Belongs to the ATPase alpha/beta chains family.
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 adenylyl cyclase CyaB family.
Could catalyze the biosynthesis of cyclic AMP (cAMP) from ATP.
Belongs to the peptidase A24 family. Archaeal preflagellin peptidase subfamily.
Cleaves the N-terminal leader peptide from preflagellins.
Belongs to the eukaryotic ribosomal protein eS6 family.
Catalyzes the conversion of cobalt-precorrin-8 to cobyrinate.
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.
Subunit of the protein translocation channel SecYEG. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex.
Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.
Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily.
Belongs to the class I-like SAM-binding methyltransferase superfamily. TRM5/TYW2 family.
Specifically methylates the N1 position of guanosine-37 in various tRNAs.
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 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.
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. Can also catalyze the cleavage of fructose-1,6-bisphosphate (FBP) to glyceraldehyde-3-phosphate (GAP) and dihydroxyacetone phosphate (DHAP).
Inhibited by NaBH4 in the presence of FBP.
Belongs to the universal ribosomal protein uS11 family.
Located on the platform of the 30S subunit.
Belongs to the ribose 5-phosphate isomerase family.
Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
The RCK N-terminal domain binds NAD and possibly other effectors. This is expected to cause a conformation change that regulates potassium transport.
To M.jannaschii MJ0123 and A.aeolicus AA15.
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 universal ribosomal protein uS2 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.
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.
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. Increases the resistance of DNA to thermal denaturation (in vitro).
Homodimer or heterodimer with another histone. Dimers then assemble into higher oligomers, with the DNA wrapped around the protein core (By similarity).
Belongs to the NiCoT transporter (TC 2.A.52) family.
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 eL39 family.
Belongs to the CitM (TC 2.A.11) transporter family.
Belongs to the Mrp/NBP35 ATP-binding proteins family.
Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP.
Belongs to the PTPS family. QueD subfamily.
Catalyzes the conversion of 7,8-dihydroneopterin triphosphate (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) and acetaldehyde.
The active site is at the interface between 2 subunits. The proton acceptor Cys is on one subunit, and the charge relay system is on the other subunit (By similarity).
Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.
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, a reaction that requires three enzymes in E.coli.
Belongs to the universal ribosomal protein uS15 family.
Binds 2 magnesium or manganese ions per subunit.
CarB is split into two genes in M.jannaschii (MJ1378 and MJ1381).
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.
Belongs to the organic radical-activating enzymes 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 phenylalanyl-tRNA synthetase beta subunit family. Type 2 subfamily.
Tetramer of two alpha and two beta subunits.
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 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 dethiobiotin synthetase family.
Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
Binds 1 thiamine pyrophosphate per subunit.
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. Is specific for SIH and inosine as it is unable to either hydrolyze SAH or synthesize SAH from adenosine and Hcy.
Exists both as a homotetramer and a homodimer, in a 4:1 ratio.
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.
Belongs to the eukaryotic ribosomal protein eL24 family.
Part of the 50S ribosomal subunit. Forms a cluster with proteins L3 and L14.
Could be the product of a pseudogene. Corresponds to the N-terminal of members of this family.
Belongs to the archaeal flagellin family.
Flagellin is the subunit protein which polymerizes to form the filaments of archaeal flagella.
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 SsuE family. Isf subfamily.
Redox-active protein probably involved in electron transport.
To M.jannaschii MJ1394 and A.fulgidus AF2028.
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).
Belongs to the gamma-class carbonic anhydrase family.
Probably reversibly hydrates carbon dioxide.
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 eukaryotic ribosomal protein eS31 family.
Homodimer (PubMed:10545127). Heterotetramer of two Top6A and two Top6B chains.
Mg(2+) is directly coordinated by Glu-197 and Asp-249 as well as indirectly coordinated through 2 water molecules by Asp-251 (PubMed:10545127).
Relaxes both positive and negative superturns and exhibits a strong decatenase activity.
The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity).
Belongs to the metallo-dependent hydrolases superfamily.
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.
Belongs to the methyltransferase superfamily. TrmY family.
Specifically catalyzes the N1-methylation of pseudouridine at position 54 (Psi54) in tRNAs.
Putative toxin component of a putative type VII toxin-antitoxin (TA) system. Its cognate antitoxin might be MJ1305.
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.
To M.jannaschii MJ1249.1, MJ0210.1 and MJ0785.1.
Belongs to the class-II aminoacyl-tRNA synthetase family.
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) (PubMed:15240874). Also activates L-serine, but does not detectably transfer it to tRNA(Thr) (PubMed:15240874). Edits incorrectly charged L-seryl-tRNA(Thr) via its editing domain (PubMed:15240874). Has no activity on correctly acylated L-seryl-tRNA(Ser) or L-threonyl-tRNA(Thr) (PubMed:15240874). Deacylates correctly charged glycyl-tRNA(Gly), but not glycyl-tRNA(Gly)(2'-dA76) (the terminal 2'-OH of tRNA adenine 76 has been dehydroxylated) nor the 2'-fluoro tRNA derivative, strongly suggesting the editing function is tRNA catalyzed (PubMed:26113036).
Not inhibited by 1 uM borrelidin (BN); probably does not bind BN.
The N-terminal domain (about residues 1-140) is an archaea-specific tRNA-editing domain (PubMed:15240874, PubMed:26113036) that has a highly similar structure to Dtd (D-aminoacyl-tRNA deacylase). Editing of incorrectly charged L-seryl-tRNA(Thr) by this domain is tRNA catalyzed (PubMed:26113036).
Belongs to the inorganic phosphate transporter (PiT) (TC 2.A.20) family.
Putative antitoxin component of a putative type VII toxin-antitoxin (TA) system. Its cognate toxin might be MJ0605, which it might AMPylate.
Belongs to the eukaryotic RPB7/RPC8 RNA polymerase subunit family.
DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
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 CDP-alcohol phosphatidyltransferase class-I family.
Belongs to the universal ribosomal protein uS19 family.
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
Catalyzes the reversible interconversion of serine and glycine with tetrahydromethanopterin (H4MPT) serving as the one-carbon carrier. The use of tetrahydrofolate (THF or H4PteGlu) as the pteridine substrate is 450-fold less efficient than that of H4MPT. Also exhibits a pteridine-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of L-allo-threonine and L-threo-beta-phenylserine.
Belongs to the uroporphyrinogen-III synthase family.
Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
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 glycosyltransferase 1 family. Bacterial/plant glycogen synthase subfamily.
Could lack activity as the potential ADP-glucose binding site Arg/Lys residue in position 15 is replaced by an Ser.
Synthesizes alpha-1,4-glucan chains using ADP-glucose.
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 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).
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).
Putative antitoxin component of a putative type VII toxin-antitoxin (TA) system. Its cognate toxin might be MF0142, which it might AMPylate.
Belongs to the 2H phosphoesterase superfamily. ThpR family.
Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
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 eukaryotic ribosomal protein eS8 family.
Associates with stalled 50S ribosomal subunits.
Probably part of the ribosome quality control system (RQC). May mediate the addition of alanine residues (Ala tailing) to incompletely synthesized nascent chains from stalled ribosomes, leading to their degradation.
To M.jannaschii MJ1244 and M.thermoautotrophicum MTH1110.
Belongs to the major facilitator superfamily.
Homodimer. Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ and 2 PurS subunits (By similarity).
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 Ni-containing carbon monoxide dehydrogenase family.
Binds 2 [Ni-4Fe-5S] clusters per homodimer.
Binds 3 [4Fe-4S] clusters per homodimer.
CODH oxidizes carbon monoxide coupled, via CooF, to the reduction of a hydrogen cation by a hydrogenase (possibly CooH).
Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster C is a mixed Ni-Fe-S cluster is to be the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges the two subunits of the CODH dimer.
This protein lacks the conserved Cys in position 45; it is replaced by a Tyr. It is therefore possible that the D-cluster is either altered or missing in this protein, which may not form homodimers.
Might be involved in Fe(2+) ion uptake (By similarity).
Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35) family.
Homopentamer (PubMed:23091000, PubMed:26051127). In the absence of Mg(2+), interactions between subunits are weakened, and dimers, trimers and tetramers can be observed in vitro (By similarity). Was initially proposed to be a homotetramer, based on the cross-linking studies (PubMed:15231793). This is in contradiction with current 3D-structures that clearly show it is a homopentamer (PubMed:23091000, PubMed:26051127).
Mediates influx of magnesium ions (PubMed:9573171, PubMed:10748031). Alternates between open and closed states. Activated by low cytoplasmic Mg(2+) levels. Inactive when cytoplasmic Mg(2+) levels are high (By similarity).
The central ion permeation pathway is formed by the first transmembrane domain from each of the five subunits. Mg(2+) binding strengthens interactions between subunits and leads to the formation of a symmetrical homopentamer surrounding a closed ion permeation pathway (PubMed:23091000). Low cytoplasmic Mg(2+) concentrations trigger both a conformation change within each subunit and a loosening of the interactions between subunits. This results in an open ion conduction pathway. In addition, this results in a less symmetrical shape of the whole complex (PubMed:26051127).
Belongs to the methyl-coenzyme M reductase alpha 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.
Is methylated on C5 of Arg-274 by the methyltransferase MJ0841. This post-translational methylation, despite being not essential in vivo, plays a role for the stability and structural integrity of MCR.
MCR is a hexamer of two alpha, two beta, and two gamma chains, forming a dimer of heterotrimers.
Belongs to the branched-chain polyamine synthase family.
