reaction in vitro, i.e. the synthesis of SIH from Hcy and inosine.
SAH is a product of SAM methyltransferases and is known to be a feedback inhibitor of these enzymes. As a result of this inhibition, organisms have evolved efficient enzymes to metabolize SAH via different pathways. The pathway found in methanogens differs from the canonical pathway, it uses the deamination of S-adenosyl-L-homocysteine to form S-inosyl-L-homocysteine for the regeneration of SAM from S-adenosyl-L-homocysteine.
Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. May hydrolyze nucleoside diphosphates with lower efficiency.
Functions by promoting the formation of the first peptide bond.
Belongs to the universal ribosomal protein uS3 family.
Binds the lower part of the 30S subunit head.
Belongs to the universal ribosomal protein uL1 family.
Binds directly to 23S rRNA. Probably involved in E site tRNA release.
Protein L1 is also a translational repressor protein, it controls the translation of its operon by binding to its mRNA.
Belongs to the ammonia transporter channel (TC 1.A.11.2) family.
The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Component of the Sec protein translocase complex. Heterotrimer consisting of SecY (alpha), SecG (beta) and SecE (gamma) subunits. The heterotrimers can form oligomers, although 1 heterotrimer is thought to be able to translocate proteins. Interacts with the ribosome. May interact with SecDF, and other proteins may be involved.
Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Belongs to the ferredoxin thioredoxin reductase beta subunit family.
Catalytic subunit of the ferredoxin-thioredoxin reductase (FTR), which catalyzes the two-electron reduction of thioredoxins by the electrons provided by reduced ferredoxin.
Heterodimer of subunit A (variable subunit) and subunit B (catalytic subunit). Heterodimeric FTR forms a complex with ferredoxin and thioredoxin.
Belongs to the autoinducer-2 exporter (AI-2E) (TC 2.A.86) family.
Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 2 subfamily.
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).
Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Belongs to the eukaryotic ribosomal protein eL43 family. Putative zinc-binding subfamily.
Belongs to the methyl-coenzyme M reductase alpha subunit family.
The alpha subunit contains six modified amino acids near the active site region. Is methylated on His-257, Arg-271, Gln-400 and Cys-452, probably by the action of specific S-adenosylmethionine-dependent methyltransferases. Also contains a thioglycine at position 445, forming a thiopeptide bond. Contains a didehydroaspartate residue at position 450 (By similarity). The methylation on C5 of Arg-271 is a post-translational methylation not essential in vivo, but which plays a role for the stability and structural integrity of MCR (By similarity).
Belongs to the ATP phosphoribosyltransferase family. Long subfamily.
Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity (By similarity).
Heterodimer of delta and gamma chains. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).
Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2).
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit (By similarity).
Involved in the biosynthesis of the thiazole moiety of thiamine. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylate (ADT), an adenylated thiazole intermediate, using free sulfide as a source of sulfur.
DNA-binding protein which can interact with a randomly chosen 20-mer of double-stranded DNA.
Belongs to the eukaryotic/archaeal RNase P protein component 3 family.
Belongs to the CRISPR-associated Csm4 family.
Belongs to the adenylosuccinate synthetase family.
Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Belongs to the DEAD box helicase family.
Component of the archaeal exosome complex. Forms a trimer of Rrp4 and/or Csl4 subunits. The trimer associates with a hexameric ring-like arrangement composed of 3 Rrp41-Rrp42 heterodimers.
Non-catalytic component of the exosome, which is a complex involved in RNA degradation. Increases the RNA binding and the efficiency of RNA degradation. Confers strong poly(A) specificity to the exosome.
Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal beta chain is a regulatory subunit.
Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.
Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Belongs to the universal ribosomal protein uS7 family.
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center.
Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family. RsmA subfamily.
Specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Belongs to the eukaryotic/archaeal RNase P protein component 1 family.
Belongs to the PINc/VapC protein family.
Has 2 structurally independent domains; the N-terminal PINc domain which binds Mn(2+), rRNA substrate and probably has endoribonuclease activity, and the C-terminal zinc ribbon domain which also binds rRNA substrate.
Toxic component of a type II toxin-antitoxin (TA) system. Processes pre-16S-rRNA at its 3' end (the D-site) to yield the mature 3' end (By similarity).
Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.
Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.
Acts to maintain redox homeostasis; functions as a protein disulfide reductase.
Belongs to the universal ribosomal protein uS2 family.
Belongs to the RNase PH family. Rrp41 subfamily.
