The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.
Belongs to the transcriptional regulatory CopG/NikR family.
Belongs to the DNA polymerase type-B family.
Belongs to the binding-protein-dependent transport system permease family.
An intermediate of this reaction is the autophosphorylated ppk in which a phosphate is covalently linked to a histidine residue through a N-P bond.
Belongs to the polyphosphate kinase 1 (PPK1) family.
Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP).
Belongs to the methylglyoxal synthase family.
Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate.
Belongs to the V-ATPase E subunit family.
Produces ATP from ADP in the presence of a proton gradient across the membrane.
Expression is highly up-regulated in presence of fructose.
General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr then transfers it to the PTS EIIA domain (By similarity). Is involved in fructose transport.
PTS-type transport systems are very rare in archaea.
Phosphorylation on Ser-47 inhibits the phosphoryl transfer from enzyme I to HPr.
Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.
Belongs to the thioesterase PaaI family.
Belongs to the purine/pyrimidine phosphoribosyltransferase family. Archaeal HPRT subfamily.
May catalyze a purine salvage reaction, the substrate is unknown.
Monomer. Interaction with RNA polymerase subunits RpoF and RpoE is necessary for Tfe stimulatory transcription activity. Able to interact with Tbp and RNA polymerase in the absence of DNA promoter. Interacts both with the preinitiation and elongation complexes.
The winged helix domain is involved in binding to DNA in the preinitiation complex.
Transcription factor that plays a role in the activation of archaeal genes transcribed by RNA polymerase. Facilitates transcription initiation by enhancing TATA-box recognition by TATA-box-binding protein (Tbp), and transcription factor B (Tfb) and RNA polymerase recruitment. Not absolutely required for transcription in vitro, but particularly important in cases where Tbp or Tfb function is not optimal. It dynamically alters the nucleic acid-binding properties of RNA polymerases by stabilizing the initiation complex and destabilizing elongation complexes. Seems to translocate with the RNA polymerase following initiation and acts by binding to the non template strand of the transcription bubble in elongation complexes.
Cells having transposon insertions in this gene are hypermotile.
May be part of a signal-dependent gene regulation cascade that is relevant to swimming motility. May be involved in the transcription regulation of target genes.
Belongs to the ammonia transporter channel (TC 1.A.11.2) family.
Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Lacks conserved residue(s) required for the propagation of feature annotation.
Belongs to the PEP-utilizing enzyme family.
General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr).
The N-terminal domain contains the HPr binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site.
The reaction takes place in three steps, mediated by a phosphocarrier histidine residue located on the surface of the central domain. The two first partial reactions are catalyzed at an active site located on the N-terminal domain, and the third partial reaction is catalyzed at an active site located on the C-terminal domain. For catalytic turnover, the central domain swivels from the concave surface of the N-terminal domain to that of the C-terminal domain.
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Belongs to the GatB/GatE family. GatB subfamily.
Belongs to the exosortase/archaeosortase family. Archaeosortase A subfamily.
Deletion of the gene results in poor growth, especially under low-salt conditions, alterations in cell shape and in the S-layer, impaired motility and impaired conjugation.
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 (Probable). This sortase recognizes a tripartite structure consisting of a conserved Pro-Gly-Phe (PGF) motif, followed by a transmembrane alpha helix domain and a cluster of basic residues, usually at the C-terminus of target proteins (Probable). Confirmed substrates include the cell surface S-layer glycoprotein Csg and HVO_0405 (PubMed:23651326, PubMed:26712937, PubMed:28069824). ArtA is required for the C-terminal processing of Csg and for its lipidation and attachment to the archaeal plasma membrane (PubMed:23651326, PubMed:26712937). It is also required for the processing of HVO_0405, which contains an atypical central tripartite structure (PubMed:28069824).
Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively.
Belongs to the uracil-DNA glycosylase (UDG) superfamily. Type 4 (UDGa) family.
Homotrimer. The subunits circularize to form a toroid; DNA passes through its center. Replication factor C (RFC) is required to load the toroid on the DNA.
Sliding clamp subunit that acts as a moving platform for DNA processing. Responsible for tethering the catalytic subunit of DNA polymerase and other proteins to DNA during high-speed replication.
Sliding clamp subunit. Responsible for tethering the catalytic subunit of DNA polymerase to DNA during high-speed replication.
Belongs to the acyl-CoA dehydrogenase family.
Belongs to the complex I 20 kDa subunit family.
Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate.
Belongs to the HAD-like hydrolase superfamily.
Belongs to the eukaryotic ribosomal protein eL40 family.
Belongs to the eukaryotic ribosomal protein eL21 family.
Belongs to the RimK family. LysX subfamily.
Belongs to the deoxyhypusine synthase family.
Belongs to the intradiol ring-cleavage dioxygenase family.
Belongs to the class-II aminoacyl-tRNA synthetase family.
Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Belongs to the urease gamma subunit family.
Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha) subunits. Three heterotrimers associate to form the active enzyme.
Homodimer. Heterotetramer of two Top6A and two Top6B chains.
Relaxes both positive and negative superturns and exhibits a strong decatenase activity.
Belongs to the activator 1 small subunits family. RfcL subfamily.
Heteromultimer composed of small subunits (RfcS) and large subunits (RfcL).
Part of the RFC clamp loader complex which loads the PCNA sliding clamp onto DNA.
Belongs to the ATPase alpha/beta chains family.
Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal alpha chain is a catalytic subunit.
H.volcanii possesses two TatC translocases: TatCo and TatCt. Both paralogs are structurally atypical and may represent adaptation to the extensive utilization of the Tat pathway in haloarchaea (PubMed:16291683).
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes.
Belongs to the SAM hydrolase / SAM-dependent halogenase family.
Catalyzes the oxidation of methyl-H(4)MPT to methylene-H(4)MPT.
Belongs to the SLC41A transporter family.
Belongs to the eukaryotic ribosomal protein eL43 family.
Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.
Belongs to the universal ribosomal protein uL11 family.
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
Part of the ribosomal stalk of the 50S ribosomal subunit. Interacts with L10 and the large rRNA to form the base of the stalk. L10 forms an elongated spine to which L12 dimers bind in a sequential fashion forming a multimeric L10(L12)X complex.
Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.
Catalyzes the synthesis of GMP from XMP.
Heterodimer composed of a glutamine amidotransferase subunit (A) and a GMP-binding subunit (B).
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 ribonucleoside diphosphate reductase class-2 family.
Catalyzes the reduction of ribonucleotides to deoxyribonucleotides. May function to provide a pool of deoxyribonucleotide precursors for DNA repair during oxygen limitation and/or for immediate growth after restoration of oxygen.
Belongs to the 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.
Forms a complex with TatC (By similarity). Cytoplasmic and membrane-bound TatA form high-molecular-weight complexes.
H.volcanii possesses two TatA translocases: TatAo and TatAt. Each may interact with specific Tat substrates (PubMed:16291683).
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system (Probable).
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
The PTS EIIB type-2 domain is phosphorylated by phospho-EIIA on a cysteinyl residue. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the PTS EIIC type-2 domain.
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II PtfABC PTS system is involved in fructose transport.
Belongs to the archaeal Rpo5/eukaryotic RPB5 RNA polymerase subunit family.
DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR).
Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)- to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR).
Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily.
Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding.
Homodimer. The tRNA molecule binds across the dimer.
Belongs to the acetylglutamate kinase family. LysZ subfamily.
Involved in both the arginine and lysine biosynthetic pathways. Phosphorylates the LysW-bound precursors glutamate (for arginine biosynthesis), respectively alpha-aminoadipate (for lysine biosynthesis).
Belongs to the carbohydrate kinase PfkB family.
Deletion of the gene abolishes growth on glucose, but does not affect growth on galactose. Double deletion mutant kdgK1/kdgK2 loses the ability to grow on galactose.
Involved in the degradation of glucose via the semi-phosphorylative Entner-Doudoroff pathway. Catalyzes the phosphorylation of 2-keto-3-deoxygluconate (KDG) to produce 2-keto-3-deoxy-6-phosphogluconate (KDPG). Also catalyzes efficiently the phosphorylation of 2-keto-3-deoxygalactonate (KDGal) to 2-keto-3-deoxy-6-phosphogalactonate (KDPGal).
Belongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family.
Carbamylation allows a single lysine to coordinate two nickel ions.
Carboxylation allows a single lysine to coordinate two nickel ions.
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.
Part of an ABC transporter complex involved in anions import.
Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
The complex is composed of two ATP-binding proteins (HVO_1886), two transmembrane proteins (HVO_1887) and a solute-binding protein (HVO_1888).
Belongs to the SIMIBI class G3E GTPase family. ZNG1 subfamily.
Component of the Sec protein translocase complex. Heterotrimer consisting of SecY (alpha), SecG (beta) and SecE (gamma) subunits. The heterotrimers can form oligomers, although 1 heterotrimer is thought to be able to translocate proteins. Interacts with the ribosome. May interact with SecDF, and other proteins may be involved.
Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Belongs to the archaeal-type GTP cyclohydrolase family.
Catalyzes the formation of 2-amino-5-formylamino-6-ribofuranosylamino-4(3H)-pyrimidinone ribonucleotide monophosphate and inorganic phosphate from GTP. Also has an independent pyrophosphate phosphohydrolase activity.
Belongs to the complex I subunit 4 family.
The crystal structure with reduced Cu(1+) has also been determined.
Belongs to the transcriptional regulator TrmB family.
Belongs to the universal ribosomal protein uL16 family.
Seems to be required for maximal rate of protein biosynthesis. Enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal subunits.
Belongs to the glucose-1-phosphate thymidylyltransferase family.
Impaired formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg. No effect on 'Asn-47' and 'Asn-117' glycosylation of S-layer glycoprotein Csg.
Nucleotidyltransferase involved in N-glycan biosynthetic pathway that takes place under low-salt conditions (1.75 M instead of 3.4 M). Participates in the formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg, consisting of a sulfated hexose, 2 hexoses and rhamnose. Involved in the addition of final rhamnose (sugar 4) of the tetrasaccharide on the dolichol phosphate carrier.
Belongs to the radical SAM superfamily. 7-carboxy-7-deazaguanine synthase family.
Binds 1 S-adenosyl-L-methionine per subunit.
Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
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.
Heterodimer composed of Spt4 and Spt5. Interacts with RNA polymerase (RNAP).
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.
By heat shock (60 degrees Celsius), with a 2-fold increase (at protein level).
Stabilizes TBP binding to an archaeal box-A promoter. Also responsible for recruiting RNA polymerase II to the pre-initiation complex (DNA-TBP-TFIIB).
There are 6-12 TFIIB paralogs in this organism.
Belongs to the protein kinase superfamily. BUD32 family.
Component of the KEOPS complex that consists of Kae1, Bud32, Cgi121 and Pcc1; the whole complex dimerizes.
In the C-terminal section; belongs to the protein kinase superfamily. Tyr protein kinase family. BUD32 subfamily.
In the N-terminal section; belongs to the KAE1 / TsaD family.
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is a component of the KEOPS complex that is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. The Kae1 domain likely plays a direct catalytic role in this reaction. The Bud32 domain probably displays kinase activity that regulates Kae1 function.