Involved in the biosynthesis of branched-chain polyamines, which support the growth of thermophiles under high-temperature conditions. Catalyzes the sequential condensation of spermidine with the aminopropyl groups of decarboxylated S-adenosylmethionines to produce N(4)-bis(aminopropyl)spermidine via N(4)-aminopropylspermidine.
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.
Belongs to the M.jannaschii MJ0023/MJ0349/MJ1072/MJ1074/MJ1107/MJECL16 family.
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.
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.
This protein undergoes a protein self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation.
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.
Probably involved in the biogenesis of the ribosome.
May be involved in control of expression of the type II restriction enzyme MjaV and/or its methyltransferase M.MjaV.
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 glycosyltransferase 28 family.
An alpha subtype methylase that recognizes the double-stranded sequence 5'-GATC-3', methylates A-2 on both strands, and protects the DNA from cleavage by the MjaIII endonuclease.
Belongs to the N(4)/N(6)-methyltransferase family.
The subtype gamma methyltransferase (M) subunit of a type I restriction enzyme. The M and S subunits together form a methyltransferase (MTase) that methylates A-2 on the top and A-3 on the bottom strand of the sequence 5'-GAYN(5)GTAA-3'. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance MTase modifying the DNA so that both strands become methylated. After locating a non-methylated recognition site, the enzyme complex serves as a molecular motor that translocates DNA in an ATP-dependent manner until a collision occurs that triggers cleavage.
The type I restriction/modification system is composed of three polypeptides R, M and S.
Type I restriction and modification enzymes are complex, multifunctional systems which require ATP, S-adenosyl methionine and Mg(2+) as cofactors and, in addition to their endonucleolytic and methylase activities, are potent DNA-dependent ATPases.
Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase 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.
Putative toxin component of a putative type VII toxin-antitoxin (TA) system. Its cognate antitoxin might be MJ0141.
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 class-IV pyridoxal-phosphate-dependent aminotransferase family.
Belongs to the prefoldin subunit beta 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 (By similarity).
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 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 alpha-IPM synthase/homocitrate synthase family.
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 methyltransferase superfamily.
S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the methylation of the guanosine nucleotide at position 6 (m2G6) in tRNA(Cys).
Belongs to the IPP isomerase type 2 family.
Inhibited by 3,4-epoxy-3-methylbutyl diphosphate (EIPP).
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 'phage' integrase family.
Belongs to the radical SAM superfamily. KamA family.
Binds GTP first, before binding AdoCbi-P.
Guanylyltransferase that catalyzes the synthesis of adenosylcobinamide-GDP (AdoCbi-GDP) from adenosylcobinamide-phosphate (AdoCbi-P) and GTP. Is involved in adenosylcobalamin biosynthesis. Binds one GTP per dimer. Cannot use other NTPs or GDP. Does not display AdoCbi kinase activity. Is also able to catalyze the condensation of 2-phospho-L-lactate (LP) with GTP in vitro to form PPi and (2S)-lactyl-2-diphospho-5'-guanosine (LPPG), but is much less efficient than CofC, the presumed enzyme catalyzing this reaction in vivo.
Catalyzes the reversible reduction of methylene-H(4)MPT to methyl-H(4)MPT.
Belongs to the PINc/VapC protein family.
Toxic component of a type II toxin-antitoxin (TA) system. An RNase. Its cognate antitoxin is VapB4 (By similarity).
To M.jannaschii MJ1245 and M.thermoautotrophicum MTH1110.
Belongs to the ABC transporter superfamily.
Belongs to the universal ribosomal protein uS3 family.
Binds the lower part of the 30S subunit head.
Probable antitoxin component of a putative type VII toxin-antitoxin (TA) system. Neutralizes cognate toxic MJ0125 by di-AMPylation.
Probably forms a complex with cognate toxin MJ0125.
Belongs to the amino acid-polyamine-organocation (APC) superfamily.
An endodeoxyribonuclease that may play a role in defense against invading genetic elements. Uses short DNA sequences as guides to bind complementary target strands, resulting in slicing of the target DNA (PubMed:24442234, PubMed:27741323, PubMed:28319081, PubMed:28319084). Also has guide-independent activity on target DNA (PubMed:28319081). Probably a first round of guide-independent activity on an invading plasmid or virus would generate guide DNAs for subsequent, more efficient, guide-dependent degradation of invading nucleic acids (PubMed:28319081). Endonucleolytically cleaves DNA in short dsDNA (the guide DNA indicates where to cleave on the target DNA) (PubMed:24442234, PubMed:27741323, PubMed:28319081, PubMed:28319084). Efficient guide-dependent target DNA cleavage requires a minimal length of 15 bp and is maximal at 19 bp (PubMed:28319081). Prefers guide DNA with 5'-phosphorylated purines and 3'-pyrimidines; changing these bases alters the cleavage activity and patterns (PubMed:28319084). Has no activity on substrate with a mismatch at positions 10 and 11, ssDNA or RNA, nor on DNA-RNA hybrids (PubMed:24442234). Digests longer (750 bp) dsDNA as well as circular plasmid and naked genomic DNA, but not chromatin, in a guide DNA-independent manner (PubMed:28319081). Addition of endogenous histone A3 protects DNA from cleavage, while cleavage is insensitive to methylation (PubMed:28319081). When plasmid encoding active or mutated protein (Ala-541) is transformed into Sulfolobus acidocaldarius about 25-fold fewer transformants are found with active protein; reduced levels of plasmid are found in wild-type transformed cells. While S.acidocaldarius grows at a similar temperature to M.jannaschii (70 to 80 degrees Celsius) it has very different histone-like proteins, which presumably do not protect against MjAgo (PubMed:28319081). Binds ssDNA, dsDNA and DNA-RNA hybrids; binding is most efficient with dsDNA (PubMed:24442234).
Belongs to the argonaute family. Long pAgo subfamily.
Constitutively expressed (at protein level) (PubMed:28319081).
Has 4 structurally distinct domains; N-terminal, PAZ (binds the 3'-end of guide DNA), Mid (binds the phosphorylated 5'-end of guide DNA) and PIWI (binds near the 5'-end of guide DNA) arranged in a bilobal manner (PubMed:28319084). Upon binding of guide DNA the PAZ and Mid domains separate, opening a channel probably for target DNA-binding; a smaller channel also opens between the N-terminal and PIWI domains (PubMed:28319084). The N-terminal and PAZ domains undergo further major rearrangement when the binary Ago-guide DNA complex binds target DNA; the PAZ domain binds the 3'-end of guide DNA in the absence of target, upon ternary complex formation it is probably the N-terminal domain that binds that end of the dsDNA (PubMed:24442234).
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 dCTP deaminase family. Archaeal dUTPase subfamily.
This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Belongs to the universal ribosomal protein uL30 family.
Monomer. Binds to single-stranded DNA sequences.
Probably plays an essential for replication of the chromosome, DNA recombination and repair (By similarity). Binds approximately 20 nucleotides.
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.
Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetyl-glucosamine (UDP-GlcNAc). Responsible for the acetylation of GlcN-1-P to GlcNAc-1-P, and for the uridyl transfer from UTP to GlcNAc-1-P, to produce UDP-GlcNAc and pyrophosphate. Also catalyzes the reverse reaction, i.e. the cleavage of UDP-GlcNAc with pyrophosphate to form UTP and GlcNAc-1-P. To a lesser extent, is also able to use dUTP or dTTP as the nucleotide substrate, but not CTP, ATP or GTP.
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 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.
Activated by cyclic oligoadenylate (cOA) to endonucleolytically degrade linear RNA; when cOA levels decrease the RNase activity of Csx1 is abrogated.
Belongs to the CRISPR-associated Csx1 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 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.
The RNase activity is stimulated by cOA.
A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-GGNCC-3'; the cleavage site is unknown.
Belongs to the TdeIII type II restriction endonuclease family.
Belongs to the radical SAM superfamily. MCR alpha subunit C-methyltransferase family.
Binds at least 1 [4Fe-4S] cluster. This cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Radical SAM methyltransferase that is responsible for the C(5)-methylation of 'Arg-274' of the methyl-coenzyme M reductase (MCR) subunit alpha McrA. This post-translational methylation, despite being not essential in vivo, plays a role for the stability and structural integrity of MCR.
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.
This enzyme couples pyrophosphate hydrolysis to the guanine ring-opening reaction. GTP cyclohydrolase and pyrophosphate phosphoydrolase activities probably occur at independent sites.
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 ABC transporter superfamily. Phosphate importer (TC 3.A.1.7) family.
Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
The complex is composed of two ATP-binding proteins (PstB), two transmembrane proteins (PstC and PstA) and a solute-binding protein (PstS).
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.
Putative toxin component of a putative type VII toxin-antitoxin (TA) system. Its cognate antitoxin might be MJ0604.
Belongs to the monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family.
This is a Na(+)/H(+) antiporter. Can also transport lithium.
Belongs to the eukaryotic ribosomal protein eL14 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 isocitrate and isopropylmalate dehydrogenases family.
Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate, which decarboxylates to 4-methyl-2-oxopentanoate (2-oxoisocaproate). Also catalyzes the oxidative decarboxylation of 3-methylmalate to 2-oxobutyrate, and that of D-malate to pyruvate. Cannot use NADP(+) instead of NAD(+). Cannot catalyze the oxidation of L-malate, L-tartrate, D-tartrate, DL-isocitrate, or DL-lactate.
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.
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.
Possibly the antitoxin component of a type II toxin-antitoxin (TA) system. Its cognate toxin is VapC1 (Potential).
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).
Belongs to the UDP-glucose/GDP-mannose dehydrogenase family.