Catalytic component of the exosome, which is a complex involved in RNA degradation. Has 3'->5' exoribonuclease activity. Can also synthesize heteromeric RNA-tails.
Component of the archaeal exosome complex. Forms a hexameric ring-like arrangement composed of 3 Rrp41-Rrp42 heterodimers. The hexameric ring associates with a trimer of Rrp4 and/or Csl4 subunits.
Monomer. Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ and 2 PurS subunits.
Forms membrane-associated dynamic filaments that are essential for cell shape determination. Acts by regulating cell wall synthesis and cell elongation, and thus cell shape. A feedback loop between cell geometry and MreB localization may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature.
Could be involved in the regulation of nitrogen fixation.
General factor that plays a role in the activation of archaeal genes transcribed by RNA polymerase. Binds specifically to the TATA box promoter element which lies close to the position of transcription initiation (By similarity).
Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Part of a complex that catalyzes the formation of methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and methyl-tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step. MtrH catalyzes the transfer of the methyl group from methyl-tetrahydromethanopterin to the corrinoid prosthetic group of MtrA.
An RNase that has 5'-3' exonuclease activity. May be involved in RNA degradation.
Belongs to the metallo-beta-lactamase superfamily. RNA-metabolizing metallo-beta-lactamase-like family. Archaeal RNase J subfamily.
Binds 2 Zn(2+) ions per subunit. It is not clear if Zn(2+) or Mg(2+) is physiologically important.
Belongs to the AB hydrolase superfamily. MetX family.
Belongs to the RNase PH family. Rrp42 subfamily.
Non-catalytic component of the exosome, which is a complex involved in RNA degradation. Contributes to the structuring of the Rrp41 active site.
Binds and compacts DNA (95 to 150 base pairs) to form nucleosome-like structures that contain positive DNA supercoils.
Homodimer or heterodimer with HmtB (By similarity). Dimers then assemble into higher oligomers, with the DNA wrapped around the protein core (By similarity).
Component of the protein translocase complex. Heterotrimer consisting of alpha (SecY), beta (SecG) and gamma (SecE) subunits. Can form oligomers of the heterotrimer (By similarity).
Involved in protein export. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex (By similarity).
Belongs to the eukaryotic ribosomal protein eL24 family.
Part of the 50S ribosomal subunit. Forms a cluster with proteins L3 and L14.
Belongs to the RNA polymerase beta' chain family.
DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Forms the clamp head domain.
Belongs to the tRNA pseudouridine synthase TruA family.
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Belongs to the V-ATPase F subunit family.
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Belongs to the GatB/GatE family. GatB subfamily.
Belongs to the isopentenyl phosphate kinase family.
Catalyzes the formation of isopentenyl diphosphate (IPP), the building block of all isoprenoids. Has lower activity with dimethylallyl phosphate (DMAP) and isopentenyl thiolophosphate (ISP). Has low activity with 1-butyl phosphate (BP) and 3-buten-1-yl phosphate (BEP). Has no significant activity with geranyl phosphate (in vitro).
Belongs to the binding-protein-dependent transport system permease family.
Belongs to the eukaryotic RecA-like protein family. RadB subfamily.
Involved in DNA repair and in homologous recombination. May regulate the cleavage reactions of the branch-structured DNA. Has a very weak ATPase activity that is not stimulated by DNA. Binds DNA but does not promote DNA strands exchange (By similarity).
Belongs to the glycerol-1-phosphate dehydrogenase family.
Catalyzes the NAD(P)H-dependent reduction of dihydroxyacetonephosphate (DHAP or glycerone phosphate) to glycerol 1-phosphate (G1P). The G1P thus generated is used as the glycerophosphate backbone of phospholipids in the cellular membranes of Archaea. Is also able to catalyze the reverse reaction, i.e. the NAD(P)(+)-dependent oxidation of G1P but not of G3P. Is not active toward glycerol, dihydroxyacetone, glyceraldehyde-3-phosphate, glyceraldehyde and glycerol-2-phosphate.
G1PDH is a pro-R type dehydrogenase, which selectively transfers the pro-R hydrogen from NADH to dihydroxyacetonephosphate.
Partially inhibited by divalent metal cations such as Co(2+), Cu(2+) and Ni(2+).
Belongs to the class-II aminoacyl-tRNA synthetase family. O-phosphoseryl-tRNA(Cys) synthetase subfamily.
Catalyzes the attachment of O-phosphoserine (Sep) to tRNA(Cys).