Belongs to the metallo-dependent hydrolases superfamily. MTA/SAH deaminase family.
Catalyzes the deamination of 5-methylthioadenosine and S-adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L-homocysteine, respectively. Is also able to deaminate adenosine.
Belongs to the ribose-phosphate pyrophosphokinase family. Class III (archaeal) subfamily.
Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P).
Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.
Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family.
Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Interacts with the DNA polymerase sliding clamp (PCNA) via the PIP (PCNA-interacting peptide) motif.
Involved in DNA damage repair. Works together with the UvrABC proteins in repairing DNA damage resulting from exposure to the DNA damaging agent mitomycin C (MMC).
Non-essential, but cells lacking this gene are sensitive to DNA damage induced by treatment with MMC. Does not display increased sensitivity to UV light or to the alkylating agent methyl methanesulphonate (MMS).
Belongs to the universal ribosomal protein uL23 family.
Binds to 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome.
Part of the 50S ribosomal subunit. Contacts protein L29.
Belongs to the heme-copper respiratory oxidase family.
Belongs to the isocitrate and isopropylmalate dehydrogenases family.
Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Belongs to the phosphatidylserine decarboxylase family. PSD-A subfamily.
Binds 1 pyruvoyl group covalently per subunit.
Catalyzes the formation of archaetidylethanolamine (PtdEtn) from archaetidylserine (PtdSer).
Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit.
Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain.
Belongs to the eukaryotic ribosomal protein eS1 family.
Belongs to the methyl-accepting chemotaxis (MCP) protein family.
The PTS EIIA type-2 domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the PTS EIIB type-2 domain.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Belongs to the PNP/UDP phosphorylase family.
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.
Belongs to the eukaryotic ribosomal protein eL42 family.
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 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.
Belongs to the bacterial solute-binding protein 1 family. WtpA subfamily.
Part of an ABC transporter complex involved in molybdenum import.
The complex is composed of two ATP-binding proteins, two transmembrane proteins (HVO_B0370) and a solute-binding protein (HVO_B0369).
Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35) family.
Belongs to the universal ribosomal protein uS3 family.
Binds the lower part of the 30S subunit head.
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 phosphohexose mutase family.
Belongs to the inorganic phosphate transporter (PiT) (TC 2.A.20) family.
Belongs to the ribose 5-phosphate isomerase family.
Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
Does not affect motility. No differences in growth rate or cell size.
Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.
Belongs to the peroxidase family. Peroxidase/catalase subfamily.
Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.
Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme.
Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ and 2 PurS subunits.
Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Belongs to the thymidylate kinase family.
Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. HflX GTPase family.
GTPase that associates with the 50S ribosomal subunit and may have a role during protein synthesis or ribosome biogenesis.
Monomer. Associates with the 50S ribosomal subunit.
Belongs to the eukaryotic ribosomal protein eS24 family.
Acetylated. The acetylated form at Met-1 was shown to be in 100-fold excess of the unacetylated form with the initiator methionine removed in whole cells and purified 20S proteasomes.
Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.
Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The H.volcanii alpha1-beta proteasome is able to cleave oligopeptides after Phe, Tyr and Trp, poorly after Glu but not after Arg. Thus, displays chymotrypsin-like activity, low caspase-like activity but no trypsin-like activity.
H.volcanii proteasome requires high concentrations of salt, similar to the extracellular environment and cytoplasm of this organism, for complex stability and optimal activity.
Strains lacking psmA1 gene alone display relatively normal growth rate and overall cell yield, but they are more sensitive to growth on organic versus inorganic nitrogen sources and hypo-osmotic stress, and they show limited growth in the presence of L-canavanine. Abolition of alpha1 subunit synthesis also has a severe impact on the ability of cells to withstand thermal stress. Moreover, depletion of psmA1 and psmA2 together renders the cells inviable.
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. H.volcanii produces at least 2 types of 20S proteasomes: an alpha1-beta proteasome and a proteasome containing all three subunits (alpha1, alpha2, and beta) that appears to be asymmetrical with homo-oligomeric alpha1 and alpha2 rings positioned on separate ends. The catalytic chamber with the active sites is on the inside of the barrel. Has probably a gated structure, the ends of the cylinder being occluded by the N-termini of the alpha-subunits. Is likely capped at one or both ends by the proteasome regulatory ATPase, PAN.
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 (By similarity). In vitro, the chymotrypsin-like activity of the alpha1-beta proteasome is potently inhibited by carbobenzoxyl-leucinyl-leucinyl-leucinal-H (MG132) and significantly by N-acetyl-leucinyl-leucinyl-norleucinal-H (calpain inhibitor I).
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.
Up-regulated at the mRNA level during transition from exponential to stationary phase. However, at the protein level, PsmA 1 is expressed at a high and relatively constant level throughout growth.
Belongs to the eukaryotic ribosomal protein eL31 family.
Cells lacking this gene are auxotrophic for thiamine. The mutants thiamine requirement can be overcome by adding thiazole moiety 4-methyl-5-(beta-hydroxyethyl)thiazole (THZ) to the growth medium.
During the catalytic reaction, a sulfide is transferred from Cys-165 to a reaction intermediate, generating a dehydroalanine residue.
Involved in biosynthesis of the thiamine precursor thiazole (PubMed:25348237). Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid (ADT), an adenylated thiazole intermediate. The reaction includes an iron-dependent sulfide transfer from a conserved cysteine residue of the protein to a thiazole intermediate. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme (By similarity).
Belongs to the glutamine synthetase family.
Glutamine synthetase (GS) is an unusual multitasking protein that functions as an enzyme, a transcription coregulator, and a chaperone in ammonium assimilation and in the regulation of genes involved in nitrogen metabolism. It catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. Feedback-inhibited GlnA also interacts with and regulates the activity of the transcriptional regulator TnrA. During nitrogen limitation, TnrA is in its DNA-binding active state and turns on the transcription of genes required for nitrogen assimilation. Under conditions of nitrogen excess, feedback-inhibited GlnA forms a stable complex with TnrA, which inhibits its DNA-binding activity. In contrast, feedback-inhibited GlnA acts as a chaperone to stabilize the DNA-binding activity of GlnR, which represses the transcription of nitrogen assimilation genes.
Oligomer of 12 subunits arranged in the form of two hexagons. In its feedback-inhibited form, interacts with TnrA in order to block its DNA-binding activity.
Belongs to the HMG-CoA reductase family.
Catalyzes the NADPH-dependent reductive deacylation of (S)-3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) to (R)-mevalonate. 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. Is also able to catalyze the reduction of mevaldehyde to mevalonate and the oxidative acylation of mevaldehyde to HMG-CoA.
Is competitively inhibited by (R)-HMG-CoA and lovastatin (formerly called mevinolin).
Up-regulated during growth at high salinity.
Belongs to the short-chain dehydrogenases/reductases (SDR) family.
Belongs to the polyphosphate kinase 2 (PPK2) family. Class I subfamily.
Belongs to the serine/threonine dehydratase family.
A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
Belongs to the topoisomerase GyrA/ParC subunit family.
Belongs to the type II topoisomerase GyrA/ParC subunit family.
Few gyrases are as efficient as E.coli at forming negative supercoils. Not all organisms have 2 type II topoisomerases; in organisms with a single type II topoisomerase this enzyme also has to decatenate newly replicated chromosomes.
Heterotetramer, composed of two GyrA and two GyrB chains. In the heterotetramer, GyrA contains the active site tyrosine that forms a transient covalent intermediate with DNA, while GyrB binds cofactors and catalyzes ATP hydrolysis.
Binds 2 Zn(2+) ions per subunit. One is catalytic, whereas the other seems to have a structural role.
Probable zinc metalloprotease whose natural substrate is unknown.
Belongs to the AdoMet synthase 2 family.
Catalyzes the formation of S-adenosylmethionine from methionine and ATP.
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 helicase family. Hel308 subfamily.
DNA-dependent ATPase and 3'-5' DNA helicase that may be involved in repair of stalled replication forks.
Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. EngB GTPase family.
Necessary for normal cell division and for the maintenance of normal septation.
Belongs to the isocitrate lyase/PEP mutase superfamily.
Involved in the metabolic adaptation in response to environmental changes. Catalyzes the reversible formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle during growth on fatty acid substrates.
Belongs to the eukaryotic/archaeal RNase P protein component 1 family.
Consists of a catalytic RNA component and at least 4-5 protein subunits.
Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Belongs to the CDP-alcohol phosphatidyltransferase class-I family.
Involved in regulation of DNA replication.
Belongs to the helicase family. RAD25/XPB subfamily.
Belongs to the FAD-dependent oxidoreductase 2 family. NadB subfamily.
Cells lacking this gene grow similarly to wild-type in the presence of either DMSO or oxygen as the terminal electron acceptor, but are retarded in aerobic growth at 50 degrees Celsius. The lysine tRNAs of the mutant strain appear to be nonthiolated.
Functions as a protein modifier covalently attached to lysine residues of substrate proteins, as well as a sulfur carrier in tRNA thiolation. The protein modification process is termed sampylation and involves the formation of an isopeptide bond between the SAMP2 C-terminal glycine carboxylate and the epsilon-amino group of lysine residues on target proteins. Is able to form polymeric chains with itself at Lys-58, similar to ubiquitin and other ubiquitin-like proteins. May serve as a proteolytic signal in the cell to target proteins for degradation by proteasomes.
Monomer (PubMed:23821306). Monomeric and polymeric forms interact with NcsA (PubMed:24906001).
The C-terminal glycine is likely acyl-adenylated (-COAMP) by UbaA, and also probably thiocarboxylated (-COSH) to function in sulfur transfer.
Belongs to the glycosyltransferase 2 family.
Cells do not generate the small monosaccharide-charged dolichol phosphate species.
Glycosyltransferase that adds a monosaccharide to dolichol phosphate, thereby being responsible for generating one of the three monosaccharide-modified dolichol phosphates. The subunit onto which additional sugars are added is not known.
Deletion mutant loses its ability to grow on both D-xylose and L-arabinose.
Essential for D-xylose and L-arabinose catabolism. Activates the expression of genes involved in D-xylose and L-arabinose degradation (xacABCDEF) and represses its own synthesis (PubMed:25141768, PubMed:28854683). Also up-regulates the expression of the genes encoding the ABC transporter complex XacGHIJK (PubMed:31089701).
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.
Inactivation renders cells sensitive to DNA damage. Deletion of both ligA and ligN is lethal.
ATP-dependent agmatine transferase that catalyzes the formation of 2-agmatinylcytidine (agm2C) at the wobble position (C34) of tRNA(Ile2), converting the codon specificity from AUG to AUA.
Belongs to the NAGSA dehydrogenase family. Type 1 subfamily. LysY sub-subfamily.
Involved in both the arginine and lysine biosynthetic pathways.
Protects DNA against thermal denaturation and modulates transcription.
Catalyzes the first step of diphthamide biosynthesis, i.e. the transfer of the 3-amino-3-carboxypropyl group from S-adenosyl-L-methionine (SAM) to the C2 position of the imidazole ring of the target histidine residue in translation elongation factor 2 (EF-2).
