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.
Tetramer of two alpha and two beta chains.
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Belongs to the universal ribosomal protein uS10 family.
Involved in the binding of tRNA to the ribosomes.
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.
Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine.
In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase 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.
Belongs to the cytidylate kinase family. Type 2 subfamily.
Belongs to the methyltransferase superfamily. TrmY family.
Lacks conserved residue(s) required for the propagation of feature annotation.
Specifically catalyzes the N1-methylation of pseudouridine at position 54 (Psi54) in tRNAs.
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 lyase 1 family. Adenylosuccinate lyase subfamily.
Homotetramer. Residues from neighboring subunits contribute catalytic and substrate-binding residues to each active site.
Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily.
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 involved in tRNA binding.
Homodimer. The tRNA molecule binds across the dimer.
Belongs to the GGGP/HepGP synthase family. Group II subfamily.
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 archaeal Rpo6/eukaryotic RPB6 RNA polymerase subunit family.
DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
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).
Belongs to the deoxyhypusine synthase family.
Belongs to the adenosylhomocysteinase family.
May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine.
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.
Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.
Belongs to the triosephosphate isomerase family.
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Belongs to the eukaryotic ribosomal protein eL21 family.
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Belongs to the universal ribosomal protein uL2 family.
Belongs to the isopentenyl phosphate kinase family.
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.
Belongs to the universal ribosomal protein uS11 family.
Located on the platform of the 30S subunit.
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 universal ribosomal protein uS9 family.
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.
Monomer. 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.
Belongs to the HAD-like hydrolase superfamily.
Belongs to the class-I aminoacyl-tRNA synthetase family.
Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated.
This enzyme catalyzes only one turnover and therefore is not strictly catalytic. According to one definition, an enzyme is a biocatalyst that acts repeatedly and over many reaction cycles.
Belongs to the thiolase-like superfamily. Thiolase family.
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 archaeal Rpo3/eukaryotic RPB3 RNA polymerase subunit family.
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.
Homodimer. Heterotetramer of two Top6A and two Top6B chains.
Relaxes both positive and negative superturns and exhibits a strong decatenase activity.
Belongs to the universal ribosomal protein uL16 family.
Belongs to the eukaryotic ribosomal protein eL30 family.
Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.
Although this enzyme belongs to the family of MTA phosphorylases based on sequence homology, it lacks several conserved amino acids in the substrate binding pocket that confer specificity towards MTA.
Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.
Purine nucleoside phosphorylase involved in purine salvage.
Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.
Belongs to the eukaryotic ribosomal protein eS17 family.
Catalyzes the synthesis of GMP from XMP.
Heterodimer composed of a glutamine amidotransferase subunit (A) and a GMP-binding subunit (B).
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 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 uracil-DNA glycosylase (UDG) superfamily. Type 4 (UDGa) family.
Belongs to the eukaryotic/archaeal RNase P protein component 4 family.
Consists of a catalytic RNA component and at least 4-5 protein subunits.
Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
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-Tu/EF-1A subfamily.
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Belongs to the universal ribosomal protein uS15 family.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EIF2G subfamily.
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 universal ribosomal protein uL15 family.
Belongs to the snRNP Sm proteins 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. Forms part of the jaw domain.
Heterodimer composed of Spt4 and Spt5. Interacts with RNA polymerase (RNAP).
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.
Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.
Belongs to the NifD/NifK/NifE/NifN family.
Belongs to the HMG-CoA reductase 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 heteropolymeric 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.
Belongs to the alpha-IPM synthase/homocitrate synthase family.
Belongs to the pseudouridine synthase TruB family. Type 2 subfamily.
Could be responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
Belongs to the archaeal riboflavin kinase family.
Catalyzes the CTP-dependent phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN).
Belongs to the universal ribosomal protein uL30 family.
Belongs to the GHMP kinase family. PoK subfamily.
Phosphorylates (R)-pantoate to form (R)-4-phosphopantoate in the CoA biosynthesis pathway.
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 class-II aminoacyl-tRNA synthetase family.