Belongs to the prefoldin subunit alpha family.
Heterohexamer of two alpha and four beta subunits.
Molecular chaperone capable of stabilizing a range of proteins. Seems to fulfill an ATP-independent, HSP70-like function in archaeal de novo protein folding.
Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.
Belongs to the eukaryotic ribosomal protein eS31 family.
Belongs to the CDP-glycerol glycerophosphotransferase family.
Homotrimer. The subunits circularize to form a toroid; DNA passes through its center. Replication factor C (RFC) is required to load the toroid on the DNA.
Sliding clamp subunit that acts as a moving platform for DNA processing. Responsible for tethering the catalytic subunit of DNA polymerase to DNA during high-speed replication (By similarity). In conjunction with replication factor C (RFC) stimulates DNA synthesis by PolB, relieving inhibition by replication protein A (RPA).
Belongs to the quinolinate synthase family. Type 2 subfamily.
Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
Belongs to the archaeal-type GTP cyclohydrolase family.
Catalyzes the formation of 2-amino-5-formylamino-6-ribofuranosylamino-4(3H)-pyrimidinone ribonucleotide monophosphate and inorganic phosphate from GTP. Also has an independent pyrophosphate phosphohydrolase activity.
Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily.
Belongs to the diphthine synthase family.
S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.
By growth on tungsten or molybdenum under anaerobic conditions.
Catalyzes the reversible oxidation of CO(2) and methanofuran (MFR) to N-formylmethanofuran (CHO-MFR). Can only oxidize formylmethanofuran. This enzyme is oxygen-labile.
This enzyme is composed of seven subunits FwdA (65 kDa), FwdB (53 kDa), FwdC (31 kDa), FwdD (15 kDa), FwdE, FwdF and FwdG.
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.
Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently (By similarity). May also act as a chaperone or modulator of proteins involved in DNA or RNA processing.
Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds directly to 7S RNA and mediates binding of the 54 kDa subunit of the SRP.
Belongs to the HMG-CoA reductase family.
Belongs to the pseudouridine synthase Pus10 family.
Responsible for synthesis of pseudouridine from uracil-54 and uracil-55 in the psi GC loop of transfer RNAs.
Belongs to the universal ribosomal protein uL29 family.
Belongs to the archaeal IMP cyclohydrolase family.
Catalyzes the cyclization of 5-formylamidoimidazole-4-carboxamide ribonucleotide to IMP.
Forms a heterotetramer with UvrA during the search for lesions. Interacts with UvrC in an incision complex.
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
The beta-hairpin motif is involved in DNA binding.
Seems to be required for maximal rate of protein biosynthesis. Enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal subunits (By similarity).
Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.
Homodimer. Polymerizes to form a dynamic ring structure in a strictly GTP-dependent manner. Interacts directly with several other division proteins.
Heterotetramer of the KorA, KorB, KorC and KorD subunits.
Belongs to the CRISPR-associated Csm3 family.
CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). The type III-A Csm effector complex binds crRNA and acts as a crRNA-guided RNase, DNase and cyclic oligoadenylate synthase; binding of target RNA cognate to the crRNA is required for all activities.
Part of the Csm effector complex that includes Cas10, Csm2, Csm3, Csm4 and Csm5.
This subunit has the target ssRNA endonuclease activity; it cleaves multiple sites in the target RNA at 6 nucleotide intervals.
Belongs to the methyl-coenzyme M reductase beta subunit family.
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. PCNA stimulates the nuclease activity without altering cleavage specificity.
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. Binds the unpaired 3'-DNA end and kinks the DNA to facilitate 5' cleavage specificity. Cleaves one nucleotide into the double-stranded DNA from the junction in flap DNA, leaving a nick for ligation. Also involved in the base excision repair (BER) pathway. 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 (By similarity).
Belongs to the PEP-utilizing enzyme family.
Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. In the second step the latter compound is decarboxylated to form 4'-phosphopantotheine.
In the C-terminal section; belongs to the PPC synthetase family.
In the N-terminal section; belongs to the HFCD (homo-oligomeric flavin containing Cys decarboxylase) superfamily.
Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.
Catalyzes the reversible phosphorylation of UMP to UDP.
Participates in transcription termination.
By growth on molybdenum, under anaerobic conditions.
Consists of five subunits; FmdA, FmdB, FmdC, FmdD, and FmdE.
In the C-terminal section; belongs to the molybdenum dinucleotide binding protein family.
In the N-terminal section; belongs to the FwdC/FmdC family.