Activity improves as salinity decreases.
Belongs to the UDP-glucose/GDP-mannose dehydrogenase family.
Involved in the assembly of a N-linked pentasaccharide that decorates the S-layer glycoprotein and flagellins. Involved in the biosynthesis of the hexuronic acids found at both positions 2 and 3 of the pentasaccharide.
Mutants exhibit defective or limited motility.
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 eukaryotic ribosomal protein eL39 family.
Belongs to the eukaryotic/archaeal RNase P protein component 4 family.
Belongs to the archaeal Rpo10/eukaryotic RPB10 RNA polymerase subunit family.
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.
Belongs to the peptidase S16 family. Archaeal LonB subfamily.
Homohexamer. Organized in a ring with a central cavity.
Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
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.
Activates transcription of the denitrifying genes (nitrate reductase narA and nitrite reductase nirK) under anaerobic conditions.
Cells lacking this gene are not able to grow anaerobically by denitrification. Inactivated transcription of the denitrifying genes (nitrate reductase narA and nitrite reductase nirK). No effect on growth under aerobic conditions. No effect on dimethyl sulfoxide (DMSO) respiration.
Constitutively expressed regardless of cultivation under aerobic or anaerobic conditions. Increased expression under denitrifying conditions.
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.
The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
The glycine cleavage system is composed of four proteins: P, T, L and H.
Belongs to the prefoldin alpha subunit family.
Belongs to the prefoldin subunit alpha family.
Heterohexamer of two alpha and four beta subunits.
Molecular chaperone capable of stabilizing a range of proteins. Seems to fulfill an ATP-independent, HSP70-like function in archaeal de novo protein folding.
Catalyzes the transfer of a methyl group to L-homocysteine resulting in methionine formation. The physiological methyl donor is unknown.
Catalyzes the deamination of dCTP to dUTP.
Belongs to the DsbB family. BdbC subfamily.
Belongs to the binding-protein-dependent transport system permease family. FecCD subfamily.
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 GTP cyclohydrolase I type 2/NIF3 family.
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.
Belongs to the FAD-dependent glycerol-3-phosphate dehydrogenase family.
Composed of a catalytic GlpA/B dimer and of membrane bound GlpC.
Conversion of glycerol 3-phosphate to dihydroxyacetone phosphate. Functional analog of glpA1 required for the basal levels of glycerol-3-phosphate dehydrogenase activity, but not expressed during standard growth on glycerol or when glpA1 is knockout.
H.volcanii contains 2 glpABC operons, one located on the main chromosome and the other on megaplasmid pHV4.
Belongs to the glutaredoxin family. Monothiol subfamily.
Part of the ABC transporter complex XacGHIJK involved in the uptake of xylose and arabinose (PubMed:31089701). Responsible for the translocation of the substrate across the membrane (Probable).
The complex is composed of two ATP-binding proteins (XacJ and XacK), two transmembrane proteins (XacH and XacI) and a solute-binding protein (XacG).
Transcriptionally up-regulated by both L-arabinose and D-xylose via the pentose-specific regulator XacR.
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 universal ribosomal protein uS10 family.
Involved in the binding of tRNA to the ribosomes.
Belongs to the GTP-dependent DPCK family.
Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).
Belongs to the eukaryotic/archaeal RNase P protein component 3 family.
Belongs to the small heat shock protein (HSP20) family.
Belongs to the archaeal IMP cyclohydrolase family.
Catalyzes the cyclization of 5-formylamidoimidazole-4-carboxamide ribonucleotide to IMP.
Can complement an H.volcanii mutant strain that is thymidine auxotroph because it lacks the two dihydrofolate reductase genes encoded by hdrA and hdrB.
In the C-terminal section; belongs to the DHPS family.
In the N-terminal section; belongs to the folylpolyglutamate synthase family.
Belongs to the ornithine cyclodeaminase/mu-crystallin family. Archaeal alanine dehydrogenase subfamily.
Catalyzes the NAD(+)-dependent oxidative deamination of L-alanine to pyruvate, and the reverse reaction, the reductive amination of pyruvate.
Contains catalytic and regulatory chains.
Involved in allosteric regulation of aspartate carbamoyltransferase.
Belongs to the CDP-archaeol synthase family.
Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.
Belongs to the radical SAM superfamily. Biotin synthase family.
Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine.
Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
Decarboxylates L-threonine-O-3-phosphate to yield (R)-1-amino-2-propanol O-2-phosphate, the precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin.
Belongs to the ATP-dependent AMP-binding enzyme family. MenE subfamily.
Converts 2-succinylbenzoate (OSB) to 2-succinylbenzoyl-CoA (OSB-CoA).
Belongs to the iron/manganese superoxide dismutase family.
Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Belongs to the SMC family. RAD50 subfamily.
Homodimer. Forms a heterotetramer composed of two Mre11 subunits and two Rad50 subunits.
Mutants are more resistant to DNA damage, but recover more slowly than the wild-type.
Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. Rad50 controls the balance between DNA end bridging and DNA resection via ATP-dependent structural rearrangements of the Rad50/Mre11 complex (By similarity). In polyploid organisms, the Rad50/Mre11 complex appears to restrain the repair of double-strand breaks by homologous recombination, allowing another pathway to act as the primary mode of repair (PubMed:19593371).
The two conserved Cys that bind zinc constitute the zinc-hook, which separates the large intramolecular coiled coil regions. The 2 Cys residues coordinate one molecule of zinc with the help of the 2 Cys residues of the zinc-hook of another Rad50 molecule, thereby forming a V-shaped homodimer.
Belongs to the glycosyl hydrolase 28 family.
Belongs to the adenylate cyclase family. DacZ subfamily.
Cannot use Mg(2+), Ca(2+), Ni(2+) or Co(2+) instead of Mn(2+) as cofactor.
Diadenylate cyclase that catalyzes the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP). c-di-AMP is a second messenger for intracellular signal transduction involved in the control of important regulatory processes such as osmoregulation.
Diadenylate cyclase that catalyzes the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP). c-di-AMP is a second messenger for intracellular signal transduction involved in the control of important regulatory processes such as osmoregulation. Is essential for H.volcanii. Overexpression of DacZ leads to cell death, suggesting the need for tight regulation of c-di-AMP levels. Cannot use GTP as substrate.
Is constantly expressed at different growth phases in rich and selective media.
It was not possible to obtain a strain in which the dacZ gene was deleted in standard growth conditions, indicating that dacZ is an essential gene.
Nudix hydrolase involved in N-glycan biosynthetic pathway that takes place under low-salt conditions (1.75 M instead of 3.4 M). Participates in the formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg, consisting of a sulfated hexose, 2 hexoses and rhamnose. Mediates attachment of sugar 3 in the tetrasaccharide.
Catalyzes the reversible oxidation of malate to oxaloacetate.
Belongs to the arginase family. Agmatinase subfamily.
Belongs to the GGGP/HepGP synthase family. Group I 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.
Conversion of glycerol 3-phosphate to dihydroxyacetone phosphate. Required for growth on glycerol and for glycerol metabolism.
Unable to grow on glycerol. Can be complemented in trans by glpA2 under the control from a strong promoter.
Up-regulated by glycerol and no inhibition by glucose.
Belongs to the 2-oxoacid dehydrogenase family.
Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
Heterooligomer of catalytic and regulatory chains.
Belongs to the MsrA Met sulfoxide reductase family.
Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Probable metalloprotease. Does not hydrolyze SAMP1- and SAMP2-protein conjugates, diglycine-AMC, Ub-AMC, hemoglobin, cytochrome c, carbonic anhydrase, creatinine phosphokinase, beta-amylase and bovine serum albumin.
Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Belongs to the universal ribosomal protein uS15 family.
Belongs to the archaeal Rpo12/eukaryotic RPC10 RNA polymerase subunit family.
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.
Auxotroph for uracil and resistant to 5-FOA (5-fluoroorotic acid).
Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrE subfamily.
Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Belongs to the V-ATPase F subunit family.
Composed of six subunits; A, B, C, D, E, F and G.
Belongs to the FPP/GGPP synthase family.
Belongs to the precorrin methyltransferase family.
General factor that plays a role in the activation of archaeal genes transcribed by RNA polymerase. Binds specifically to the TATA box promoter element which lies close to the position of transcription initiation (By similarity).
General factor that plays a role in the activation of archaeal genes transcribed by RNA polymerase. Binds specifically to the TATA box promoter element which lies close to the position of transcription initiation.
Belongs to the 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.
Belongs to the phosphomevalonate decarboxylase family.
Catalyzes the decarboxylation of mevalonate 5-phosphate (MVAP) to isopentenyl phosphate (IP). Functions in an alternate mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoid compounds such as archaeal membrane lipids.
Is strongly inhibited by 6-fluoromevalonate monophosphate but shows negligible inhibition by 6-fluoromevalonate diphosphate (a potent inhibitor of the classical mevalonate pathway).
Belongs to the mandelate racemase/muconate lactonizing enzyme family.
Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues.
Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly.
Belongs to the pterin-4-alpha-carbinolamine dehydratase family.
Belongs to the aspartate/ornithine carbamoyltransferase superfamily. OTCase family.
Catalyzes the reversible phosphorylation of UMP to UDP.
Belongs to the DNA polymerase type-Y family.
Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis.
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). Plasmid targeted by CRISPR locus P1 transform wild-type cells very poorly (PubMed:22767603). This protein helps process or stabilize pre-crRNA into individual crRNA units, in vivo Cas6 and Cas7 are also required for optimal crRNA processing and/or stability (PubMed:24459147).
Component of the Cascade-like complex (Cascade I-B), composed of Cas5, Cas6, Cas7 and crRNA.
Loss of the 8 Cas genes in this locus (cas1, cas2, cas3, cas4, cas5, cas6, cas7 and cas8b) leads to loss of CRISPR interference against plasmid targeted by this CRISPR locus, i.e. plasmid is not destroyed by CRISPR.
There are 3 CRISPR RNA loci in this organism and a single cas gene locus. A CRISPR-Cas type I-B system.
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.
Binds 2 divalent metal cations per subunit.
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 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).
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 (By similarity). Binds GTP and shows GTPase activity, but only at high salt (2 M KCl) concentrations (PubMed:8858586). Involved in division ring assembly directing the assembly, positioning and stabilization of FtsZ2 at the midcell envelope. Plays a role in defining cell shape (PubMed:33903747).
Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.
Homodimer. Polymerizes to form a dynamic ring structure in a strictly GTP-dependent manner. Interacts directly with several other division proteins.
It is uncertain whether Met-1 or Met-36 is the initiator.
Viable, but have fewer colony-forming units compared to wild-type. Cells are very heterogeneously sized and misshapen, and have a notable amount of cellular debris. Defects in cell division. Loss or very weak Z2 ring formation. FtsZ1/FtsZ2 double deletion mutant cells show various division defects, including fragmentation, budding, polar tubulation and fission resulting in DNA-containing particles, which are able to remain viable and propagate without regular cell division.
Belongs to the succinate/malate CoA ligase alpha subunit family.
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 alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit.