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 radical SAM superfamily. 7-carboxy-7-deazaguanine synthase family.
Binds 1 S-adenosyl-L-methionine per subunit.
Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7-deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds.
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.
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 glutamate 5-kinase family.
Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
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.
Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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.
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.
Component of the Sec protein translocase complex. Heterotrimer consisting of alpha (SecY), beta (SecG) and gamma (SecE) 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.
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Belongs to the V-ATPase V0D/AC39 subunit family.
Produces ATP from ADP in the presence of a proton gradient across the membrane.
Belongs to the archaeal NMN adenylyltransferase family.
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 universal ribosomal protein uS5 family.
Part of the 30S ribosomal subunit. Contacts protein S4.
The N-terminal domain interacts with the head of the 30S subunit; the C-terminal domain interacts with the body and contacts protein S4. The interaction surface between S4 and S5 is involved in control of translational fidelity.
With S4 and S12 plays an important role in translational accuracy.
Belongs to the GatB/GatE family. GatE subfamily.
Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.
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).
Belongs to the precorrin methyltransferase family.
Belongs to the RNA polymerase beta chain family.
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 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.
Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
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 pseudouridine synthase RsuA family.
Binds 1 pyruvoyl group covalently per subunit.
Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
Heterooctamer of four alpha and four beta subunits.
Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus.
Belongs to the aspartate/ornithine carbamoyltransferase superfamily. OTCase family.
Belongs to the sirtuin family. Class U subfamily.
NAD-dependent protein deacetylase which modulates the activities of several enzymes which are inactive in their acetylated form. Deacetylates the N-terminal lysine residue of Alba, the major archaeal chromatin protein and that, in turn, increases Alba's DNA binding affinity, thereby repressing transcription.
Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. May hydrolyze nucleoside diphosphates with lower efficiency.
Belongs to the RNA 3'-terminal cyclase family. Type 1 subfamily.
Belongs to the carbamoyltransferase HypF family.
A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
Belongs to the type II topoisomerase GyrB family.
Belongs to the type II topoisomerase family.
Few gyrases are as efficient as E.coli at forming negative supercoils. Not all organisms have 2 type II topoisomerases; in organisms with a single type II topoisomerase this enzyme also has to decatenate newly replicated chromosomes.
Heterotetramer, composed of two GyrA and two GyrB chains. In the heterotetramer, GyrA contains the active site tyrosine that forms a transient covalent intermediate with DNA, while GyrB binds cofactors and catalyzes ATP hydrolysis.
Belongs to the thiamine-phosphate synthase family.
Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Participates in transcription termination.
Belongs to the glutamine synthetase family.
Belongs to the archaeal Rpo12/eukaryotic RPC10 RNA polymerase subunit family.
Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
Heterooligomer of catalytic and regulatory chains.
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 probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37.
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.
Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions.
Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
Belongs to the SLC41A transporter family.
Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. NifS/IscS subfamily.
Homodimer. Forms a heterotetramer with IscU, interacts with other sulfur acceptors.
In Archaea the pyridoxal phosphate cofactor is not covalently bound to Lys but ligated by other amino acids.
Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins.
Belongs to the DNA polymerase type-B family.
Belongs to the archaeal Rpo10/eukaryotic RPB10 RNA polymerase subunit family.
Belongs to the LeuD family. LeuD type 2 subfamily.
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 eukaryotic ribosomal protein eL39 family.
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 eukaryotic ribosomal protein eL37 family.
Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Belongs to the 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 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 shikimate dehydrogenase family.
Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
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.
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.
Belongs to the eukaryotic ribosomal protein eL42 family.
Belongs to the peroxiredoxin family. Prx6 subfamily.
Homodecamer. Pentamer of dimers that assemble into a ring structure.
The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. Although the primary sequence of this enzyme is similar to those of the 1-Cys Prx6 enzymes, its catalytic properties resemble those of the typical 2-Cys Prxs and C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by thioredoxin.
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
Belongs to the cytidine and deoxycytidylate deaminase family.