Belongs to the universal ribosomal protein uS10 family.
Involved in the binding of tRNA to the ribosomes.
Belongs to the eukaryotic ribosomal protein eL30 family.
Belongs to the [NiFe]/[NiFeSe] hydrogenase small subunit family.
Part of a complex that provides reducing equivalents for heterodisulfide reductase.
Belongs to the ribose-phosphate pyrophosphokinase family. Class III (archaeal) subfamily.
Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P).
Belongs to the universal ribosomal protein uL16 family.
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.
Heterotrimer composed of an alpha, a beta and a gamma chain.
eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA.
Belongs to the desulfoferrodoxin family.
Binds 1 Fe(2+) ion per subunit. The iron ion 2 is coordinated via four histidines and one cysteine residue.
Binds 1 Fe(3+) ion per subunit. The iron ion 1 is coordinated via 4 cysteine residues.
Belongs to the archaeal Rpo10/eukaryotic RPB10 RNA polymerase subunit family.
Part of the binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
Stabilizes TBP binding to an archaeal box-A promoter. Also responsible for recruiting RNA polymerase II to the pre-initiation complex (DNA-TBP-TFIIB).
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.
Binds 2 magnesium or manganese ions per subunit.
Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with geranylgeranyl diphosphate (GGPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30E,34E,38E)-undecaprenyl diphosphate (tritrans,heptacis-UPP). It is probably the precursor of glycosyl carrier lipids.
Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.
Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.
The RCK N-terminal domain binds NAD and possibly other effectors. This is expected to cause a conformation change that regulates potassium transport (By similarity).
Catalyzes the condensation of alpha-ketoglutarate and acetyl-CoA to form (R)-homocitrate. Can also catalyze the condensation of alpha-ketoadipate with acetyl-CoA to form (R)-homo(2)citrate, and the condensation of alpha-ketopimelate with acetyl-CoA to form (R)-homo(3)citrate. These reactions are part of the biosynthesis pathway of coenzyme B and biotin.
Belongs to the universal ribosomal protein uS12 family.
With S4 and S5 plays an important role in translational accuracy. Located at the interface of the 30S and 50S subunits.
Binds 1 [7Fe-Mo-9S-C-homocitryl] cluster per subunit.
Belongs to the aconitase/IPM isomerase family. LeuC type 2 subfamily.
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Belongs to the universal ribosomal protein uS8 family.
One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit.
Belongs to the SecD/SecF family. SecD subfamily.
Part of the protein translocation apparatus. Forms a complex with SecF.
ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPase-20S proteasome association which triggers gate opening, and supports translocation of unfolded substrates.
Consists of three main regions, an N-terminal coiled-coil domain that may assist in substrate recognition, an interdomain involved in PAN hexamerization, and a C-terminal ATPase domain of the AAA type.
Homohexamer. The hexameric complex has a two-ring architecture resembling a top hat that caps the 20S proteasome core at one or both ends. Upon ATP-binding, the C-terminus of PAN interacts with the alpha-rings of the proteasome core by binding to the intersubunit pockets.
Belongs to the LDH2/MDH2 oxidoreductase family.
Catalyzes the reduction of sulfopyruvate to (R)-sulfolactate. Involved in the biosynthesis of both coenzyme M (with (R)-sulfolactate) and methanopterin (with alpha-ketoglutarate) (By similarity).
Belongs to the GGGP/HepGP synthase family. Group II subfamily.
Homotetramer (PubMed:21761520). Homohexamer (PubMed:24684232).
Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P). This reaction is the first ether-bond-formation step in the biosynthesis of archaeal membrane lipids.
Belongs to the trehalose phosphatase family.
Removes the phosphate from trehalose 6-phosphate to produce free trehalose.
Belongs to the glutamine synthetase family.
Oligomer of 12 subunits arranged in the form of two hexagons.
Probably involved in nitrogen metabolism via ammonium assimilation. Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia.
Probably part of an ABC transporter complex. Responsible for energy coupling to the transport system.
Catalyzes the reversible reduction of methylene-H(4)MPT to methyl-H(4)MPT.
Increase in abundance from the earliest stages of exponential growth, reaching a maximum level at the mid-exponential growth phase.
Contacts the emerging nascent chain on the ribosome.
Homodimer. Interacts with the ribosome. Binds ribosomal RNA.
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 (By similarity).
Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EIF2G subfamily.
Belongs to the eukaryotic release factor 1 family.
Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA.
Heterodimer of two subunits, one of which binds GTP.