Catalyzes the four-electron oxidation of UDP-N-acetyl-D-mannosamine (UDP-ManNAc), reducing NAD(+) and releasing UDP-N-acetylmannosaminuronic acid (UDP-ManNAcA).
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.
Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
Composed of only a NusG N-terminal (NGN) domain and a KOW domain, similar to bacterial NusG. The NGN domain is the effector domain of the complex that mediates the interaction with RNAP and is essential for elongation activity.
Heterodimer composed of Spt4 and Spt5. Interacts with RNA polymerase (RNAP). Forms a homodimer in solution.
Forms heterodimers with RelB3 and possibly a heterotetramer RelE3-RelB3(2)-RelE3 from 2 heterodimers. The heterotetramer is probably not very stable in solution.
Toxic component of a type II toxin-antitoxin (TA) system. Has RNase activity (By similarity). Is very toxic upon expression in E.coli. Its toxic activity is probably neutralized by the cognate antitoxin RelB3.
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.
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
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.
To M.jannaschii MJ0638 and MJ1252 and M.tuberculosis Rv2003c.
Both the DNA unwinding and positive supercoiling activities require the cooperation of both domains. The cooperative action between the helicase-like and the topoisomerase domains is specific. The helicase-like domain probably does not directly unwind DNA but acts more likely by driving ATP-dependent conformational changes within the whole enzyme, functioning more like a protein motor. The 'latch' region of the N-terminal domain plays a regulatory role in the enzyme, repressing topoisomerase activity in the absence of ATP and therefore preventing the enzyme from acting as an ATP-independent relaxing enzyme; it also helps to coordinate nucleotide hydrolysis by the ATPase domain with the supercoiling activity of the topoisomerase domain (By similarity).
In the C-terminal section; belongs to the prokaryotic type I/III topoisomerase family.
In the N-terminal section; belongs to the DEAD box helicase family. DDVD subfamily.
Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. It cleaves transiently a single DNA strand and remains covalently bound to the 5' DNA end through a tyrosine residue. May be involved in rewinding the DNA strands in the regions of the chromosome that have opened up to allow transcription or replication (By similarity).
This enzyme is the only unique feature of hyperthermophilic bacteria/archaea discovered so far. It appears to be essential for adaptation to life at high temperatures.
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 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).
Binds 2 divalent metal cations per subunit. The ions could be magnesium and/or manganese.
Catalyzes the GTP-dependent successive addition of two 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), with a gamma-linkage between the two glutamates. Cannot use F420-2 as substrate to add more glutamates. Exhibits maximum activity with GTP, compared with UTP (66%) and dGTP (25%); with ATP, only F420-1 is observed as the product; CTP and TTP support no activity.
Monovalent cation. The ion could be potassium.
Probable antitoxin component of a putative type VII toxin-antitoxin (TA) system. Neutralizes cognate toxic MJ1380 by di-AMPylation.
Probably forms a complex with cognate toxin MJ1380.
Belongs to the metallo-beta-lactamase superfamily.
Catalyzes the condensation of 6-hydroxymethyl-7,8-dihydropterin pyrophosphate (DHPP) with 4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate (beta-RFA-P) to form 7,8-dihydropterin-6-methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate, a precursor in the biosynthesis of 5,6,7,8-tetrahydromethanopterin (H4MPT). To a lesser extent, is able to condense beta-RFA-P with another arylamine, 1-(4-aminophenyl)-1-deoxy-D-ribitol (APDR), to form 7,8-dihydropterin-6-methyl-1-(4-aminophenyl)-1-deoxy-D-ribitol. Dephosphorylated beta-RFA-P is not a substrate.
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.
Belongs to the potassium channel family.
The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids.
Voltage-gated potassium-selective channel opened by hyperpolarization.
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 complex I 20 kDa subunit family.
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.
An alpha subtype methylase that recognizes the double-stranded sequence 5'-GGNCC-3', methylates C-5 on both strands, and protects the DNA from cleavage by the MjaII endonuclease.
Belongs to the N(4)/N(6)-methyltransferase family. N(4) subfamily.
Belongs to the Mj S-layer protein family.
S-layer protein. The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of the cell.
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.
Belongs to the tellurite-resistance/dicarboxylate transporter (TDT) family.
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 triosephosphate isomerase family.
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
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 (By similarity).
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, and even the non-physiological cis-homo(4)-aconitate with similar efficiency. These reactions are part of the biosynthesis pathway of coenzyme B. Can also catalyze the hydration of maleate to (R)-malate, and that of cis-aconitate. Cannot catalyze the hydration of citraconate and the dehydration of (S)-homocitrate, citramalate, 2-isopropylmalate, 3-isopropylmalate, citrate or threo-DL-isocitrate.
Heterotetramer of 2 HacA and 2 HacB proteins. Cannot form a complex with LeuC.
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.
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.
Heterododecamer composed of 6 subunits alpha and 6 subunits beta.
Inhibited by oxygen when heated in air at 80 degrees Celsius. The enzyme is reactivated by addition of dithionite.
Involved in the biosynthesis of the coenzyme M (2-mercaptoethanesulfonic acid). Catalyzes the decarboxylation of sulfopyruvate to sulfoacetaldehyde.
The sequence corresponding to this entry was originally entered in Swiss-Prot as AC Q57704 in November 1997 and was deleted in July 1999 because TIGR removed the CDS for that ORF. We have recreated it because of the evidence (PubMed:10940029) that it really exists.
Belongs to the metallo-dependent hydrolases superfamily. DHOase family. Class I DHOase subfamily.
Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Belongs to the class-I aminoacyl-tRNA synthetase family.
GTP-binding protein that is not required for the biosynthesis of Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor, and not necessary for the formation of active molybdoenzymes using this form of molybdenum cofactor. May act as an adapter protein to achieve the efficient biosynthesis and utilization of MGD. Displays a weak intrinsic GTPase activity (By similarity).
Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Heterotetramer of one alpha, one beta, one delta and one gamma chain.
Plays a role in the regulation of phosphate uptake.
Antitoxin component of a type II toxin-antitoxin (TA) system. Its cognate toxin is RelE1 (Potential).
Belongs to the SecD/SecF family. SecF subfamily.
Part of the protein translocation apparatus. Forms a complex with SecD.
Belongs to the eukaryotic ribosomal protein eL21 family.
Belongs to the universal ribosomal protein uS10 family.
Involved in the binding of tRNA to the ribosomes.
Catalyzes the formation of 4-(hydroxymethyl)-2-furancarboxaldehyde phosphate (4-HFC-P) from two molecules of glyceraldehyde-3-P (GA-3-P).
Belongs to the CRISPR-associated exonuclease Cas4 family.
Binds 1 [4Fe-4S] cluster per subunit. It may be important for protein stability, since mutation of the Cys that bind the cofactor leads to a colorless, insoluble protein.
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). This protein may be a 5' to 3' ssDNA exonuclease.
Mg(2+) or Mn(2+) required for ssDNA cleavage activity. Can also utilise Cu(2+).
Belongs to the archaeal Rpo3/eukaryotic RPB3 RNA polymerase subunit family.
Part of the RNA polymerase complex (By similarity). Interacts with Rpo12. Forms an Rpo3-Rpo10-Rpo11-Rpo12 complex upon coexpression (PubMed:11058130).
Heterotetramer of the KorA, KorB, KorC and KorD subunits.
Belongs to the eukaryotic ribosomal protein eS24 family.
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).
Belongs to the V-ATPase F subunit family.
Catalyzes the reversible reduction of methenyl-H(4)MPT(+) to methylene-H(4)MPT.
A beta subtype methylase that recognizes the double-stranded sequence 5'-GTAC-3', methylates C-4 on both strands, and protects the DNA from cleavage by the MjaV endonuclease.
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 Nudix hydrolase family. NudF subfamily.
Belongs to the isopentenyl phosphate kinase family.
Catalyzes the formation of isopentenyl diphosphate (IPP), the building block of all isoprenoids. Has no activity with farnesyl phosphate.
Belongs to the CRISPR-associated Csm4 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 (By similarity). Stable Cas10/Csm1-Csm4, Csm3-Csm4 (which crystallizes as 2 heterodimers) and Cas10-Csm1-Csm3-Csm4 subcomplexes can be isolated (PubMed:25451598).
The subunit probably binds to the 5' handle of the crRNA, helping in discrimination between self- and non-self (Probable). The Csm3-Csm4 complex binds both crRNA and a non-specific RNA; Csm4 alone also binds RNA (PubMed:25451598).
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).
Binds 2 Zn(2+) or Co(2+) ions per subunit.
Probably part of an ABC transporter complex. Responsible for energy coupling to the transport system (By similarity).
Homodimer, probably forms a complex with cognate antitoxin MJ0126.
Modified by cognate antitoxin MJ0126; probably at least 2 successive AMPylation events occur on Tyr-83.
Probable toxic component of a putative type VII toxin-antitoxin (TA) system, probably an RNase. Probably neutralized by cognate antitoxin MJ0126. Neutralization may be due to AMPylation by MJ0126.
Belongs to the geranylgeranyl reductase family. ChlP subfamily.
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 prokaryotic AdoMetDC family. Type 1 subfamily.
Binds 1 pyruvoyl group covalently per subunit.
Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.
Competitively inhibited by methylglyoxal bis-guanylhydrazone. Inactivated by treatment with the imine reductant NaCNBH(3) only in the presence of substrate.
Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers.
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 group blocking the N-terminus of 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 SAICAR synthetase family.
Belongs to the GTP cyclohydrolase IV family.
Binds 1 Fe(2+) ion per subunit. Mn(2+) and Zn(2+) can be used to a lesser extent, but not at a relevant physiological concentration.