Belongs to the anthranilate synthase component I family.
Heterotetramer consisting of two non-identical subunits: a beta subunit (TrpG) and a large alpha subunit (TrpE).
Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia (By similarity).
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.
Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
Belongs to the enoyl-CoA hydratase/isomerase family.
In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.
Cells lacking this gene do not grow anaerobically with DMSO and do not show DMSO reductase activity although dmsA transcript is present, indicating lack of maturation of the DmsA apoprotein into the MoCo-holoprotein. Their growth in the presence of oxygen is not affected. Disruption of this gene does not affect the formation of SAMP-protein conjugates.
Converts molybdopterin precursor Z into molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by the thiocarboxylated form of SAMP1 (Probable).
In the C-terminal section; belongs to the MoaE family.
Sampylated at Lys-240 and Lys-247 with the archaeal ubiquitin-like proteins SAMP1 and SAMP3, which may regulate enzymatic activity.
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 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.
Cells lacking this gene grow similarly to wild-type in the presence of either DMSO or oxygen as the terminal electron acceptor; thus, SAMP3 is not needed for DMSO respiration, suggesting that it is not required for molybdenum cofactor (MoCo) biosynthesis. tRNA thiolation is not affected.
Functions as a protein modifier covalently attached to lysine residues of substrate proteins. The protein modification process is termed sampylation and involves the formation of an isopeptide bond between the SAMP3 C-terminal glycine carboxylate and the epsilon-amino group of lysine residues on target proteins. Seems to be able to form polymeric chains with itself at Lys-18, Lys-55 and Lys-62, similar to ubiquitin and other ubiquitin-like proteins. SAMP3 appears not to serve as a proteolytic signal in the cell to target proteins for degradation by proteasomes. May regulate molybdenum cofactor (MoCo) biosynthesis by inhibiting the activity of MPT synthase MoaE under aerobic conditions, providing a hierarchy of oxygen use prior to that of alternative electron acceptors such as DMSO.
The C-terminal glycine is likely acyl-adenylated (-COAMP) by UbaA.
Up-regulated by the addition of dimethyl sulfoxide to aerobically growing cells. These conditions also increase the levels of SAMP3 conjugates in cells.
Belongs to the eukaryotic ribosomal protein eS8 family.
Belongs to the DNA mismatch repair MutS family. Archaeal Muts2 subfamily.
Has ATPase and non-specific DNA-binding activities.
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.
Belongs to the gamma-glutamyl phosphate reductase family.
Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.
Belongs to the 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.
Expression is repressed by glycerol but highly up-regulated in the presence of fructose or glucose, regardless of glycerol supplementation.
Leads to pfkB-specific transcript up-regulation.
Transcriptional repressor of genes encoding both fructose and glucose metabolic enzymes such as phosphofructokinase (PFK) or 2-keto-3-deoxy-D-gluconate kinase (KDGK) during growth on glycerol. Required for the glycerol-mediated repression of pfkB-specific transcripts, but not needed for the high-levels of the pfkB-specific transcript present when cells are grown on fructose.
Specifically catalyzes the AdoMet-dependent 2'-O-ribose methylation of cytidine at position 56 in tRNAs.
Involved in the protein N-glycosylation pathway responsible for the assembly and attachment of an N-linked pentasaccharide that decorates the S-layer glycoprotein and flagellins (PubMed:18631242, PubMed:21091511, PubMed:22730124). Catalyzes the transfer of a glucuronate residue (GlcA) to a glucose residue already bound to a dolichol phosphate (DolP), a compound that serves as a glycan lipid carrier in Archaea. In vitro, is able to add GlcA to DolP-Glc in which the omega-position isoprene is not saturated. However, the likely physiological lipid substrate is alpha,omega-saturated (PubMed:28809486).
Mutants contain only hexose-modified phosphodolichols and exhibit defective or limited motility.
Belongs to the archaeosine tRNA-ribosyltransferase family.
Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.
Mutants lack the archaeosine modification, but do not show any growth defects.
Belongs to the OHCU decarboxylase family.
Catalyzes the stereoselective decarboxylation of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) to (S)-allantoin.
In the C-terminal section; belongs to the complex I 49 kDa subunit family.
In the N-terminal section; belongs to the complex I 30 kDa subunit family.
NDH-1 is composed of 13 different subunits. Subunits NuoB, CD, E, F, and G constitute the peripheral sector of the complex (By similarity).
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity).
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.
To bacterial alkanal monooxygenase alpha and beta chains.
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 SOS response-associated peptidase family.
Belongs to the beta-class carbonic anhydrase family.
Belongs to the adenylosuccinate synthetase family.
Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Belongs to the 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.
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 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 hydrolysis of the adenine ring of phosphoribosyl-AMP.
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.
The FO synthase complex consists of two subunits, CofG and CofH.
Belongs to the prefoldin subunit beta family.
Belongs to the type IA topoisomerase family.
Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.
Belongs to the zinc-containing alcohol dehydrogenase family.
Belongs to the glycosyltransferase group 1 family.
Hexosyltransferase involved in N-glycan biosynthetic pathway that takes place under low-salt conditions (1.75 M instead of 3.4 M). Participates in the formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg, consisting of a sulfated hexose, 2 hexoses and rhamnose. Involved in the addition of sugar 3 to the disaccharide-charged dolichol phosphate in the tetrasaccharide.
Belongs to the eukaryotic ribosomal protein eS17 family.
Belongs to the universal ribosomal protein uL18 family.
Part of the 50S ribosomal subunit. Contacts the 5S and 23S rRNAs (By similarity).
Part of the 50S ribosomal subunit. Contacts the 5S and 23S rRNAs.
This is one of the proteins that bind and probably mediate the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.
Belongs to the DNA photolyase class-1 family.
Binds 1 5,10-methenyltetrahydrofolate (MTHF) per subunit.
Belongs to the eukaryotic ribosomal protein eL19 family.
Belongs to the NAD(P)-dependent epimerase/dehydratase family.
Catalyzes the NAD-dependent oxidation of glucose 6-phosphate to 6-phosphogluconolactone.
Deletion mutants do not grow on glucose.
Belongs to the HAD-like hydrolase superfamily. SerB family.
Belongs to the dTDP-4-dehydrorhamnose reductase family.
Reductase involved in N-glycan biosynthetic pathway that takes place under low-salt conditions (1.75 M instead of 3.4 M). Participates in the formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg, consisting of a sulfated hexose, 2 hexoses and rhamnose. Involved in the addition of final rhamnose (sugar 4) of the tetrasaccharide on the dolichol phosphate carrier.
Belongs to the class-I aminoacyl-tRNA synthetase family.
Contains large globular domains required for ATP hydrolysis at each terminus and a third globular domain forming a flexible hinge near the middle of the molecule. These domains are separated by coiled-coil structures.
Required for chromosome condensation and partitioning.
Belongs to the RNA cytidine acetyltransferase family. TmcA subfamily.
Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl donor and ATP (or GTP).
Mutants lack the ac(4)C modification, but do not show any growth defects.
Binds 1 divalent metal cation per subunit (By similarity). Most active with Co(2+), Mg(2+) or Mn(2+). Has weaker activity with Fe(2+), Ni(2+) or Zn(2+) (PubMed:28854683).
Deletion mutant shows restricted growth on L-arabinose but grows on D-xylose as the wild type.
Pentonolactonase involved in D-arabinose and D-xylose catabolism. Catalyzes the hydrolysis of both L-arabino-gamma-lactone and D-xylono-gamma-lactone to the corresponding acids. Can also hydrolyze D-galactono-gamma-lactone and D-glucono-delta-lactone.
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
UreD, UreF and UreG form a complex that acts as a GTP-hydrolysis-dependent molecular chaperone, activating the urease apoprotein by helping to assemble the nickel containing metallocenter of UreC. The UreE protein probably delivers the nickel.
Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family.
Belongs to the isopentenyl phosphate kinase family.
Catalyzes the phosphorylation of isopentenyl phosphate (IP) to isopentenyl diphosphate (IPP). Functions in an alternate mevalonate (MVA) pathway leading to IPP, a key precursor for the biosynthesis of isoprenoid compounds such as archaeal membrane lipids.
A single active site specifically recognizes both ATP and CTP and is responsible for their addition.
Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.
Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition is required both for tRNA processing and repair. Also involved in tRNA surveillance by mediating tandem CCA addition to generate a CCACCA at the 3' terminus of unstable tRNAs. While stable tRNAs receive only 3'-terminal CCA, unstable tRNAs are marked with CCACCA and rapidly degraded.
Belongs to the LDH/MDH superfamily. LDH family.
Belongs to the eukaryotic ribosomal protein P1/P2 family.
Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.
Part of the 50S ribosomal subunit. Homodimer, it forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Forms a heptameric L10(L12)2(L12)2(L12)2 complex, where L10 forms an elongated spine to which the L12 dimers bind in a sequential fashion.
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 uL10/P0(P1)2(P1)2(P1)2 complex, where uL10/P0 forms an elongated spine to which the P1 dimers bind in a sequential fashion.
Belongs to the eukaryotic ribosomal protein eS28 family.
Catalyzes the transfer of diphosphate from ATP to 6-hydroxymethyl-7,8-dihydropterin (6-HMD), leading to 6-hydroxymethyl-7,8-dihydropterin diphosphate (6-HMDP).
In the C-terminal section; belongs to the phosphate acetyltransferase and butyryltransferase family.
In the N-terminal section; belongs to the malic enzymes family.
Belongs to the MenA family. Type 1 subfamily.
Conversion of 1,4-dihydroxy-2-naphthoate (DHNA) to demethylmenaquinone (DMK).
Belongs to the complex I subunit 3 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 archaeal histone HMF family.
Belongs to the thiamine-monophosphate kinase family.
Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.
Reaction mechanism of ThiL seems to utilize a direct, inline transfer of the gamma-phosphate of ATP to TMP rather than a phosphorylated enzyme intermediate.
Belongs to the ETF alpha-subunit/FixB family.
Involved in ribosome biogenesis; more specifically in 18S rRNA pseudouridylation and in cleavage of pre-rRNA.
Belongs to the XPG/RAD2 endonuclease family. FEN1 subfamily.
Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Interacts with PCNA. PCNA stimulates the nuclease activity without altering cleavage specificity.
Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Binds the unpaired 3'-DNA end and kinks the DNA to facilitate 5' cleavage specificity. Cleaves one nucleotide into the double-stranded DNA from the junction in flap DNA, leaving a nick for ligation. Also involved in the base excision repair (BER) pathway. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA.
Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Binds the unpaired 3'-DNA end and kinks the DNA to facilitate 5' cleavage specificity. Cleaves one nucleotide into the double-stranded DNA from the junction in flap DNA, leaving a nick for ligation. Also involved in the base excision repair (BER) pathway. Acts as a genome stabilization factor that prevents flaps from equilibrating into structurs that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA.
Belongs to the 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.
Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.
Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.
Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Belongs to the universal ribosomal protein uL30 family.
Belongs to the LeuD family. LeuD type 2 subfamily.
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Belongs to the V-ATPase V0D/AC39 subunit family.