Belongs to the universal ribosomal protein uL5 family.
Part of the 50S ribosomal subunit; contacts the 5S rRNA and probably tRNA. Forms a bridge to the 30S subunit in the 70S ribosome.
This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. May contact the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.
Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Belongs to the UDP-glucose/GDP-mannose dehydrogenase family.
A single active site specifically recognizes both ATP and CTP and is responsible for their addition.
Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.
Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.
Catalyzes the reversible interconversion of serine and glycine with tetrahydromethanopterin (H4MPT) serving as the one-carbon carrier. Cannot use tetrahydrofolate (THF or H4PteGlu) instead of H4MPT as the pteridine substrate. Also probably exhibits a pteridine-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalyzes the ATP- and formate-dependent formylation of 5-aminoimidazole-4-carboxamide-1-beta-d-ribofuranosyl 5'-monophosphate (AICAR) to 5-formaminoimidazole-4-carboxamide-1-beta-d-ribofuranosyl 5'-monophosphate (FAICAR) in the absence of folates.
Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.
The 20S proteasome core is composed of 14 alpha and 14 beta subunits that assemble into four stacked heptameric rings, resulting in a barrel-shaped structure. The two inner rings, each composed of seven catalytic beta subunits, are sandwiched by two outer rings, each composed of seven alpha subunits. The catalytic chamber with the active sites is on the inside of the barrel. Has a gated structure, the ends of the cylinder being occluded by the N-termini of the alpha-subunits. Is capped at one or both ends by the proteasome regulatory ATPase, PAN.
The formation of the proteasomal ATPase PAN-20S proteasome complex, via the docking of the C-termini of PAN into the intersubunit pockets in the alpha-rings, triggers opening of the gate for substrate entry. Interconversion between the open-gate and close-gate conformations leads to a dynamic regulation of the 20S proteasome proteolysis activity.
Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 3 subfamily.
Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Belongs to the universal ribosomal protein uS17 family.
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
Belongs to the CRISPR-associated exonuclease Cas4 family.
CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA).
Mg(2+) or Mn(2+) required for ssDNA cleavage activity.
Binds 1 5-hydroxybenzimidazolylcobamide group.
Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
Belongs to the GTP-dependent DPCK family.
Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).
Not known. Could have a role in a phosphorylation-independent two-component response regulator system.
Belongs to the HAD-like hydrolase superfamily.
Catalyzes the dephosphorylation of D,L-glyceraldehyde 3-phosphate in vitro.
Belongs to the universal ribosomal protein uL10 family.
Part of the 50S ribosomal subunit. Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Forms a heptameric L10(L12)2(L12)2(L12)2 complex, where L10 forms an elongated spine to which the L12 dimers bind in a sequential fashion.
Belongs to the EF-1-beta/EF-1-delta family.
Promotes the exchange of GDP for GTP in EF-1-alpha/GDP, thus allowing the regeneration of EF-1-alpha/GTP that could then be used to form the ternary complex EF-1-alpha/GTP/AAtRNA.
Belongs to the succinate/malate CoA ligase beta subunit family.
Heterotetramer of two alpha and two beta subunits.
Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP 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.
Although this enzyme belongs to the family of MTA phosphorylases based on sequence homology, it has been shown that conserved amino acid substitutions in the substrate binding pocket convert the substrate specificity of this enzyme from 6-aminopurines to 6-oxopurines.
Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.
Catalyzes the reversible phosphorylation of S-methyl-5'-thioinosine (MTI) to hypoxanthine and 5-methylthioribose-1-phosphate. Involved in the breakdown of S-methyl-5'-thioadenosine (MTA), a major by-product of polyamine biosynthesis. Catabolism of (MTA) occurs via deamination to MTI and phosphorolysis to hypoxanthine.
Aminocarboxypropyltransferase that catalyzes the aminocarboxypropyl transfer on pseudouridine corresponding to position 914 in M.jannaschii 16S rRNA. It constitutes the last step in biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi).
Belongs to the TDD superfamily. TSR3 family.
Monomer (By similarity). Interaction with RNA polymerase subunits RpoF and RpoE is necessary for Tfe stimulatory transcription activity. Able to interact with RNA polymerase in the absence of Tbp or DNA promoter. Interacts both with the preinitiation and elongation complexes (By similarity).
The winged helix domain is involved in binding to DNA in the preinitiation complex.