Converts GTP to 7,8-dihydro-D-neopterin 2',3'-cyclic phosphate, the first intermediate in the biosynthesis of coenzyme methanopterin. It is also able to utilize a variety of GTP analogs as substrates, including GDP, beta,gamma-methylene-GTP and GTP-[gamma-thio].
Inhibited by GTP concentrations greater than 0.3 mM and by 2-amino-5-formylamino-6-ribofuranosylamino-4(3H)-pyrimidinone 5'-phosphate (fapyGMP). Partial inhibition is observed when 2 mM GMP, dGTP, or 7-methyl-GTP was included along with 2 mM GTP.
MptA is the archetype of a new class of GTP cyclohydrolases that catalyzes a series of reactions most similar to that seen with GTPCHI but unique in that the cyclic phosphate is the product.
Binds 2 S-adenosyl-L-methionine per subunit.
Binds 2 [4Fe-4S] clusters. The clusters are coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Is responsible for the addition of methyl groups at C-7 and C-9 of the pterin ring during methanopterin (MPT) biosynthesis. Catalyzes methylation of 7,8-dihydro-6-hydroxymethylpterin, likely using methylenetetrahydromethanopterin as a methyl group donor, via a radical-based mechanism.
The most N-terminal iron-sulfur cluster is involved in C-9 methylation, while the second cluster is required for C-7 methylation of the pterin ring. Moreover, C-7 methylation occurs before C-9 methylation.
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.
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.
Binds 1 [4Fe-4S] cluster per subunit. The cluster is chelated by three Cys residues.
Belongs to the CRISPR-associated Cas10/Csm1 family.
Part of the Csm effector complex, that includes Cas10/Csm1, Csm2, Csm3, Csm4, Csm5 and mature crRNA (By similarity). Stable Cas10/Csm1-Csm4 and Cas10-Csm1-Csm3-Csm4 subcomplexes can be isolated; Cas10 and Csm3 probably do not directly interact (PubMed:25451598).
The N-terminal HD domain has ssDNase activity. The C-terminal GGDEF domain has the cOA synthesis activity.
This subunit is a single-strand-specific deoxyribonuclease (ssDNase) which digests both linear and circular ssDNA; it has both exo- and endonuclease activity.
When associated with the ternary Csm effector complex (the crRNA, Cas proteins and a cognate target ssRNA) synthesizes cyclic oligoadenylates (cOA) from ATP. cOAs are second messengers that stimulate the ssRNase activity of Csx1, inducing an antiviral state important for defense against invading nucleic acids.
ssDNase activity is stimulated in the ternary Csm effector complex; binding of cognate target RNA activates the ssDNase, as the target RNA is degraded ssDNA activity decreases.
Required for O-acetylhomoserine sulfhydrylase (OAHS)-independent homocysteine (Hcy) biosynthesis. Together with MJ0100, catalyzes the condensation of sulfide with aspartate semialdehyde to generate homocysteine. May be involved in the reduction of the disulfide formed in MJ0100.
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.
Belongs to the Holliday junction resolvase Hjc 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.
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.
A putative methylase that may protect DNA from cleavage by an unknown endonuclease.
Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.
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.
Heterodimer of a small subunit (PriS) and a large subunit (PriL).
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 class-II pyridoxal-phosphate-dependent aminotransferase family.
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.
Large-conductance mechanosensitive channel that opens in response to stretch forces in the membrane lipid bilayer. Selective for cations. Rectifies with voltage.
Essential subunit of the protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
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 class I-like SAM-binding methyltransferase superfamily. TRM61 family.
Catalyzes the S-adenosyl-L-methionine-dependent formation of N(1)-methyladenine at position 58 (m1A58) in tRNA.
Contains a large catalytic C-terminal domain that binds S-adenosyl-L-methionine and a smaller N-terminal domain that may play a role in tRNA recognition. Domains are connected by a linker region.
Homotetramer composed of a dimer of dimers.
Acts to maintain redox homeostasis; functions as a protein disulfide reductase.
Belongs to the adenylate cyclase family. DacZ subfamily.
Diadenylate cyclase that catalyzes the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP) (PubMed:25965978). c-di-AMP is a second messenger for intracellular signal transduction involved in the control of important regulatory processes such as osmoregulation (By similarity).
Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase 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.
Belongs to the eukaryotic-type primase large subunit family.
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.
Possibly the antitoxin component of a type II toxin-antitoxin (TA) system. Its cognate toxin is VapC2 (Potential).
Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.
Catalyzes the formation of acetate and ATP from acetyl-CoA by using ADP and phosphate. Can also use butyryl-CoA, but not phenylacetyl-CoA. Cannot catalyze the reverse reaction.
In the C-terminal section; belongs to the acetate CoA ligase beta subunit family.
In the N-terminal section; belongs to the acetate CoA ligase alpha subunit 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 TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. FeoB GTPase (TC 9.A.8) family.
Probable transporter of a GTP-driven Fe(2+) uptake system, might be able to transport Fe(2+) into or out of the cell (Probable).
The G protein domain (about resides 1-184) binds GDP faster and with higher affinity than GTP and releases GTP much faster than GDP. Release of bound nucleotide causes a rearrangement of GTP-binding domain G5, which may transmit information about the nucleotide-bound state from the G-domain to the transmembrane region of FeoB and effect Fe(2+) transport.
The crystallized N-terminal domain is a homodimer.
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).
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.
Inhibited by L-phenylalanine but not by L-tyrosine or L-tryptophan.
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 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.
Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.
Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
In the C-terminal section; belongs to the ThiN family.
In the N-terminal section; belongs to the ThiD family.
In the C-terminal section; belongs to the transposase 35 family.
In the N-terminal section; belongs to the transposase 2 family.
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Belongs to the argininosuccinate synthase family. Type 1 subfamily.
Binds 1 5-hydroxybenzimidazolylcobamide group.
Belongs to the universal ribosomal protein uL29 family.
Belongs to the protein kinase superfamily. RIO-type Ser/Thr kinase family.
Belongs to the eukaryotic ribosomal protein eL18 family.
Belongs to the asparagine synthetase family.
Belongs to the CRISPR-associated Csm2 family.
Part of the Csm effector complex that includes Cas10, Csm2, Csm3, Csm4 and Csm5.
This subunit may be involved in monitoring complementarity of crRNA and target RNA.
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.
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 ParA family. MinD subfamily.
Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family.
The active site is a redox-active disulfide bond.
Homodimer, probably forms a complex with antitoxin MJ1215 or MJ1217.
Modified by antitoxin MJ1215 or MJ1217; probably at least 2 successive AMPylation events occur on Tyr-83.
Probable toxic component of a putative type VII toxin-antitoxin (TA) system, probably an RNase. Probably neutralized by antitoxin MJ1215 or MJ1217. Neutralization may be due to AMPylation by antitoxin.
Belongs to the HAD-like hydrolase superfamily.
Catalyzes the dephosphorylation of D,L-glyceraldehyde 3-phosphate in vitro.
Belongs to the GTP cyclohydrolase I type 2/NIF3 family.
DNA-binding protein exhibiting the ability to bind to both single-stranded and double-stranded DNA.
Homohexamer; trimer of dimers, that forms a hollow cage-like architecture.
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.
Catalyzes the adenylation of molybdopterin as part of the biosynthesis of the molybdenum-cofactor.
Toxic component of a type II toxin-antitoxin (TA) system. Its cognate antitoxin is RelB1 (Potential).
Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate. It also acts as a dUTP diphosphatase with a lower affinity for dUTP than for dCTP.
Homotrimer (PubMed:12756253, PubMed:12909016). Two trimers assemble into a hexamer by stacking on top of each other (PubMed:12909016).
Belongs to the eukaryotic ribosomal protein eL40 family.
Belongs to the transaldolase family. Type 3B subfamily.
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Belongs to the phosphosulfolactate synthase family.
Catalyzes the addition of sulfite to phosphoenolpyruvate (PEP) to yield (2R)-phospho-3-sulfolactate (PSL).
Belongs to the polysaccharide synthase 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).
Belongs to the class-III pyridine nucleotide-disulfide oxidoreductase family.
Catalyzes the four-electron reduction of molecular oxygen to water.
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.
Heterooctamer of four A and four B subunits.
Inhibited by magnesium, when its concentration exceeded the ATP one, and by high concentration of ATP 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 archaeal Rpo6/eukaryotic RPB6 RNA polymerase subunit 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).
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) (By similarity). Also functions in trans to edit the amino acid moiety from incorrectly charged Ser-tRNA(Ala), and maybe also from Gly-tRNA(Ala).
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 (By similarity).
Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.
Belongs to the UDP-N-acetylglucosamine 2-epimerase family.
Catalyzes the reversible epimerization at C-2 of UDP-N-acetylglucosamine (UDP-GlcNAc) to produce UDP-N-acetylmannosamine (UDP-ManNAc), the activated donor of ManNAc residues.
Belongs to the transcriptional regulatory CopG/NikR family.
Toxic component of a type II toxin-antitoxin (TA) system. Its cognate antitoxin is RelB2 (Potential).
Homodimer, probably forms a complex with cognate antitoxin MJ0128.
Modified by cognate antitoxin MJ0128; probably at least 2 successive AMPylation events occur on Tyr-83.
Probable toxic component of a putative type VII toxin-antitoxin (TA) system, probably an RNase. Probably neutralized by cognate antitoxin MJ0128. Neutralization may be due to AMPylation by MJ0128.
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).
Contacts the emerging nascent chain on the ribosome.
Homodimer. Interacts with the ribosome. Binds ribosomal RNA.
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 methyltransferase superfamily. L-isoaspartyl/D-aspartyl protein methyltransferase family.
Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins (By similarity).
Belongs to the desulfoferrodoxin family.
Uses electrons from reduced NADP, by way of rubredoxin and an oxidoreductase, to catalyze the reduction of superoxide to hydrogen peroxide.
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.
Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. BioA subfamily.
Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only aminotransferase known to utilize SAM as an amino donor.
Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
Requires divalent metal ions, preferentially magnesium, for activity (Probable). Binds 2 divalent metal cations per subunit (PubMed:12904291, PubMed:15213409). Zinc and calcium, which are present in the crystals do not support the enzymatic reaction.
Probable antitoxin component of a putative type VII toxin-antitoxin (TA) system. Neutralizes cognate toxic MJ1548 by di-AMPylation.
Probably forms a complex with cognate toxin MJ1548.
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). Cas3 plus Cascade participate in CRISPR interference, the third stage of CRISPR immunity (By similarity).
In the N-terminal section; belongs to the CRISPR-associated nuclease Cas3-HD family.
In the central section; belongs to the CRISPR-associated helicase Cas3 family.
This protein is about 60 residues too short at the N-terminus compared to its close orthologs.
Belongs to the gamma-glutamylcyclotransferase family.
Putative gamma-glutamylcyclotransferase.
Belongs to the F420-dependent NADP reductase family.
Catalyzes the reduction of NADP(+) with F420H(2) via hydride transfer, and the reverse reaction, i.e. the reduction of F420 with NADPH. Probably functions in the regeneration of NADPH required in biosynthetic reactions.
Belongs to the HMG-CoA reductase family.
Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The M.jannaschii proteasome is able to cleave oligopeptides after Glu, Asp, Tyr, Phe, Trp, slightly after Arg, but not after Ala. Thus, displays caspase-like and chymotrypsin-like activities and low level of trypsin-like activity.
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 prokaryotic molybdopterin-containing oxidoreductase family.
Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit.
Belongs to the radical SAM superfamily. NifB family.
Binds 3 [4Fe-4S] clusters per monomer. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. The two others probably act as substrate.
Involved in the biosynthesis of the iron-molybdenum cofactor (FeMo-co or M-cluster) found in the dinitrogenase enzyme of the nitrogenase complex in nitrogen-fixing microorganisms. NifB catalyzes the crucial step of radical SAM-dependent carbide insertion that occurs concomitant with the insertion of a 9th sulfur and the rearrangement/coupling of two [4Fe-4S] clusters into a [8Fe-9S-C] cluster, the precursor to the M-cluster.
Belongs to the eukaryotic ribosomal protein eL15 family.
Belongs to the methyl-coenzyme M reductase gamma subunit family.
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 archaeal adenylate kinase family.
In the C-terminal section; belongs to the N(4)/N(6)-methyltransferase family.
Probably a G subtype restriction enzyme that recognizes an undetermined sequence and cleaves at an undetermined site. Probably also acts as an alpha subtype methylase, presumably on the same sequence.
Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
Heterododecamer (2C3:3R2) of six catalytic PyrB chains organized as two trimers (C3), and six regulatory PyrI chains organized as three dimers (R2).
Belongs to the ABC-4 integral membrane protein family.
Belongs to the small heat shock protein (HSP20) family.
Chaperone that confers thermal protection to other proteins.
Homooligomer of 24 subunits. Forms a spherical shape.
Belongs to the eukaryotic ribosomal protein eS19 family.
May be involved in maturation of the 30S ribosomal subunit.
To B.burgdorferi BB0465 N-terminal region.
Converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
Binds 1 Fe(2+) ion per subunit. Since MptB requires Fe2(+) for activity, the Fe(2+) ion likely has a catalytic role. The enzyme is also active under high concentrations of Mn(2+) in vitro.
Binds 1 Zn(2+) ion per subunit. The Zn(2+) ion is proposed to have a structural role.
Cyclic phosphodiesterase that hydrolyzes the cyclic phosphate of 7,8-dihydroneopterin 2',3'-cyclic phosphate (H2N-cP) and converts it to a mixture of 7,8-dihydroneopterin 2'-phosphate (H2N-2'P) and 7,8-dihydroneopterin 3'-phosphate (H2N-3'P). Is also able to utilize other phosphodiesters as substrates in vitro: hydrolysis of bis-pNPP and pNPPC produces nitrophenyl phosphate, and that of 2',3'-cAMP produces 3'-AMP. ATP, 3',5'-cAMP, GTP, 3',5'-cGMP, and 4',5'-cFMN cannot serve as substrates.
ATPase activity is inhibited by EDTA, N-ethylmaleimide (NEM) and p-chloromercuriphenyl-sulfonic acid (PCMS) in vitro.
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. In addition to ATP, is able to cleave other nucleotide triphosphates such as CTP, GTP and UTP, but hydrolysis of these other nucleotides is less effective in promoting proteolysis than ATP. Moreover, PAN by itself can function as a chaperone in vitro.
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. Alone, can form a complex composed of two stacked hexameric rings in vitro. 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 metallo-dependent hydrolases superfamily. FwdA/FmdA 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).
Forms an oligomeric complex of eight-membered rings.
Molecular chaperone; binds unfolded polypeptides in vitro, and has a weak ATPase activity.
The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.
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 succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
Catalyzes the condensation of pyruvate and acetyl-coenzyme A to form (R)-citramalate.
Belongs to the eukaryotic ribosomal protein eL34 family.
Belongs to the thiolase-like superfamily. UPF0219 family.
A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-GATC-3'; the cleavage site is unknown.
Belongs to the DpnII type II restriction endonuclease family.
Belongs to the eukaryotic ribosomal protein eS4 family.
Belongs to the AdoMet synthase 2 family.
Catalyzes the formation of S-adenosylmethionine from methionine and ATP.
A beta subtype methylase that recognizes the double-stranded sequence 5'-CTAG-3', methylates C-1 on both strands, and protects the DNA from cleavage by the MjaI endonuclease.
Belongs to the GHMP kinase family. Homoserine kinase subfamily.
Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Participates in positive as well as negative regulation of transcription. Binds to its own promoter.
Belongs to the cation diffusion facilitator (CDF) transporter (TC 2.A.4) family.
Belongs to the inositol monophosphatase superfamily. FBPase class 4 family.
IMPase activity is inhibited by Ca(2+) and Zn(2+). In contrast to mammalian I-1-P phosphatases, is not inhibited by Li(+) up to 100 mM.
Phosphatase with broad specificity; it can dephosphorylate fructose 1,6-bisphosphate, both D and L isomers of inositol-1-phosphate (I-1-P), 2'-AMP, pNPP, beta-glycerol phosphate, and alpha-D-glucose-1-phosphate. Cannot hydrolyze glucose-6-phosphate, fructose-6-phosphate, NAD(+) or 5'-AMP. May be involved in the biosynthesis of a unique osmolyte, di-myo-inositol 1,1-phosphate.
Belongs to the eukaryotic/archaeal RNase P protein component 3 family.
Consists of a catalytic RNA component and at least 4-5 protein subunits. Forms a subcomplex with Rnp2 which stimulates the catalytic RNA.
Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Belongs to the DEAD box helicase family.
Belongs to the chromate ion transporter (CHR) (TC 2.A.51) family.
Belongs to the GHMP kinase family. Mevalonate kinase subfamily.
Catalyzes the phosphorylation of (R)-mevalonate (MVA) to (R)-mevalonate 5-phosphate (MVAP). Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoid compounds such as archaeal membrane lipids.
Farnesyl- and geranyl-pyrophosphates are competitive inhibitors. Slightly inhibited by high concentration of ATP.
Belongs to the archaeal IMP cyclohydrolase family.
Catalyzes the cyclization of 5-formylamidoimidazole-4-carboxamide ribonucleotide to IMP.
Belongs to the TrkH potassium transport family.
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.
The intein interrupts the potential ATP-binding site.
Putative antitoxin component of a putative type VII toxin-antitoxin (TA) system. Its cognate toxin might be MJ1304, which it might AMPylate.
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 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.
Despite a certain similarity to SelA, PubMed:16201757 reported that this protein does not harbor SelA activity, i.e. it fails to bind to Ser-tRNA(Sec) and is not able to convert this substrate to selenocysteinyl-tRNA(Sec). It also does not convert O-phosphoseryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec).
Belongs to the M.jannaschii MJ0150/MJ0739/MJ0745/MJ1460/MJ1642 family.
Formation of the GlnK1/Amt1 complex is decreased in the presence of Mg-ATP or 2-oxoglutarate. The presence of both effectors abolishes the formation of the complex.
Homotrimer (PubMed:17203075). Interacts and forms a complex with Amt1 (PubMed:17203075).
Involved in the regulation of nitrogen metabolism (PubMed:17203075). Regulates the activity of its targets by protein-protein interaction in response to the nitrogen status of the cell (PubMed:17203075). Regulates the activity of the ammonia channel Amt1 via direct interaction (PubMed:17203075).
Belongs to the archaeal Rpo11/eukaryotic RPB11/RPC19 RNA polymerase subunit family.
Part of the RNA polymerase complex (By similarity). Forms an Rpo3-Rpo10-Rpo11-Rpo12 complex upon coexpression (PubMed:11058130).
Belongs to the aconitase/IPM isomerase family. LeuC type 2 subfamily.
Enzyme with broad specificity that catalyzes reversible hydroxyacid isomerizations via dehydration/hydration reactions. Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate, a step involved in leucine biosynthesis. Catalyzes the isomerization between 2-methylmalate and 3-methylmalate, via the formation of 2-methylmaleate (citraconate), a step involved in isoleucine biosynthesis. Also displays malease activity, i.e. catalyzes the hydration of maleate to form (R)-malate.