Catalyzes the ATP-dependent phosphorylation of fructose-l-phosphate to fructose-l,6-bisphosphate. Involved in the utilization of fructose as a sole carbon and energy source.
Loss of growth on fructose. Growth on glucose is not affected.
Allosterically activated by GTP, when glutamine is the substrate; GTP has no effect on the reaction when ammonia is the substrate. The allosteric effector GTP functions by stabilizing the protein conformation that binds the tetrahedral intermediate(s) formed during glutamine hydrolysis. Inhibited by the product CTP, via allosteric rather than competitive inhibition.
CTPSs have evolved a hybrid strategy for distinguishing between UTP and CTP. The overlapping regions of the product feedback inhibitory and substrate sites recognize a common feature in both compounds, the triphosphate moiety. To differentiate isosteric substrate and product pyrimidine rings, an additional pocket far from the expected kinase/ligase catalytic site, specifically recognizes the cytosine and ribose portions of the product inhibitor.
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
Belongs to the metallophosphoesterase superfamily. YfcE family.
Belongs to the metallo-dependent hydrolases superfamily. HutI family.
Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway.
Cells lacking this gene are unable to grow on fructose. Growth on glucose is unaffected.
The EIIC type-2 domain forms the PTS system translocation channel and contains the specific substrate-binding site.
Belongs to the universal ribosomal protein uS11 family.
Located on the platform of the 30S subunit.
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 dTDP-4-dehydrorhamnose 3,5-epimerase family.
Epimerase involved in N-glycan biosynthetic pathway that takes place under low-salt conditions (1.75 M instead of 3.4 M). Participates in the formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg, consisting of a sulfated hexose, 2 hexoses and rhamnose. Involved in the addition of final rhamnose (sugar 4) of the tetrasaccharide on the dolichol phosphate carrier.
Belongs to the DeoC/FbaB aldolase family. ADHS subfamily.
Catalyzes a transaldol reaction between 6-deoxy-5-ketofructose 1-phosphate (DKFP) and L-aspartate semialdehyde (ASA) with an elimination of hydroxypyruvaldehyde phosphate to yield 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate (ADH). Plays a key role in an alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ), which is involved in the canonical pathway for the biosynthesis of aromatic amino acids.
Belongs to the aspartate/glutamate racemases family.
Binds to the 50S ribosomal subunit and prevents its association with the 30S ribosomal subunit to form the 70S initiation complex.
Belongs to the universal ribosomal protein uS17 family.
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family.
Belongs to the beta-RFA-P synthase family.
Catalyzes the condensation of 4-aminobenzoate (pABA) with 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to produce beta-ribofuranosylaminobenzene 5'-phosphate (beta-RFA-P).
Involved in the assembly of a N-linked pentasaccharide that decorates the S-layer glycoprotein and flagellins. Catalyzes the addition to the dolichol phosphate carrier of the hexuronic acid found at position 3 of the pentasaccharide.
Mutants contain only mono- and disaccharide-modified phosphodolichols and exhibit defective or limited motility.
Inhibited by EDTA and N-ethylmaleimide (NEM) in vitro.
Is optimally active at NaCl concentrations of 0.7-2 M, and displays little to no activity at low concentrations of salt (150 mM NaCl).
Metalloprotease that displays desampylase (DSAMP) activity, cleaving ubiquitin-like small archaeal modifier proteins (SAMP1, SAMP2 and SAMP3) from protein conjugates (isopeptide- and linear-linked). Thus, likely regulates sampylation and the pools of 'free' SAMP available for protein modification. Functions as a specific and not a general protease since it is unable to hydrolyze a variety of unmodified proteins otherwise hydrolyzed by proteinase K.
Belongs to the archaeal flagellin family.
Cells are non-motile. Cells lacking both flgA1 and flgA2 show defects in motility, whitout affecting surface adhesion ability.
Glycosylated by a pentasaccharide similar to the S-layer glycoprotein, probably comprising a hexose, 2 hexuronic acids, a methyl ester of a hexuronic acid and mannose. Glycosylation is required for biosynthesis of stable flagella.
Major flagellin required for motility. Not involved in PibD-dependent surface adhesion. Much more abundant in cells compared to FlgA2.
Tetramer of two alpha and two beta chains.
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Belongs to the eukaryotic ribosomal protein eL20 family.
Part of the 50S ribosomal subunit. Binds 23S rRNA.
Belongs to the auxin efflux carrier (TC 2.A.69) family.
Belongs to the cytochrome c oxidase subunit 3 family.
Belongs to the archaeal rpoM/eukaryotic RPA12/RPB9/RPC11 RNA polymerase family.
Belongs to the eukaryotic ribosomal protein eL15 family.
Belongs to the alpha-IPM synthase/homocitrate synthase family.
Probable RNase involved in rRNA stability through maturation and/or degradation of precursor rRNAs. Binds to RNA in loop regions with AU-rich sequences.
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.
Depletion of this protein leads to formation of large cells with a cragged cell surface, which are unable to establish a cell division plane.
Homodimer. Does not oligomerize. Interacts with FtsZ2.
Involved in cell division. Probably acts as a membrane anchor for FstZ2, tethering its filaments to the division site. May be involved in septum closure.
Belongs to the aldehyde dehydrogenase 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.
Belongs to the V-ATPase D subunit family.
Belongs to the universal ribosomal protein uS8 family.
One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit.
Belongs to the 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.
Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.
Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Belongs to the alkylbase DNA glycosidase AlkA family.
Belongs to the universal ribosomal protein uL5 family.
Part of the 50S ribosomal subunit; contacts the 5S rRNA and probably tRNA. Forms a bridge to the 30S subunit in the 70S ribosome.
This is 1 of the proteins that bind and probably mediate 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.
This is one of the proteins that bind and probably mediate 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.
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Binds 3 Mg(2+) cations per subunit. The strongest magnesium site (Mg1) is bound to the beta- and gamma-phosphates of ATP and four water molecules complete its coordination sphere.
Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. LysJ subfamily.
Binds 1 pyridoxal phosphate per subunit.
Belongs to the eukaryotic ribosomal protein eL24 family.
Part of the 50S ribosomal subunit. Forms a cluster with proteins L3 and L14.
Belongs to the eukaryotic RPB4 RNA polymerase subunit family.
DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit is less well bound than the others.
Part of the RNA polymerase complex. Forms a stalk with Rpo7 that extends from the main structure.
Belongs to the inorganic carbon transporter (TC 9.A.2) DabA family.
Part of an energy-coupled inorganic carbon pump.
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. Plasmid targeted by CRISPR locus P1 transform wild-type cells very poorly (PubMed:22767603).
Homodimer, forms a heterotetramer with a Cas2 homodimer.
Belongs to the archaeal Rpo6/eukaryotic RPB6 RNA polymerase subunit family.
Functions by promoting the formation of the first peptide bond.
Belongs to the fluoride channel Fluc/FEX (TC 1.A.43) family.
Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Na(+) is not transported, but it plays an essential structural role and its presence is essential for fluoride channel function.
Belongs to the eukaryotic ribosomal protein eL37 family.
Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Belongs to the archaeal NMN adenylyltransferase family.
Belongs to the AAA ATPase family. CDC48 subfamily.
Involved in the assembly of a N-linked pentasaccharide that decorates the S-layer glycoprotein and flagellins. Involved in the biosynthesis of the hexuronic acid found at position 3 of the pentasaccharide.
Part of an ABC transporter complex involved in glucose import.
The complex is composed of two ATP-binding proteins (TsgD13), two transmembrane proteins (TsgB13 and TsgC13) and a solute-binding protein (TsgA13).
Belongs to the TPP enzyme family. MenD subfamily.
Binds 1 thiamine pyrophosphate per subunit.
Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
Forms a heterotetramer with UvrA during the search for lesions. Interacts with UvrC in an incision complex.
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
The beta-hairpin motif is involved in DNA binding.
Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 2 subfamily.
Tetramer of two alpha and two beta subunits.
Belongs to the ABC transporter superfamily. Carbohydrate uptake transporter-1 (CUT1) (TC 3.A.1.1) family.
Part of the ABC transporter complex XacGHIJK involved in the uptake of xylose and arabinose (PubMed:31089701). Responsible for energy coupling to the transport system (Probable).
Belongs to the glutamate synthase family.
Belongs to the eukaryotic ribosomal protein eS6 family.
Belongs to the activator 1 small subunits family. RfcS subfamily.
Belongs to the eukaryotic RPB7/RPC8 RNA polymerase subunit family.
Forms 2 domains with an elongated structure; Rpo4 packs into the hinge region between the 2 domains.
Part of the RNA polymerase complex. Forms a stalk with Rpo4 that extends from the main structure.
Belongs to the tRNA-intron endonuclease family. Archaeal long subfamily.
Divalent cations; Ca(2+) better than Mg(2+).
Endonuclease that removes tRNA introns. Cleaves pre-tRNA at the 5' and 3' splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. Recognizes a pseudosymmetric substrate in which 2 bulged loops of 3 bases are separated by a stem of 4 bp.
Endonuclease that removes tRNA introns. Cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. Recognizes a pseudosymmetric substrate in which 2 bulged loops of 3 bases are separated by a stem of 4 bp.
Belongs to the 6-phosphogluconate dehydrogenase family.
Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NAD to NADH.
Belongs to the cytochrome c oxidase subunit 2 family.
Belongs to the CRISPR-associated exonuclease Cas4 family.
CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). This protein may be a 5' to 3' ssDNA exonuclease. Plasmid targeted by CRISPR locus P1 transform wild-type cells very poorly (PubMed:22767603).
Mg(2+) or Mn(2+) required for ssDNA cleavage activity. Can also utilise Cu(2+).
Belongs to the group II decarboxylase family. MfnA subfamily.
Catalyzes the decarboxylation of L-aspartate to produce beta-alanine.
Participates in transcription termination.
Belongs to the eukaryotic ribosomal protein eS27 family.
Belongs to the eukaryotic ribosomal protein eS4 family.
Belongs to the TtcA family. CTU1/NCS6/ATPBD3 subfamily.
Cells lacking this gene are nonthiolated at the wobble uridine position of tRNA(Lys). No effect on cell growth or yield at 42 degrees Celsius. Transferring the cells grown at 42 degrees Celsius to 50 degrees Celsius results in a slow-growth phenotype.
Interacts with monomeric and polymeric forms of SAMP2. Interacts with UbaA. Interacts with archaeal EF-1-alpha and Pan1. Non-sampylated protein forms a complex with archaeal CPSF1 of approximately 100 kDa.
Required for thiolation of mcm(5)S(2)U at the wobble uridine position of tRNA specific for lysine (tRNA(Lys)). Probably acts by catalyzing adenylation of tRNA, an intermediate required for 2-thiolation. May also act as a sulfurtransferase that transfers sulfur from thiocarboxylated SAMP2 onto the uridine of tRNA at wobble position. Required for cell growth at elevated temperatures.
Sampylated at Lys-204 with the archaeal ubiquitin-like protein SAMP2. Polymeric chains of SAMP2 are also linked.
Belongs to the archaeal SPP-like hydrolase family.
Catalyzes the dephosphorylation of 2-phosphoglycolate.