Transcription factor that plays a role in the activation of archaeal genes transcribed by RNA polymerase. Facilitates transcription initiation by enhancing TATA-box recognition by TATA-box-binding protein (Tbp), and transcription factor B (Tfb) and RNA polymerase recruitment. Not absolutely required for transcription in vitro, but particularly important in cases where Tbp or Tfb function is not optimal. It dynamically alters the nucleic acid-binding properties of RNA polymerases by stabilizing the initiation complex and destabilizing elongation complexes. Seems to translocate with the RNA polymerase following initiation and acts by binding to the non template strand of the transcription bubble in elongation complexes.
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.
The alpha subunit contains six modified amino acids near the active site region. Is methylated on His-260, Arg-274, Gln-402 and Cys-454, probably by the action of specific S-adenosylmethionine-dependent methyltransferases. Also contains a thioglycine at position 447, forming a thiopeptide bond. Contains a didehydroaspartate residue at position 452 (By similarity). The methylation on C5 of Arg-274 is a post-translational methylation not essential in vivo, but which plays a role for the stability and structural integrity of MCR (By similarity).
Belongs to the 2H phosphoesterase superfamily. ThpR family.
Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
Belongs to the DNA polymerase type-B family.
Homodimer or heterodimer with HmtB (PubMed:1459937). Dimers then assemble into higher oligomers, with the DNA wrapped around the protein core (By similarity).
Belongs to the eukaryotic/archaeal RNase P protein component 2 family.
Belongs to the acetylglutamate kinase family. ArgB subfamily.
Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalyzes the transfer of a methyl group to L-homocysteine resulting in methionine formation. Can use methylcobalamin and methylcobinamide as methyl donors, but methylcobalamin is not considered to be the physiological substrate.
Belongs to the prefoldin subunit beta family.
Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 2 subfamily.
Belongs to the complex I 24 kDa subunit family.
Methyltransferase that likely catalyzes the ring contraction and methylation of C-17 in cobalt-factor III to form cobalt-factor IV. May also convert cobalt-precorrin-3 to cobalt-precorrin-4 (By similarity).
Belongs to the arginase family. Agmatinase subfamily.
Belongs to the eukaryotic ribosomal protein eL40 family.
Belongs to the eukaryotic ribosomal protein eS27 family.
Belongs to the methyltransferase superfamily. Trm-G10 family.
Catalyzes the adenosylmethionine-dependent methylation of the exocyclic amino group (N(2)) of guanosine at position 10 of various tRNAs. Acts via a two-step process that leads to the formation of either N(2)-monomethyl (m(2)G) or N(2)-dimethylguanosine (m(2)(2)G) (By similarity).
Catalyzes the reversible oxidation of CO(2) and methanofuran (MFR) to N-formylmethanofuran (CHO-MFR). This enzyme is oxygen-labile.
This enzyme is composed of six subunits FwdA, FwdC, FwdD, FwdE, FwdF and FwdG.
Belongs to the SMC family. RAD50 subfamily.
Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Rad50 controls the balance between DNA end bridging and DNA resection via ATP-dependent structural rearrangements of the Rad50/Mre11 complex.
The two conserved Cys that bind zinc constitute the zinc-hook, which separates the large intramolecular coiled coil regions. The 2 Cys residues coordinate one molecule of zinc with the help of the 2 Cys residues of the zinc-hook of another Rad50 molecule, thereby forming a V-shaped homodimer.
Belongs to the ribonucleoside diphosphate reductase class-2 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 DNA repair enzymes AP/exoA family.
Depletion leads to the loss of DNA-U repair.
Involved in DNA uracil repair (PubMed:17012282, PubMed:19240141, PubMed:20129830). Recognizes DNA uracil residues within double-stranded DNA and initiates DNA-U repair by endonucleotic incision on the 5'-side of the 2'-d-uridine residue, irrespective of the nature of the opposing nucleotide (PubMed:17012282, PubMed:19240141, PubMed:20129830). In addition, acts as an apurinic/apyrimidinic (AP) endonuclease hydrolyzing the DNA phosphodiester backbone immediately at the 5'-side of AP sites, and as a 3'-5' exonuclease (PubMed:15725624, PubMed:17012282). Strongly binds to double-stranded DNA (PubMed:15725624).
The insertion of the side chain of Arg-209 into the DNA helical base stack seems to be crucial for the uridine recognition.
Belongs to the metallo-dependent hydrolases superfamily. Adenine deaminase family.
Involved in the catabolism of quinolinic acid (QA).
Belongs to the eukaryotic ribosomal protein eS4 family.