Heterotetramer of 2 LeuC and 2 LeuD. Cannot form a complex with HacB.
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.
This is probably a Na(+)/H(+) antiporter.
Functions by promoting the formation of the first peptide bond.
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.
Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.
Mycophenolic acid (MPA) is a non-competitive inhibitor that prevents formation of the closed enzyme conformation by binding to the same site as the amobile flap. In contrast, mizoribine monophosphate (MZP) is a competitive inhibitor that induces the closed conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of bacterial IMPDH.
Contains large globular domains required for ATP hydrolysis at each terminus and a third globular domain forming a flexible SMC hinge near the middle of the molecule. These domains are separated by coiled-coil structures.
Required for chromosome condensation and partitioning.
Catalyzes the transamination reaction between 4-(hydroxymethyl)-2-furancarboxaldehyde phosphate (4-HFC-P) and alanine to produce pyruvate and 5-(aminomethyl)-3-furanmethanol phosphate (F1-P), the precursor for the furan moiety in methanofuran.
Toxic component of a type II toxin-antitoxin (TA) system. Its cognate antitoxin is RelB4 (Potential).
Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. BioF subfamily.
Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.
Belongs to the NAD(P)-dependent epimerase/dehydratase family.
Involved in the metabolism of galactose. Catalyzes the conversion of UDP-galactose (UDP-Gal) to UDP-glucose (UDP-Glc) through a mechanism involving the transient reduction of NAD (By similarity).
Anion-transporting ATPase. Catalyzes the extrusion of arsenite (By similarity).
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.
Belongs to the GHMP kinase family. Archaeal shikimate kinase subfamily.
DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.
To M.jannaschii MJ1213 and A.aeolicus AA15.
Belongs to the binding-protein-dependent transport system permease family. LivHM subfamily.
Part of the binding-protein-dependent transport system for branched-chain amino acids. Probably responsible for the translocation of the substrates across the membrane (By similarity).
Belongs to the prefoldin subunit alpha family.
Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
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-97 inactivates the nitrogenase reductase and regulates nitrogenase activity.
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.
To M.jannaschii MJ0871, MJ1556 and MJ1589.
Belongs to the biotin--protein ligase family.
Homodimer (PubMed:10741836). Dimers then assemble into higher oligomers, with the DNA wrapped around the protein core (By similarity).
Catalyzes the formation of 5-(aminomethyl)-3-furanmethanol diphosphate (F1-PP) from 5-(aminomethyl)-3-furanmethanol phosphate (F1-P) and ATP (PubMed:26100040). In vitro, can also act as an adenylate kinase that catalyzes the transfer of a phosphoryl group from ATP to AMP, generating two molecules of ADP (PubMed:22002406).
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 precorrin methyltransferase family.
Catalyzes the methylation of C-5 in cobalt-precorrin-7 to form cobalt-precorrin-8.
Belongs to the CbiX family. CbiXS subfamily.
Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis. 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 insertion of Ni(2+) into sirohydrochlorin to yield Ni-sirohydrochlorin.
Belongs to the glutamyl-tRNA reductase family.
Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
During catalysis, the active site Cys acts as a nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate with the formation of a thioester intermediate between enzyme and glutamate, and the concomitant release of tRNA(Glu). The thioester intermediate is finally reduced by direct hydride transfer from NADPH, to form the product GSA.
Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.
A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-GTAC-3'; the cleavage site is unknown.
Catalyzes the reversible oxidation of (S)-malate and (S)-sulfolactate to oxaloacetate and sulfopyruvate, respectively. Can use both NADH and NADPH, although activity is higher with NADPH. Oxidation of (S)-sulfolactate is observed only in the presence of NADP(+). Can also oxidize tartrate. Cannot reduce pyruvate, nor alpha-ketoglutarate.
Belongs to the metallo-dependent hydrolases superfamily. TatD-type hydrolase family.
Binds 2 divalent metal cations per subunit.
Probable methyltransferase that uses S-adenosylmethionine as the methyl donor. Binds neither NAD nor NADP in vitro.
Binds 2 [Ni-4Fe-4S] clusters per heterotetramer.
Binds 7 [4Fe-4S] clusters per heterotetramer.
Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges the two subunits of the CODH dimer. Contains two additional 4Fe-4S clusters, dubbed E and F, that probably transport electrons from ferredoxin to the B cluster.
Heterotetramer of two alpha and two epsilon subunits. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).
Part of the ACDS complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase.
Belongs to the CRISPR-associated protein Cas7/Cst2/DevR family. Subtype I-a/Apern subfamily.
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) (By similarity).
Probable antitoxin component of a putative type VII toxin-antitoxin (TA) system. Neutralizes cognate toxic MJ1216 by di-AMPylation.
Probably forms a complex with cognate toxin MJ1216.
Belongs to the acetyltransferase family.
Belongs to the AAA ATPase family. CDC48 subfamily.
Belongs to the homoserine dehydrogenase family.
Belongs to the peptidase M24A family. Methionine aminopeptidase archaeal type 2 subfamily.
Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.
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 archaeal Rpo5/eukaryotic RPB5 RNA polymerase subunit family.
Involved in the catabolism of quinolinic acid (QA).
Antitoxin component of a type II toxin-antitoxin (TA) system. Its cognate toxin is RelE2 (Potential).
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 TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. NOG subfamily.
Belongs to the SecD/SecF family. SecD subfamily.
Part of the protein translocation apparatus. Forms a complex with SecF.
D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
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 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 CRISPR-associated helicase Cas3 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). Cas3 plus Cascade participate in CRISPR interference, the third stage of CRISPR immunity. Probably unwinds dsDNA templates, thus providing substrates for CRISPR-associated endonuclease Cas3-HD. Unwinding is strongly increased in the presence of ATP, implying the helicase uses ATP to unwind substrate.
Proteins of this family have an N-terminal nuclease domain and a C-terminal helicase/ATPase domain. In some CRISPR/Cas systems the domains are swapped, in others they are encoded separately.
Belongs to the thymidylate synthase family. Archaeal-type ThyA subfamily.
May catalyze the biosynthesis of dTMP using an unknown cosubstrate.
Belongs to the archaeal Rpo10/eukaryotic RPB10 RNA polymerase subunit family.
Belongs to the eukaryotic ribosomal protein eL43 family. Putative zinc-binding subfamily.
Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase. The precise role of the epsilon subunit is unclear; it may have a stabilizing role within the alpha(2)epsilon(2) component and/or be involved in electron transfer to FAD during a potential FAD-mediated CO oxidation.
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 Mg-chelatase subunit H family.
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.
In the C-terminal section; belongs to the PAPS reductase family.
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 (PubMed:24375099). Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions (PubMed:25917907). 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 (PubMed:24375099).
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 (PubMed:25917907). 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 (PubMed:24375099).
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.
Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
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. Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ and 2 PurS subunits.
Methylated at an undetermined residue between Ser-2 and Asp-26.
Belongs to the eukaryotic ribosomal protein eL42 family.
Belongs to the helicase family. DinG subfamily.
According to PubMed:12130658, ProRS is unable to edit the misacylated Cys-tRNA(Pro) and Ala-tRNA(Pro), whereas according to PubMed:11408489, it hydrolyzes Ala-AMP and Ala-tRNA(Pro) by 'pretransfer' and 'posttransfer' editing activities, respectively.
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). Can inadvertently accommodate and process non-cognate amino acids such as cysteine and alanine.
Consists of three domains: the N-terminal catalytic domain, the anticodon-binding domain and the C-terminal extension.
Homodimer. The dimer is functionally asymmetric: only one of the two active sites at a time is able to form prolyl-adenylate, and only one tRNA molecule binds per dimer.
Inhibited by high concentrations of prolinamide.
Was originally (PubMed:10642548, PubMed:10869184 and PubMed:11141055) thought to have both prolyl- and cysteinyl-tRNA synthetase activities (ProCysRS). However, recent biochemical and structural studies show that ProRS misaminoacylates tRNA(Pro) with cysteine but is unable to aminoacylate tRNA(Cys). These conflicting results may be due to the fact that much of the previous work was done with unfractionated tRNA.
Belongs to the RimK family. MptN subfamily.
Catalyzes the ATP or GTP-dependent addition of one L-glutamate molecule to tetrahydromethanopterin, producing tetrahydrosarcinapterin.
Belongs to the aldehyde dehydrogenase family.
Involved in F420 biosynthesis through the oxidation of lactaldehyde to lactate. The substrate preference order is propionaldehyde > DL-lactaldehyde, DL-glyceraldehyde > crotonaldehyde > glycolaldehyde > acetaldehyde, acrolein > formaldehyde. No activity was observed towards methylglyoxal or glyceraldehyde-3-phosphate. Has a preference for NAD over NADP.
Could be the product of a pseudogene. Corresponds to the C-terminal of members of this family.
Catalyzes the attachment of glycine to tRNA(Gly).
Belongs to the radical SAM superfamily. CofH family.
Catalyzes the radical-mediated synthesis of 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine.
Consists of two subunits, CofG and CofH.
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.
Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.
Catalyzes the reduction of sulfite to sulfide using reduced F420 as the electron source. Involved in sulfite detoxification and assimilation. Cannot use NADH or NADPH.
Contains an N-terminal H(2)F420 dehydrogenase domain and a C-terminal dissimilatory-type siroheme sulfite reductase domain.
Expression in Methanococcus maripaludis, a sulfite-sensitive methanogen, leads to sulfite detoxification and use of sulfite as a sole sulfur source by M. maripaludis.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily.