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.
Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Belongs to the heat shock protein 70 family.
Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family.
Component of the protein translocase complex. Heterotrimer consisting of alpha (SecY), beta (SecG) and gamma (SecE) subunits. Can form oligomers of the heterotrimer.
Involved in protein export. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex.
Belongs to the H(+)-translocating pyrophosphatase (TC 3.A.10) family. K(+)-insensitive subfamily.
Proton pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for proton movement across the membrane. Generates a proton motive force.
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 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.
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.
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.
Belongs to the activator 1 small subunits family. RfcS subfamily.
Heteromultimer composed of small subunits (RfcS) and large subunits (RfcL).
Part of the RFC clamp loader complex which loads the PCNA sliding clamp onto DNA.
Belongs to the transaldolase family. Type 3B subfamily.
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
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 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).
Belongs to the eukaryotic ribosomal protein eL40 family.
Belongs to the EIF-2B alpha/beta/delta subunits family. MtnA subfamily.
Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Belongs to the metallo-dependent hydrolases superfamily. DHOase family. Class I DHOase subfamily.
Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Belongs to the 2H phosphoesterase superfamily. ThpR family.
Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
Belongs to the L-aspartate dehydrogenase family.
Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.
The iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia.
Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Belongs to the V-ATPase D subunit family.
Belongs to the archaeal dihydroneopterin aldolase family.
Catalyzes the conversion of 7,8-dihydroneopterin (H2Neo) to 6-hydroxymethyl-7,8-dihydropterin (6-HMD).
Belongs to the transcriptional regulatory CopG/NikR 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.
Belongs to the ribose 5-phosphate isomerase family.
Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 2 subfamily.
Involved in regulation of DNA replication.
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 eukaryotic ribosomal protein eS4 family.
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.
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 ATP-dependent DNA ligase family.
DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.
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.
Belongs to the eukaryotic ribosomal protein eL18 family.
Belongs to the topoisomerase GyrA/ParC subunit family.
Belongs to the type II topoisomerase GyrA/ParC subunit family.
Belongs to the ribulose-phosphate 3-epimerase family.
Binds 1 divalent metal cation per subunit.
Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.
Belongs to the pyrroline-5-carboxylate reductase family.
Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
Belongs to the Orn/Lys/Arg decarboxylase class-II family. LysA subfamily.
Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine.
Belongs to the thymidylate synthase ThyX family.
Binds 4 FAD per tetramer. Each FAD binding site is formed by three monomers.
Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor, and NADPH and FADH(2) as the reductant.
Belongs to the complex I 20 kDa subunit family.
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.
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 ferredoxin:CoB-CoM heterodisulfide reductase is composed of three subunits; HdrA, HdrB and HdrC.
Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ and 2 PurS subunits.
Belongs to the archaeal DNA polymerase II 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.
Belongs to the eukaryotic ribosomal protein eL31 family.
Belongs to the ribosomal protein L31e family.
Belongs to the CitM (TC 2.A.11) transporter family.
Belongs to the methyltransferase superfamily. Fibrillarin family.
Interacts with nop5. Component of box C/D small ribonucleoprotein (sRNP) particles that contain rpl7ae, FlpA and nop5, plus a guide RNA.
Involved in pre-rRNA and tRNA processing. Utilizes the methyl donor S-adenosyl-L-methionine to catalyze the site-specific 2'-hydroxyl methylation of ribose moieties in rRNA and tRNA. Site specificity is provided by a guide RNA that base pairs with the substrate. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA.
Belongs to the eukaryotic RPB4 RNA polymerase subunit family.
DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit is less well bound than the others.
Part of the RNA polymerase complex. Forms a stalk with Rpo7 that extends from the main structure.
Belongs to the SIS family. PHI subfamily.
Binds 1 thiamine pyrophosphate per subunit.
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.
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 structurs that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA.
Belongs to the acetylglutamate kinase family. ArgB subfamily.
Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Belongs to the V-ATPase E subunit family.
Belongs to the anthranilate synthase component I family.