Belongs to the ABC transporter superfamily.
Mutant with a disruption within tsgB13 or tsgD13 cannot use glucose for nitrate respirative growth. However, the mutant can grow aerobically using glucose as the sole energy source.
Part of an ABC transporter complex involved in glucose import (Probable). Responsible for energy coupling to the transport system (By similarity).
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.
Was called L10e in this organism; in this case 'e' is for E.coli-like, not eukaryotic-type protein.
Belongs to the UbiA prenyltransferase family.
H.volcanii does not produce any known rhodopsins and unlike in H.salinarum, Lye is not regulated by bacterioopsin.
Involved in the biosynthesis of the acyclic C50 carotenoid bacterioruberin (BR) (PubMed:21840984). Acts as a bifunctional elongase/hydratase that catalyzes the elongation of lycopene by attaching a C(5) isoprene unit at C-2, as well as the hydroxylation of the previous end of the molecule (By similarity). The enzyme acts at both ends of the substrate, and catalyzes the conversion of lycopene to the C(45) intermediate dihydroisopentenyldehydrorhodopin (DH-IDR) and the conversion of isopentenyldehydrorhodopin (IDR) to the C(50) carotenoid dihydrobisanhydrobacterioruberin (DH-BABR) (By similarity). Can also catalyze the conversion of lycopene to tetrahydrobisanhydrobacterioruberin (TH-BABR) (By similarity).
Deletion of the gene affects the composition of the glycan N linked to the S-layer glycoprotein. Also affects the level of monosaccharide-modified dolichol phosphate. Mutants exhibit defective or limited motility.
Involved in the assembly of a N-linked pentasaccharide that decorates the S-layer glycoprotein and flagellins. Adds the first hexose subunit of the pentasaccharide to the dolichol phosphate carrier.
Belongs to the eukaryotic ribosomal protein eL32 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.
Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.
Belongs to the DNA mismatch repair MutL/HexB family.
This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex.
Belongs to the universal ribosomal protein uS2 family.
Belongs to the pseudouridine synthase Pus10 family.
Responsible for synthesis of pseudouridine from uracil-54 and uracil-55 in the psi GC loop of transfer RNAs.
Belongs to the HpcH/HpaI aldolase family.
Homotrimer and homohexamer in equilibrium.
Involved in the glyoxylate cycle which synthesizes precursors for carbohydrates from C2 compounds such as acetate. Catalyzes the Claisen condensation between acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form the malyl-CoA intermediate that is subsequently hydrolyzed to produce malate and CoA.
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.
Mutation within HVO_1886 or HVO_1887 causes nitrate respiration deficiency.
Part of an ABC transporter complex involved in anions import (Probable). Responsible for the translocation of the substrate across the membrane (By similarity).
Belongs to the archaeal phosphopantothenate synthetase family.
Catalyzes the condensation of (R)-4-phosphopantoate and beta-alanine to 4'-phosphopantothenate in the CoA biosynthesis pathway.
Belongs to the trans-sulfuration enzymes family.
Belongs to the eukaryotic RecA-like protein family. RadB subfamily.
Involved in DNA repair and in homologous recombination. May regulate the cleavage reactions of the branch-structured DNA. Has a very weak ATPase activity that is not stimulated by DNA. Binds DNA but does not promote DNA strands exchange.
Belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.
Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Belongs to the transferase hexapeptide repeat family.
Belongs to the autoinducer-2 exporter (AI-2E) (TC 2.A.86) family.
Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.
Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate.
There are 2 substrate-binding sites: the catalytic A site, and the non-catalytic B site that may play a role in the transfer of substrate or product between the active site and the solvent. Alternatively, the B site may bind allosteric effectors.
Although this enzyme belongs to the family of MTA phosphorylases based on sequence homology, it lacks several conserved amino acids in the substrate binding pocket that confer specificity towards MTA.
Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.
Purine nucleoside phosphorylase involved in purine salvage.
Belongs to the adenosylhomocysteinase family.
May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine.
Belongs to the class II fructose-bisphosphate aldolase family.
Binds 2 Zn(2+) ions per subunit. One is catalytic and the other provides a structural contribution.
Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis. Is required for the utilization of fructose as a sole carbon and energy source. Plays a role in gluconeogenesis during growth on acetate, D-xylose, and casamino acids.
EDTA is an inhibitor of catalytic activity.
Loss of growth on fructose, but growth on glucose is slightly stimulated. Loss of growth on acetate, D-xylose, or Casamino acids.
Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.
Probably part of an ABC transporter complex. Responsible for energy coupling to the transport system.
Belongs to the eukaryotic ribosomal protein eS19 family.
May be involved in maturation of the 30S ribosomal subunit.
Belongs to the eukaryotic/archaeal PrmC-related family.
The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Belongs to the NAD(P)-dependent epimerase/dehydratase family. dTDP-glucose dehydratase subfamily.
Lyase involved in N-glycan biosynthetic pathway that takes place under low-salt conditions (1.75 M instead of 3.4 M). Participates in the formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg, consisting of a sulfated hexose, 2 hexoses and rhamnose. Involved in the addition of final rhamnose (sugar 4) of the tetrasaccharide on the dolichol phosphate carrier.
Deletion mutant shows no growth phenotype under standard conditions, temperature stress or salt stress.
RNA-free RNase P that catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus.
The ease to obtain knockout of this gene and the lack of growth phenotypes upon gene deletion suggests that archaeal HARPs do not make a major contribution to global tRNA 5'-end maturation in archaea, but may well exert a specialised, yet unknown function in (t)RNA metabolism.
Belongs to the eukaryotic RecA-like protein family.
Decreased growth rate, loss of homologous recombination, increased sensitivity to DNA damaging agents such as UV light and ethylmethane sulfonate (EMS). Loss of maintenance and/or replication of pHH1 and pHV2 (but not pHK2) replicon-containing plasmids.
Involved in DNA repair and in homologous recombination. Binds and assemble on single-stranded DNA to form a nucleoprotein filament. Hydrolyzes ATP in a ssDNA-dependent manner and promotes DNA strand exchange between homologous DNA molecules.
Involved in DNA repair and in homologous recombination. Binds and assembles on single-stranded DNA to form a nucleoprotein filament. Hydrolyzes ATP in a ssDNA-dependent manner and promotes DNA strand exchange between homologous DNA molecules (Probable). In addition to its role in homologous recombination plays a critical role in maintenance and/or replication of some plasmids, but not in plasmid transformation.
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.
Belongs to the acetolactate synthase small subunit family.
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 (By similarity). Required for division ring constriction (PubMed:33903747).
Homodimer. Polymerizes to form a dynamic ring structure in a strictly GTP-dependent manner. Interacts directly with several other division proteins (By similarity). Interacts with SepF (PubMed:34103513).
Viable, but have fewer colony-forming units compared to wild-type. Cells are very heterogeneously sized and misshapen, and have a notable amount of cellular debris. Loss of cell division. No effect on Z1 ring formation. FtsZ1/FtsZ2 double deletion mutant cells show various division defects, including fragmentation, budding, polar tubulation and fission resulting in DNA-containing particles, which are able to remain viable and propagate without regular cell division.
Aminocarboxypropyltransferase that catalyzes the aminocarboxypropyl transfer on pseudouridine corresponding to position 914 in M.jannaschii 16S rRNA. It constitutes the last step in biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi).
Belongs to the TDD superfamily. TSR3 family.
Belongs to the eIF-2B alpha/beta/delta subunits family. R15P isomerase subfamily.
Catalyzes the isomerization of ribose 1,5-bisphosphate (R15P) to ribulose 1,5-bisphosphate (RuBP), the CO(2) acceptor and substrate for RubisCO. Functions in an archaeal AMP degradation pathway, together with AMP phosphorylase and RubisCO.
Reaction proceeds via a cis-phosphoenolate intermediate.
Belongs to the eIF-2B alpha/beta/delta subunits family.
Belongs to the methylmalonyl-CoA epimerase family.
Interacts with UvrB in an incision complex.
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
Belongs to the dihydrofolate reductase family.
Deletion of the gene does not affect growth on glucose or galactose. Double deletion mutant kdgK1/kdgK2 loses the ability to grow on galactose.
Involved in galactose catabolism. Catalyzes the phosphorylation of 2-keto-3-deoxygalactonate (KDGal) to produce 2-keto-3-deoxy-6-phosphogalactonate (KDPGal). Can also phosphorylate 2-keto-3-deoxygluconate (KDG) to 2-keto-3-deoxy-6-phosphogluconate (KDPG), but the catalytic efficiency for KDGal is 50-fold higher than for KDG.
Belongs to the flavin oxidoreductase frp family.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family.
Belongs to the nucleobase:cation symporter-2 (NCS2) (TC 2.A.40) family.
In the C-terminal section; belongs to the transferase hexapeptide repeat family.
In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family.
Belongs to the 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). Plasmid targeted by CRISPR locus P1 transform wild-type cells very poorly (PubMed:22767603). This protein processes pre-crRNA into individual crRNA units, in vivo at least Cas5 and Cas7 are also required for optimal crRNA processing and/or stability (PubMed:24459147).
Expressed in exponential and stationary phases.
Loss of the 8 Cas genes in this locus (cas1, cas2, cas3, cas4, cas5, cas6, cas7 and cas8b) leads to loss of CRISPR interference against plasmid targeted by this CRISPR locus, i.e. plasmid is not destroyed by CRISPR (PubMed:22767603). Upon disruption of only this gene, no visible phenotype when grown under differing temperature and salt regimes. Does not produce mature length crRNA. Can be complemented by endogenous Cas6, but not by Cas6 from halophilic archaea H.lacusprofundi, or non-halophilic archaea M. maripaludis or M. mazei. Loss of CRISPR interference against plasmid targeted by this CRISPR locus, i.e. plasmid is not destroyed by CRISPR action (PubMed:24459147).
Belongs to the universal ribosomal protein uL15 family.
Heterotrimer composed of an alpha, a beta and a gamma chain.
eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA.
Belongs to the SIMIBI class G3E GTPase family. UreG subfamily.
Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG.
Homodimer. UreD, UreF and UreG form a complex that acts as a GTP-hydrolysis-dependent molecular chaperone, activating the urease apoprotein by helping to assemble the nickel containing metallocenter of UreC. The UreE protein probably delivers the nickel.
Belongs to the vitamin uptake transporter (VUT/ECF) (TC 2.A.88) family. Q precursor transporter subfamily.
Involved in the import of queuosine (Q) precursors, required for Q precursor salvage.
Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
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.
Alpha-ketoglutarate semialdehyde dehydrogenase involved in the degradation of D-xylose, a major component of hemicelluloses such as xylan. Catalyzes the fifth reaction in the xylose utilization pathway through dehydratation of alpha-ketoglutarate semialdehyde (2,5-dioxopentanoate) into alpha-ketoglutarate.
Impairs growth on D-xylose as sole energy and carbon substrate.
Transcriptionally up-regulated by both L-arabinose and D-xylose via the pentose-specific regulator XacR (PubMed:25141768, PubMed:19584053). Expression is repressed by glucose (PubMed:19584053).