Most probably acts as a phosphatase in the cytosol.
Belongs to the binding-protein-dependent transport system permease family. FecCD subfamily.
Probably part of a binding-protein-dependent transport system. Probably responsible for the translocation of the substrate across the membrane.
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 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 archaeal Rpo12/eukaryotic RPC10 RNA polymerase subunit family.
Part of the RNA polymerase complex (By similarity). Interacts with Rpo3. Forms an Rpo3-Rpo10-Rpo11-Rpo12 complex upon coexpression (PubMed:11058130).
Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
Belongs to the DEAD box helicase family. DEAH subfamily.
To M.jannaschii MJ0977 C-terminal region.
Belongs to the eukaryotic ribosomal protein eS17 family.
Catalyzes the isomerization of glucose-6-P to fructose-6-P.
Competively inhibited by 6-phosphogluconate and erythrose 4-phosphate.
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) (By similarity).
Belongs to the amidase family. GatA subfamily.
Hydrolyzes both enantiomers of 2-phosphosulfolactate. Able to hydrolyze both enantiomers of 2-hydroxycarboxylic acids with pseudosymmetric centers of inversion. Specifically hydrolyzes (S)-phospholactate and (S)-phosphoglycerate.
Belongs to the LDH2/MDH2 oxidoreductase family.
Catalyzes the reduction of sulfopyruvate to (R)-sulfolactate much more efficiently than the reverse reaction. Also catalyzes the reduction of oxaloacetate, alpha-ketoglutarate, and to a much lower extent, KHTCA, but not pyruvate. Involved in the biosynthesis of both coenzyme M (with (R)-sulfolactate) and methanopterin (with alpha-ketoglutarate).
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 NAD(P)-dependent epimerase/dehydratase family. dTDP-glucose dehydratase subfamily.
Belongs to the autoinducer-2 exporter (AI-2E) (TC 2.A.86) family.
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 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.
Belongs to the LysR transcriptional regulatory family.
Belongs to the spermidine/spermine synthase family.
Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.
Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily.
Belongs to the metallo-beta-lactamase superfamily. RNA-metabolizing metallo-beta-lactamase-like family.
Potassium channel protein. Seems to conduct potassium at low membrane potentials.
Belongs to the universal ribosomal protein uL15 family.
Belongs to the eukaryotic ribosomal protein eS1 family.
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 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.
Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. May hydrolyze nucleoside diphosphates with lower efficiency (By similarity).
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.
Catalyzes only the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor.
Heterotetramer of two alpha and two beta chains.
Some bacteria possess a monofunctional ArgJ, i.e. capable of catalyzing only the fifth step of the arginine biosynthetic pathway.
Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit family.
The F420-non-reducing hydrogenase vhu is composed of four subunits; VhuA, VhuD, VhuG and VhuU.
The large subunit of Vhu is split into VhuA and VhuU. Each contributes two ligands to the [NiFeSe] center.
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.
In the N-terminal section; belongs to the prephenate/arogenate dehydrogenase family.
MCR is composed of three subunits: alpha, beta, and gamma. The function of proteins C and D is not known (By similarity).
Belongs to the GatB/GatE family. GatE subfamily.
Probable antitoxin component of a putative type VII toxin-antitoxin (TA) system. Neutralizes cognate toxic MJ0127 by di-AMPylation.
Probably forms a complex with cognate toxin MJ0127.
A site-2 regulated intramembrane protease (S2P) that cleaves type-2 transmembrane proteins within their membrane-spanning domains; its endogenous substrate is unknown. Regulated intramembrane proteolysis (RIP) occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. A membrane-spanning regulatory substrate protein is first cut extracytoplasmically (site-1 protease, S1P), then within the membrane itself (site-2 protease, S2P, this enzyme), while cytoplasmic proteases finish degrading the regulatory protein, liberating the effector protein. Possible signals, S1P and substrates are unknown in this organism.
Belongs to the binding-protein-dependent transport system permease family. CysTW subfamily.
Part of the binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
Belongs to the RimK family. CofF subfamily.
Catalyzes the ATP-dependent addition of one alpha-linked L-glutamate molecule to coenzyme gamma-F420-2, producing alpha-F420-3, the major form of coenzyme F420 found in M.jannaschii. Thus, caps the gamma-polyglutamate tail of coenzyme F420 with a terminal alpha-linked glutamate. Prefers ATP to other purine nucleotide triphosphates; GTP gives about 25% of the activity observed with ATP. Cannot catalyze the addition of the following amino acids or analogs: D-glutamate, beta-glutamate, L-aspartate, L-glutamine, L-alpha-aminoadipate, or D,L-2-amino-4-phosphono-butyrate.
Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase.
Component of the KEOPS complex that consists of Kae1, Bud32, Cgi121 and Pcc1; the whole complex dimerizes.
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, a step in the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Cgi121 stimulates Bud32 kinase activity via an activation of Bud32 autophosphorylation.
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 (PubMed:15558053). Polymerizes to form a dynamic ring structure in a strictly GTP-dependent manner. Interacts directly with several other division proteins (By similarity).
Belongs to the universal ribosomal protein uL16 family.
Belongs to the eukaryotic/archaeal RNase P protein component 1 family.
Consists of a catalytic RNA component and at least 4 protein subunits. Forms a subcomplex with Rnp4 which stimulates the catalytic RNA.
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 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.
Belongs to the HAD-like hydrolase superfamily. SerB family.
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 (Probable).
Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ and 2 PurS subunits.
Belongs to the ribulose-phosphate 3-epimerase family.
Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.
Belongs to the activator 1 small subunits family. RfcL subfamily.
Oxygen-binding protein. May be involved in a storage mechanism or for delivery to oxygen-requiring enzymes. The oxygen-binding site contains two iron atoms.
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate.
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.
Possibly the antitoxin component of a type II toxin-antitoxin (TA) system.
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).
The intein interrupts the GTP-binding site.
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) (By similarity).
A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-CCGG-3'; the cleavage site is unknown.
Belongs to the BsaWI type II restriction endonuclease family.
Catalyzes the reversible phosphorylation of UMP to UDP.
To M.jannaschii MJ0880, MJ1556 and MJ1589.
Belongs to the exosortase/archaeosortase family. Archaeosortase D subfamily.
Transpeptidase that recognizes and modifies its substrate by proteolytic cleavage of a sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the archaeosortase and its substrate, which is then transferred and covalently attached to the cell membrane.
S-adenosyl-L-methionine-dependent methyltransferase that acts as a component of the wyosine derivatives biosynthesis pathway. Probably methylates N-4 position of wybutosine-86 to produce wybutosine-72.
Belongs to the metallophosphoesterase superfamily. YfcE family.
Binds 2 divalent metal ions per subunit. Most effective are nickel and manganese.
Shows phosphodiesterase activity, hydrolyzing phosphodiesters bonds in the artificial chromogenic substrates bis-p-nitrophenyl phosphate (bis-pNPP), and less efficiently thymidine 5'-monophosphate p-nitrophenyl ester (pNP-TMP) and p-nitrophenylphosphorylcholine (pNPPC). No catalytic activity was found toward cAMP or cGMP, nucleotides or phospholipase substrates such as phosphatidylcholine. The physiological substrate is unknown.
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 eukaryotic ribosomal protein eL37 family.
Belongs to the diaminopimelate epimerase family.
Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine.
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).
Belongs to the phosphohexose mutase family.
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.
Single-stranded-DNA-specific exonuclease.
Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19) family.
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).
Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
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.
Participates in transcription termination.
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 thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.
Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.
Because the Archaea possessing a type III RuBisCO are all anaerobic, it is most likely that only the carboxylase activity of RuBisCO, and not the competitive oxygenase activity (by which RuBP reacts with O(2) to form one molecule of 3-phosphoglycerate and one molecule of 2-phosphoglycolate), is biologically relevant in these strains.
Belongs to the RuBisCO large chain family. Type III subfamily.
Catalyzes the addition of molecular CO(2) and H(2)O to ribulose 1,5-bisphosphate (RuBP), generating two molecules of 3-phosphoglycerate (3-PGA). Functions in an archaeal AMP degradation pathway, together with AMP phosphorylase and R15P isomerase.
Homodimer. In contrast to form I RuBisCO, the form III RuBisCO is composed solely of large subunits.
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 methyltransferase superfamily. RlmI family.
Heterotetramer of 2 HacA and 2 HacB proteins.
The heterotetramer that can be formed in vitro between HacA and LeuD cannot catalyze citraconate hydration or the dehydration of 2-isopropylmalate or 3-isopropylmalate.
Belongs to the methyl-coenzyme M reductase beta subunit family.
Ferredoxins are iron-sulfur proteins that transfer electrons probably in the CO-dehydrogenase complex.
Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate.
Homotrimer (By similarity). Interacts and forms a complex with Amt2 (By similarity).
Involved in the regulation of nitrogen metabolism (By similarity). Regulates the activity of its targets by protein-protein interaction in response to the nitrogen status of the cell (By similarity). Regulates the activity of the ammonia channel Amt2 via direct interaction (By similarity).
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.
Specifically catalyzes the AdoMet-dependent 2'-O-ribose methylation of cytidine at position 56 in tRNAs.
Belongs to the NifD/NifK/NifE/NifN 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 archaeal NMN adenylyltransferase family.
Catalyzes the methylation of C-11 in cobalt-precorrin-4 to form cobalt-precorrin-5A.
Belongs to the eukaryotic ribosomal protein eS28 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 tRNA methyltransferase O family.
Belongs to the universal ribosomal protein uS14 family. Zinc-binding uS14 subfamily.
Binds 16S rRNA, required for the assembly of 30S particles.