Belongs to the helicase family. RAD3/XPD subfamily.
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 attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
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.
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 1 subfamily.
Belongs to the AAA ATPase family. CDC48 subfamily.
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 universal ribosomal protein uS2 family.
Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.
Belongs to the eukaryotic ribosomal protein eS27 family.
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.
Functions by promoting the formation of the first peptide bond.
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.
MCR is composed of three subunits: alpha, beta, and gamma. The function of proteins C and D is not known.
Belongs to the eukaryotic ribosomal protein eS1 family.
Belongs to the binding-protein-dependent transport system permease family.
Belongs to the ferredoxin--NADP reductase type 2 family.
An intermediate of this reaction is the autophosphorylated ppk in which a phosphate is covalently linked to a histidine residue through a N-P bond.
Belongs to the polyphosphate kinase 1 (PPK1) family.
Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP).
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 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.
Belongs to the DNA polymerase delta/II small subunit family.
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.
Belongs to the eukaryotic ribosomal protein eL43 family. Putative zinc-binding subfamily.
Belongs to the GHMP kinase family. Archaeal shikimate kinase subfamily.
Belongs to the eukaryotic ribosomal protein eS8 family.
Belongs to the dihydroorotate dehydrogenase family. Type 1 subfamily.
Catalyzes the conversion of dihydroorotate to orotate.
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.
Belongs to the thiolase-like superfamily. UPF0219 family.
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 class-II aminoacyl-tRNA synthetase family. ProS type 3 subfamily.
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro).
Consists of three domains: the N-terminal catalytic domain, the anticodon-binding domain and the C-terminal extension.
Belongs to the PEP-utilizing enzyme family.
Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate.
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 prefoldin alpha subunit family.
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.
Belongs to the eukaryotic-type primase small subunit family.
Catalytic subunit of DNA primase, an RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. The small subunit contains the primase catalytic core and has DNA synthesis activity on its own. Binding to the large subunit stabilizes and modulates the activity, increasing the rate of DNA synthesis while decreasing the length of the DNA fragments, 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.
RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
In the C-terminal section; belongs to the PRA-PH family.
In the N-terminal section; belongs to the PRA-CH family.
ATP-dependent agmatine transferase that catalyzes the formation of 2-agmatinylcytidine (agm2C) at the wobble position (C34) of tRNA(Ile2), converting the codon specificity from AUG to AUA.
Belongs to the helicase family. UvrD subfamily.
Belongs to the Mg-chelatase subunits D/I family.
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.
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).
Belongs to the GHMP kinase family. Mevalonate kinase subfamily.
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 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 thioesterase PaaI family.
Belongs to the CRISPR-associated endonuclease Cas1 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). Acts as a dsDNA endonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.
Homodimer, forms a heterotetramer with a Cas2 homodimer.
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.
Heterotetramer of one alpha, one beta, one delta and one gamma chain.
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.
Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.
Belongs to the eukaryotic ribosomal protein eL19 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.
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 universal ribosomal protein uL13 family.
This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.
Belongs to the V-ATPase F subunit family.
Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O.
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 arginase family. Agmatinase subfamily.
Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.
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.
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).
Belongs to the phD/YefM antitoxin family.
Belongs to the radical SAM superfamily. NifB family.
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 aconitase/IPM isomerase family.
Belongs to the type-I restriction system S methylase family.
Belongs to the eukaryotic ribosomal protein eS19 family.
May be involved in maturation of the 30S ribosomal subunit.
Belongs to the universal ribosomal protein uL29 family.
Belongs to the prefoldin subunit beta family.
Belongs to the OMP decarboxylase family. Type 1 subfamily.
Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
Belongs to the universal ribosomal protein uL1 family.
Binds directly to 23S rRNA. Probably involved in E site tRNA release.
Probably involved in E site tRNA release (By similarity). Binds directly to 23S rRNA.
Protein L1 is also a translational repressor protein, it controls the translation of its operon by binding to its mRNA.
Belongs to the gamma-glutamyl phosphate reductase family.
Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.
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.
Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3-polyprenylbenzoic acid decarboxylase UbiD. The prenyltransferase is metal-independent and links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms of FMN.
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 CRISPR-associated endoribonuclease Cas2 protein 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). Functions as a ssRNA-specific endoribonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.
Homodimer, forms a heterotetramer with a Cas1 homodimer.
Belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.
Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Belongs to the purine/pyrimidine phosphoribosyltransferase family.
Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Belongs to the GHMP kinase family. Homoserine kinase subfamily.
Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily.
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.
Belongs to the ribonucleoside diphosphate reductase class-2 family.
Catalyzes the reduction of ribonucleotides to deoxyribonucleotides. May function to provide a pool of deoxyribonucleotide precursors for DNA repair during oxygen limitation and/or for immediate growth after restoration of oxygen.
Belongs to the activator 1 small subunits family. RfcL subfamily.
Belongs to the methyl-coenzyme M reductase alpha subunit family.
MCR is a hexamer of two alpha, two beta, and two gamma chains, forming a dimer of heterotrimers.
Belongs to the phosphohexose mutase family.
Belongs to the archaeosine synthase type 1 family.
Belongs to the eukaryotic ribosomal protein eS28 family.
Belongs to the DEAD box helicase family.
Contains catalytic and regulatory chains.
Involved in allosteric regulation of aspartate carbamoyltransferase.
Belongs to the cysteine synthase/cystathionine beta-synthase family.
Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
Belongs to the archaeosine tRNA-ribosyltransferase family.
Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.
Belongs to the methylthiotransferase family. CDKAL1 subfamily.
Binds 1 or 2 [4Fe-4S] cluster. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Catalyzes the methylthiolation of N6-threonylcarbamoyladenosine (t(6)A), leading to the formation of 2-methylthio-N6-threonylcarbamoyladenosine (ms(2)t(6)A) at position 37 in tRNAs that read codons beginning with adenine.
Belongs to the Ni-containing carbon monoxide dehydrogenase family.
CODH oxidizes carbon monoxide coupled, via CooF, to the reduction of a hydrogen cation by a hydrogenase (possibly CooH).
Specifically catalyzes the AdoMet-dependent 2'-O-ribose methylation of cytidine at position 56 in tRNAs.
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. Some bacteria have evolved a zinc-coordinating structure that stabilizes the LID domain.
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.
Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal beta chain is a regulatory subunit.
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.
Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis acid cofactor.
Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
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 eukaryotic ribosomal protein eL20 family.
Part of the 50S ribosomal subunit. Binds 23S rRNA.
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.
Stabilizes TBP binding to an archaeal box-A promoter. Also responsible for recruiting RNA polymerase II to the pre-initiation complex (DNA-TBP-TFIIB).
Belongs to the radical SAM superfamily. Anaerobic sulfatase-maturating enzyme family.
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.
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.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIIB subfamily.
Mediates magnesium influx to the cytosol.
Belongs to the eukaryotic ribosomal protein eS6 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 chorismate synthase family.
Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
Belongs to the imidazoleglycerol-phosphate dehydratase family.
Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Component of the wyosine derivatives biosynthesis pathway that catalyzes the condensation of N-methylguanine with 2 carbon atoms from pyruvate to form the tricyclic 4-demethylwyosine (imG-14) on guanosine-37 of tRNA(Phe).
Belongs to the methyl-coenzyme M reductase beta subunit family.
Belongs to the histidinol dehydrogenase family.
Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration.
Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration.
Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
In the C-terminal section; belongs to the NnrD/CARKD family.
In the N-terminal section; belongs to the NnrE/AIBP family.
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.
A P subtype restriction enzyme that recognizes the double-stranded unmethylated sequence 5'-GATC-3'.
Belongs to the DpnII type II restriction endonuclease family.
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.
Binds 4 Mg(2+) or Mn(2+) ions per subunit.
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 heteropolymeric, adenine-rich transcripts and the exosome.
Catalyzes the attachment of tryptophan to tRNA(Trp).