Belongs to the aconitase/IPM isomerase family. LeuC type 1 subfamily.
Catalyzes the attachment of tryptophan to tRNA(Trp).
Belongs to the metallo-dependent hydrolases superfamily. DHOase family. Class I DHOase subfamily.
Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Belongs to the DNA mismatch repair MutS family.
This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity.
Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. In the second step the latter compound is decarboxylated to form 4'-phosphopantotheine.
In the C-terminal section; belongs to the PPC synthetase family.
In the N-terminal section; belongs to the HFCD (homo-oligomeric flavin containing Cys decarboxylase) superfamily.
Belongs to the 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 GTP-binding SRP family. SRP54 subfamily.
Cannot be disrupted, it is thus essential.
Composed of three domains: the N-terminal N domain, which is responsible for interactions with the ribosome, the central G domain, which binds GTP, and the C-terminal M domain, which binds the RNA and the signal sequence of the RNC.
Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY.
Part of the signal recognition particle protein translocation system, which is composed of SRP and FtsY. Archaeal SRP consists of a 7S RNA molecule of 300 nucleotides and two protein subunits: SRP54 and SRP19.
Belongs to the OMP decarboxylase family. Type 2 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.
Belongs to the disproportionating enzyme 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). Plasmid targeted by CRISPR locus P1 transform wild-type cells very poorly (PubMed:22767603). This protein helps process or stabilize pre-crRNA into individual crRNA units, in vivo Cas5 and Cas6 are also required for optimal crRNA processing and/or stability (PubMed:24459147).
NADP-dependent D-xylose dehydrogenase involved in the degradation of D-xylose, a major component of hemicelluloses such as xylan. Catalyzes the initial reaction in the xylose utilization pathway by oxydizing D-xylose into D-xylonolactone.
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 glycosyl hydrolase 4 family.
Does not affect growth on D-xylose as sole energy and carbon substrate.
Expression is highly induced during growth on D-xylose.
NADP-dependent D-xylose dehydrogenase involved in the degradation of D-xylose, a major component of hemicelluloses such as xylan. Even if it shows D-xylose dehydrogenase activity, it is not essential for D-xylose degradation.
Belongs to the metallo-dependent hydrolases superfamily. Adenine deaminase family.
Interacts with chemotaxis (Che) proteins as well as flagella accessory (Fla) proteins.
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 isochorismate synthase family.
Belongs to the archaeal Rpo3/eukaryotic RPB3 RNA polymerase subunit family.
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.
Belongs to the quinolinate synthase family. Type 3 subfamily.
Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.
Comprises of two domains. The C-terminal domain contains the binding site for glutamine and catalyzes the hydrolysis of this substrate to glutamate and ammonia. The N-terminal domain is anticipated to bind ATP and cobyrinate and catalyzes the ultimate synthesis of the diamide product. The ammonia produced via the glutaminase domain is probably translocated to the adjacent domain via a molecular tunnel, where it reacts with an activated intermediate.
The a and c carboxylates of cobyrinate are activated for nucleophilic attack via formation of a phosphorylated intermediate by ATP. CbiA catalyzes first the amidation of the c-carboxylate, and then that of the a-carboxylate.
In the C-terminal section; belongs to the transposase 35 family.
Flagellin that plays both structural and regulatory roles in flagella biosynthesis. Does not constitute a major flagellin in terms of abundance contrary to FlgA1: may regulate the flagella-dependent swimming motility depending on the relative abundance of FlgA1. Not involved in PibD-dependent surface adhesion.
Glycosylated by a pentasaccharide similar to the S-layer glycoprotein, probably comprising a hexose, 2 hexuronic acids, a methyl ester of a hexuronic acid and mannose.
Straight flagella, mainly at the poles (PubMed:10632878). Cells lacking flgA2 but not flgA1 are hypermotile, display an increased number of flagella per cell, as well as an increased flagellum length (PubMed:23989184). Cells lacking both flgA1 and flgA2 show defects in motility, whitout affecting surface adhesion ability (PubMed:20363933).
Belongs to the nucleobase:cation symporter-2 (NCS2) (TC 2.A.40) family. Azg-like subfamily.
Belongs to the type II topoisomerase GyrB family.
Binds two Mg(2+) per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn(2+) or Ca(2+).
Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.
Belongs to the PINc/VapC protein family.
Toxic component of a toxin-antitoxin (TA) system. An RNase.
Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily.
Belongs to the thiolase-like superfamily. Thiolase family.
Belongs to the eukaryotic ribosomal protein eL18 family.
Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
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 class-I pyridine nucleotide-disulfide oxidoreductase family.
The active site is a redox-active disulfide bond.
Belongs to the aconitase/IPM isomerase family.
Belongs to the argininosuccinate synthase family. Type 1 subfamily.
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.
Hexosyltransferase involved in N-glycan biosynthetic pathway that takes place under low-salt conditions (1.75 M instead of 3.4 M). Participates in the formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg, consisting of a sulfated hexose, 2 hexoses and rhamnose. Involved in the addition of final rhamnose (sugar 4) of the tetrasaccharide on the dolichol phosphate carrier.
Belongs to the NucS endonuclease family.
Cleaves both 3' and 5' ssDNA extremities of branched DNA structures.
Belongs to the thymidylate synthase family. Bacterial-type ThyA subfamily.
Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
Binds 2 divalent metal cations per subunit. Magnesium or manganese.
Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
Belongs to the Mg-chelatase subunits D/I family.
Belongs to the archaeal DNA polymerase II family.
Heterodimer of a large subunit and a small subunit.
Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase.
Belongs to the chorismate synthase family.
Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
Belongs to the type-I 3-dehydroquinase family.
Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.
Belongs to the DNA polymerase delta/II small subunit family.
Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3' to 5' direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase.
Belongs to the glycosyl hydrolase 51 family.
Belongs to the universal ribosomal protein uL24 family.
Located at the polypeptide exit tunnel on the outside of the subunit.
One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
Belongs to the N(4)/N(6)-methyltransferase family. N(4) subfamily.
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
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 methylamine corrinoid protein family.
Belongs to the pseudouridine synthase TruD family.
Could be responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
Part of an ABC transporter complex involved in anions import (Probable). Responsible for energy coupling to the transport system (By similarity).
Component of the Sec protein translocase complex. Heterotrimer consisting of alpha (SecY), beta (SecG) and gamma (SecE) subunits. The heterotrimers can form oligomers, although 1 heterotrimer is thought to be able to translocate proteins. Interacts with the ribosome. May interact with SecDF, and other proteins may be involved.
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Belongs to the AB hydrolase superfamily. MetX family.
Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
Mutation causes nitrate respiration deficiency.
Part of an ABC transporter complex involved in molybdenum import (Probable). Responsible for the translocation of the substrate across the membrane.
Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+).
Phosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP to their respective diphosphate derivatives. Probably excludes non-canonical purines from DNA/RNA precursor pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
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).
ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPase-20S proteasome association which triggers gate opening, and supports translocation of unfolded substrates.
Consists of three main regions, an N-terminal coiled-coil domain that may assist in substrate recognition, an interdomain involved in PAN hexamerization, and a C-terminal ATPase domain of the AAA type.
Homohexamer. The hexameric complex has a two-ring architecture resembling a top hat that caps the 20S proteasome core at one or both ends. Upon ATP-binding, the C-terminus of PAN interacts with the alpha-rings of the proteasome core by binding to the intersubunit pockets.
Strains lacking panB gene alone display relatively normal growth rate and overall cell yield. Moreover, strains lackings both panA and panB still show robust growth, demonstrating that the PAN proteins are not essential.
Up-regulated at mRNA and protein levels during transition from exponential to stationary phase.
Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 3 subfamily.
Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Belongs to the universal ribosomal protein uL2 family.
One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome.
Part of the 50S ribosomal subunit. Forms a bridge to the 30S subunit in the 70S ribosome.
Belongs to the phosphoglycerate kinase family.
Belongs to the BPG-independent phosphoglycerate mutase family.
Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
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 or homodecamer. In contrast to form I RuBisCO, the form III RuBisCO is composed solely of large subunits.
Belongs to the methyltransferase superfamily. TrmY family.
Deletion leads to the absence of 1-methylpseudouridine at position 54 of tRNA, but does not lead to any obvious phenotype.
Specifically catalyzes the N1-methylation of pseudouridine at position 54 (Psi54) in tRNAs.
Belongs to the archaeal Rpo11/eukaryotic RPB11/RPC19 RNA polymerase subunit family.
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.
Monomer. Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ and 2 PurS subunits.
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. Some bacteria have evolved a zinc-coordinating structure that stabilizes the LID domain.
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.
Binds 2 divalent metal cations per subunit. The ions could be magnesium and/or manganese.
Catalyzes the GTP-dependent successive addition of two or more gamma-linked L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form coenzyme F420-0-glutamyl-glutamate (F420-2) or polyglutamated F420 derivatives.
Monovalent cation. The ion could be potassium.
Abolishes formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg. No effect on 'Asn-47' and 'Asn-117' glycosylation of S-layer glycoprotein Csg.
Hexosyltransferase involved in N-glycan biosynthetic pathway that takes place under low-salt conditions (1.75 M instead of 3.4 M). Participates in the formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg, consisting of a sulfated hexose, 2 hexoses and rhamnose. Together with Agl5, mediates the addition of sugars 1 and 2 to dolichol phosphate in the tetrasaccharide.
Belongs to the heat shock protein 70 family.
Belongs to the eukaryotic ribosomal protein eL8 family.
Multifunctional RNA-binding protein that recognizes the K-turn motif in ribosomal RNA, the RNA component of RNase P, box H/ACA, box C/D and box C'/D' sRNAs.
Part of the 50S ribosomal subunit. Probably part of the RNase P complex.
Belongs to the 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.
Probable 2-keto-3-deoxyxylonate dehydratase involved in the degradation of D-xylose, a major component of hemicelluloses such as xylan. Catalyzes the fourth reaction in the xylose utilization pathway through dehydratation of 2-dehydro-3-deoxy-D-xylonate into alpha-ketoglutarate semialdehyde (2,5-dioxopentanoate).
A double secD and secF deletion grows very poorly on solid medium at 45 degrees Celsius, confers a severe cold-sensitive growth phenotype (30 degrees Celsius), as well as having defects in Sec-dependent protein translocation. Has no effects on Sec-independent Tat substrate protein export.
Belongs to the SecD/SecF family. SecF subfamily.
Part of the protein translocation apparatus. Forms a complex with SecD.
Part of the protein translocation apparatus. Forms complexes with SecD.
Belongs to the enoyl-CoA hydratase/isomerase family. MenB subfamily.
Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA).
The glycine cleavage system catalyzes the degradation of glycine.
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 histidinol dehydrogenase family.
Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
Belongs to the glutamate 5-kinase family.
Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
Belongs to the RNA polymerase beta chain family.
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Belongs to the eukaryotic-type primase large subunit family.
Heterodimer of a small subunit (PriS) and a large subunit (PriL).