Belongs to the radical SAM superfamily. CofG family.
Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) from 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil.
Belongs to the arginase family. Agmatinase subfamily.
Binds 2 Fe(2+) ions per subunit. Can also use Mn(2+), with lower efficiency.
Catalyzes the formation of putrescine from agmatine.
Inhibited by putrescine and by the substrate analog arginine. Inactive when the purified enzyme is incubated with dithiothreitol followed by excess iodoacetic acid or N-ethylmaleimide.
Catalyzes the reversible interconversion of 5-formyl-H(4)MPT to methenyl-H(4)MPT(+).
Binds 1 Mg(2+) ion per subunit (By similarity). Magnesium ions are required for optimal activity, with Mn(2+), Zn(2+) and Ni(2+) supporting <50% of the maximum rate (PubMed:11452035).
Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides xanthosine triphosphate (XTP), deoxyinosine triphosphate (dITP) and ITP (PubMed:10404228, PubMed:11452035). Probably functions 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 (PubMed:11452035). Shows very low activity on GTP or dGTP, both of which are hydrolyzed more than 100-fold less efficiently than XTP, and has nearly no activity toward the canonical nucleotides ATP, CTP, and TTP, and toward 6-N-hydroxylaminopurine deoxynucleoside triphosphate (dHAPTP) (PubMed:10404228, PubMed:11452035). Displays neither endonuclease nor 3'-exonuclease activities (PubMed:11452035).
Belongs to the universal ribosomal protein uS9 family.
Activity provided by the Kae1 region seems to be regulated via phosphorylation by the protein kinase Bud32, which is itself activated by Cgi121.
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 (By similarity). The Bud32 domain probably displays kinase activity that regulates Kae1 function. In vitro, exhibits low ATPase activity, but does not bind DNA and does not have endonuclease activity.
Belongs to the glycogen phosphorylase family.
Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 2 subfamily.
Required for formate dehydrogenase (FDH) activity.
Catalyzes the two successive C-2 and C-7 methylation reactions involved in the conversion of uroporphyrinogen III to precorrin-2 via the intermediate formation of precorrin-1. It is a step in the biosynthesis of both cobalamin (vitamin B12) and coenzyme F430.
Belongs to the glycosyltransferase 4 family.
Belongs to the SIMIBI class G3E GTPase family. HypB/HupM subfamily.
Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase. Exhibits a low intrinsic GTPase activity, which is essential for nickel insertion.
Catalyzes the cis-trans isomerization of peptidyl prolyl bonds and accelerates protein folding (By similarity). Also exhibits chaperone-like activity (PubMed:21262232).
Contains an N-terminal PPIase domain, an IF (Insert in the Flap) domain and a C-terminal domain (CTD). The CTD mediates dimerization. Chaperone activity requires both the IF domain and the CTD.
Alkylation of both Cys-126 and Cys-143 results in complete loss of enzymatic activity.
Belongs to the archaeal FAD synthase family.
Catalyzes the transfer of the AMP portion of ATP to flavin mononucleotide (FMN) to produce flavin adenine dinucleotide (FAD) coenzyme. To a lesser extent, is also able to utilize other nucleotides such as CTP and GTP as substrates, producing the modified coenzymes, flavin cytosine dinucleotide (FCD) and flavin guanine dinucleotide (FGD), respectively. Does not catalyze the reverse reaction to produce FMN and ATP from FAD and PPi. Does not function as a glycerol-3-phosphate cytidylyltransferase, as previously annotated in the complete genome.
Divalent metal cations. The best activity is observed with Co(2+), where the activity is 4 and 2.5 times greater than that with Mg(2+) and Mn(2+), respectively.
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.
Belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family.
Involved in the archaeal biosynthesis of heme. Catalyzes the oxiation of precorrin-2 into sirohydroclorin (By similarity).
Belongs to the cytidylate kinase family. Type 2 subfamily.
The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Belongs to the CRISPR-associated protein Cas6/Cse3/CasE 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). This protein processes pre-crRNA into individual crRNA units.
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.
To M.jannaschii MJ0706 and Synechocystis PCC 6803 slr1478.
Belongs to the eukaryotic/archaeal RNase P protein component 4 family.
Consists of a catalytic RNA component and at least 4 protein subunits. Forms a subcomplex with Rnp1 which stimulates the catalytic RNA.
Belongs to the eukaryotic ribosomal protein eL32 family.
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 aldolase class II family. AraD/FucA subfamily.
Involved in the biosynthesis of the coenzyme F420 which requires phospholactate produced via the aldol cleavage of L-fuculose 1-phosphate and the NAD(+)-dependent oxidation of (S)-lactaldehyde (PubMed:16585745). Catalyzes the reversible cleavage of L-fuculose 1-phosphate (Fuc1P) to yield dihydroxyacetone phosphate (DHAP) and S-lactaldehyde (Ref.2, PubMed:16585745, PubMed:17927915, PubMed:22418259). FucA possesses a high specificity for the dihydroxyacetone phosphate (DHAP), but accepts a great variety of different aldehydes such as DL-glyceraldehyde and glycolaldehyde (PubMed:16585745, PubMed:17927915).
Trimethyl phosphonoacetate and DL-threose are competitive inhibitors with respect to dihydroxyacetone phosphate, and uncompetitive inhibitors with respect to DL-glyceraldehyde.
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.
Belongs to the beta-RFA-P synthase family.
Catalyzes the condensation of 4-hydroxybenzoate (HB) with 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to produce beta-ribofuranosylphenol 5'-phosphate (beta-RFH-P) (PubMed:21634403). Also catalyzes the condensation of 4-aminobenzoate (pABA) with PRPP to produce beta-ribofuranosylaminobenzene 5'-phosphate (beta-RFA-P) (PubMed:15262968, PubMed:21634403). Only 4-hydroxybenzoate is known to be biosynthesized by methanogenic archaea, but 4-aminobenzoate can be used as substrate by growing methanogens when it is present in the growth medium (PubMed:21634403).
Lacks any chromogenic cofactor, and the presence of pyridoxal phosphate and the mechanistically related pyruvoyl cofactors has been strictly excluded.
Belongs to the ABC transporter superfamily. Sulfate/tungstate importer (TC 3.A.1.6) family.
Part of the ABC transporter complex WtpABC involved in molybdate/tungstate import. Responsible for energy coupling to the transport system.
The complex is composed of two ATP-binding proteins (WtpC), two transmembrane proteins (WtpB) and a solute-binding protein (WtpA).
Belongs to the glycosyl hydrolase 57 family.
Belongs to the CRISPR-associated Csm3 family.
Part of the Csm effector complex that includes Cas10, Csm2, Csm3, Csm4 and Csm5 (By similarity). Stable Csm3-Csm4 (which crystallizes as 2 heterodimers) and Cas10-Csm1-Csm3-Csm4 subcomplexes can be isolated; Cas10 and Csm3 probably do not directly interact (PubMed:25451598).
This subunit has the target ssRNA endonuclease activity; it cleaves multiple sites in the target RNA at 6 nucleotide intervals (By similarity). The Csm3-Csm4 complex binds both crRNA and a non-specific RNA; Csm3 alone was not seen to bind RNA (PubMed:25451598).
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) (Potential).
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 4-toluene sulfonate uptake permease (TSUP) (TC 2.A.102) family.
Belongs to the threonine synthase family.
Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine.
Belongs to the phosphatidylserine decarboxylase family. PSD-A subfamily.
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 glutamate synthase 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 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).
Toxic component of a type II toxin-antitoxin (TA) system. An RNase.
Heterotetramer of 2 PyrK and 2 PyrD type B subunits.
Responsible for channeling the electrons from the oxidation of dihydroorotate from the FMN redox center in the PyrD type B subunit to the ultimate electron acceptor NAD(+).
Catalyzes the transfer of the 2-phospholactate moiety from (2S)-lactyl-2-diphospho-5'-guanosine to 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) with the formation of oxidized coenzyme F420-0 and GMP.
Belongs to the GHMP kinase family. PoK subfamily.
Phosphorylates (R)-pantoate to form (R)-4-phosphopantoate in the CoA biosynthesis pathway.
Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.
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.
Ile-16 is present instead of the conserved His which is expected to be an active site residue. Substrate-binding sites are also not conserved. Thus, this enzyme may not display fae activity.
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.
Belongs to the archaeal riboflavin kinase family.
Binds 1 magnesium ion per subunit. This ion is coordinated by a threonine and an asparagine, and by the alpha- and beta-phosphates of CDP.
Catalyzes the CTP-dependent phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN). Can also utilize UTP as the phosphate donor, although less efficiently, and it is unclear if ATP and GTP can also serve as substrates (PubMed:18245297) or not (PubMed:18073108).
Belongs to the universal ribosomal protein uL1 family.
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 V-ATPase proteolipid subunit family.
Belongs to the exosortase/archaeosortase family. Archaeosortase E subfamily.
Belongs to the L-seryl-tRNA(Sec) kinase family.
Specifically phosphorylates seryl-tRNA(Sec) to O-phosphoseryl-tRNA(Sec), an activated intermediate for selenocysteine biosynthesis.
Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase NEP1 family.
Methyltransferase involved in ribosomal biogenesis. Specifically catalyzes the N1-methylation of pseudouridine at position 914 (Psi914) in 16S rRNA. Is not able to methylate uridine at this position.
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 eukaryotic/archaeal PrmC-related family.
Putative protein methyltransferase using S-adenosyl-L-methionine as the methyl donor. May methylate a Gln residue in target proteins (By similarity).
Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively.
In the presence of PdxT, forms a dodecamer of heterodimers.
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).