Regulatory subunit of DNA primase, an RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Stabilizes and modulates the activity of the small subunit, increasing the rate of DNA synthesis, and conferring RNA synthesis capability. The DNA polymerase activity may enable DNA primase to also catalyze primer extension after primer synthesis. May also play a role in DNA repair.
Belongs to the DNA2/NAM7 helicase family.
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 GatB/GatE family. GatE subfamily.
Component of the protein translocase complex. Heterotrimer consisting of alpha (SecY), beta (SecG) and gamma (SecE) subunits. Can form oligomers of the heterotrimer.
Involved in protein export. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
Belongs to the 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.
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.
Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
Binds 4 Mg(2+) or Mn(2+) ions per subunit.
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 truncated hemoglobin family. Group I subfamily.
Belongs to the eukaryotic-type primase small subunit family.
Catalytic subunit of DNA primase, an RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. The small subunit contains the primase catalytic core and has DNA synthesis activity on its own. Binding to the large subunit stabilizes and modulates the activity, increasing the rate of DNA synthesis while decreasing the length of the DNA fragments, and conferring RNA synthesis capability. The DNA polymerase activity may enable DNA primase to also catalyze primer extension after primer synthesis. May also play a role in DNA repair.
RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
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.
In the C-terminal section; belongs to the PEP-utilizing enzyme family.
Belongs to the GHMP kinase family. PoK subfamily.
Phosphorylates (R)-pantoate to form (R)-4-phosphopantoate in the CoA biosynthesis pathway.
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).
Belongs to the amidase family. GatA subfamily.
Belongs to the aconitase/IPM isomerase family. LeuC type 2 subfamily.
Belongs to the GTP cyclohydrolase IV family.
Cells lacking this gene are auxotrophic for thymidine (dT) and hypoxanthine (PubMed:19478918). tRNAs of the mutants lack archaeosine (G(+)) (PubMed:18931107, PubMed:19478918). A slight growth defect is seen in mutants grown at 45 degrees Celsius in Hv-YPC (yeast-peptone-casamino acids) medium supplemented with dT (PubMed:18931107). Absence of pantothenate from the growth medium of the mutant cells results in a slow-growing phenotype (PubMed:19478918).
Converts GTP to 7,8-dihydro-D-neopterin 2',3'-cyclic phosphate, the first intermediate in the biosynthesis of coenzyme methanopterin (By similarity). Involved in archaeosine (G(+)) and folate biosynthesis (PubMed:18931107, PubMed:19478918).
Belongs to the Orn/Lys/Arg decarboxylase class-II family. LysA subfamily.
Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine.
Belongs to the universal ribosomal protein uL1 family.
Binds directly to 23S rRNA. Probably involved in E site tRNA release.
Probably involved in E site tRNA release (By similarity). Binds directly to 23S rRNA.
Protein L1 is also a translational repressor protein, it controls the translation of its operon by binding to its mRNA.
Belongs to the GHMP kinase family. Archaeal shikimate kinase subfamily.
Belongs to the peptidase M20A family. LysK subfamily.
Binds 2 Zn(2+) or Co(2+) ions per subunit.
Catalyzes the release of L-lysine from [LysW]-gamma-L-lysine and the release of L-ornithine from [LysW]-L-ornithine.
Cells lacking this gene lose the ability to grow on L-arabinose but not on D-xylose.
L-AraDH initiates the degradation of L-arabinose. Catalyzes the NAD(P)(+)-dependent conversion of L-arabinose to L-arabino-gamma-lactone. It is highly specific for L-arabinose as substrate and can use both NADP(+) and NAD(+) as electron acceptor, with a slight preference for NADP(+).
Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)-oxygenase family.
Belongs to the universal ribosomal protein uL22 family.
The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.
This protein binds specifically to 23S rRNA. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.
Impaired formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg with formation of a tetrasaccharide that is not sulfated. No effect on 'Asn-47' and 'Asn-117' glycosylation of S-layer glycoprotein Csg.
Involved in N-glycan biosynthetic pathway that takes place under low-salt conditions (1.75 M instead of 3.4 M). Participates in the formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg, consisting of a sulfated hexose, 2 hexoses and rhamnose. Mediates sulfation of sugar 1 in the tetrasaccharide.
Involved in the assembly of a N-linked pentasaccharide that decorates the S-layer glycoprotein and flagellins. Catalyzes the addition of the mannose found at position 5 of the pentasaccharide to its own distinct dolichol phosphate carrier.
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 methylthiotransferase family. CDKAL1 subfamily.
Binds 1 or 2 [4Fe-4S] cluster. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Catalyzes the methylthiolation of N6-threonylcarbamoyladenosine (t(6)A), leading to the formation of 2-methylthio-N6-threonylcarbamoyladenosine (ms(2)t(6)A) at position 37 in tRNAs that read codons beginning with adenine.
Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin.
Belongs to the universal ribosomal protein uS19 family.
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
Belongs to the 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 zinc-containing alcohol dehydrogenase family. Glucose 1-dehydrogenase subfamily.
Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to D-gluconate via gluconolactone. Can utilize both NAD(+) and NADP(+) as electron acceptor. Is involved in the degradation of glucose through a modified Entner-Doudoroff pathway.
Belongs to the purine/pyrimidine phosphoribosyltransferase family.
Does not require uracil for growth, is partially resistant to 5-FOA (5-fluoroorotic acid).
May have some orotate phosphoribosyltransferase activity, but not enough to ensure growth in the absence of the physiological OPRT.
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 2H phosphoesterase superfamily. ThpR family.
Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
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 triosephosphate isomerase family.
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Belongs to the BlaI transcriptional regulatory family.
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.
By anaerobical conditions and dimethyl sulfoxide (DMSO).
Cells lacking this gene have no dimethyl sulfoxide (DMSO) reductase activity under aerobic, anaerobic without substrate, anaerobic with DMSO as substrate nor under anaerobic with nitrate as substrate conditions. Cells are not able to grow anaerobically by dimethyl sulfoxide (DMSO) respiration. DMSO does not activate transcription of the dmsEABCD genes induced by the anaerobic conditions. No effect on aerobical growth or growth under denitrifying conditions.
Involved in activating dmsEABCD gene expression related to dimethyl sulfoxide (DMSO) reductase. Required for anaerobic respiration on dimethyl sulfoxide (DMSO).
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.
A unique feature of H.volcanii PPA (HvPPA) is its high tolerance to organic solvents, with little if any enzyme inactivation after 2 hours of incubation in buffers supplemented with 50% (vol/vol) dimethyl sulfoxide (DMSO), dimethylformamide (DMF), ethanol, or methanol. The catalytic activity of HvPPA is also found to be robust when assayed in organic solvents. Moreover, HvPPA is fully active over a wide range of salt concentrations.
Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions (By similarity) (PubMed:26546423). The hydrolysis of PPi by inorganic pyrophosphatase releases a considerable amount of energy that can drive unfavorable biochemical transformations to completion (Probable). Is not active on nucleoside triphosphates (ATP, TTP, GTP, or CTP) or nucleoside diphosphate (ADP) (PubMed:26546423).
Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
Homohexamer (By similarity) (PubMed:26546423). Also forms homotrimers, but the trimeric form is 23% less active than the hexamer. In fact, likely forms a dimer of trimers (PubMed:26546423).
Inhibited by sodium fluoride (NaF) in vitro, similarly to other class A type inorganic pyrophosphatases.
Inorganic pyrophosphatases are used in a wide variety of biotechnology applications based on the ability of these enzymes to drive reactions forward and generate an easily assayed product. Since HvPPA displays robust activity under high-salt conditions and in organic solvents, it could be a valuable tool for use in bioindustry.
The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Belongs to the ketopantoate reductase family.
Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
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 four-carbon acid sugar kinase family.
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 (By similarity). Has a role that partially overlaps that of Hef endonuclease; double deletions cannot be constructed. In the presence of site-directed mutations that (probably) abolish Hef helicase or nuclease activity, a hjc deletion cannot be constructed.
Belongs to the Holliday junction resolvase Hjc family.
No alteration in sensitivity to UV light, slow growth on mitomycin C. No effect on homologous recombination; double hef/hjc deletion mutants cannot be constructed (synthetic lethality), suggesting the enzymes play overlapping roles.
Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
Belongs to the glutamate--cysteine ligase type 2 family. YbdK subfamily.
Catalyzes the synthesis of gamma-glutamylcysteine (gamma-GC), the main low-molecular-weight thiol compound instead of glutathione in halophilic archaea.
Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor.
Belongs to the archaeal dihydroneopterin aldolase family.
Catalyzes the conversion of 7,8-dihydroneopterin (H2Neo) to 6-hydroxymethyl-7,8-dihydropterin (6-HMD).
Belongs to the SAICAR synthetase 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.
Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP.
Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
Belongs to the thiolase-like superfamily. HMG-CoA synthase family.
Catalyzes the condensation of acetyl-CoA with acetoacetyl-CoA to form 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA). 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.
In contrast to bacterial and eukaryotic HMG-CoA synthases, is insensitive to feedback substrate inhibition by acetoacetyl-CoA. Enzymatic activity is inhibited by hymeglusin, which also blocks the propagation of H.volcanii cells in vivo, indicating the critical role that the mevalonate pathway plays in isoprenoid biosynthesis by these archaea.
Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal beta chain is a regulatory subunit.
Involved in the catabolism of quinolinic acid (QA).
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. Can fully reduce the unsaturated isoprenoid side chains of membrane phospholipids and glycolipids. Is also able to reduce the omega-position isoprene of dolichol phosphate.
Reduced pigmentation of cell colonies and lack of fully reduced isoprene chains of membrane phospholipids and glycolipids.
Belongs to the beta-eliminating lyase family.
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.
Belongs to the eukaryotic release factor 1 family.
Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA.
Heterodimer of two subunits, one of which binds GTP.
Belongs to the 4-toluene sulfonate uptake permease (TSUP) (TC 2.A.102) family.
Cells lacking this gene are deficient in sampylation, i.e. SAMP-protein conjugates. Moreover, they do not grow anaerobically with DMSO and do not show DMSO reductase activity, but their growth in the presence of oxygen is not affected; however, they are retarded in aerobic growth at 50 degrees Celsius. The lysine tRNAs of the mutant strain appear to be nonthiolated.
Likely activates multiple ubiquitin-like SAMPs for protein conjugation as well as for sulfur transfer, via ATP-dependent adenylation at their C-terminus (PubMed:21368171, PubMed:24097257, PubMed:24906001). In fact, it is required for the formation of all three SAMP1-, SAMP2- and SAMP3-protein conjugates, and for molybdenum cofactor (MoCo) biosynthesis and thiolation of tRNAs (PubMed:21368171, PubMed:24097257).
Sampylated at Lys-113 with the archaeal ubiquitin-like protein SAMP2. Also sampylated with SAMP1.
Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
DNA repair enzyme involved in the repair of deaminated bases. Selectively cleaves double-stranded DNA at the second phosphodiester bond 3' to a deoxyinosine leaving behind the intact lesion on the nicked DNA.
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.
Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.
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.
No effect on cell growth, membrane protein insertion, protein secretion, or ribosome levels.
Belongs to the threonine aldolase family.
Belongs to the cytidylate kinase family. Type 2 subfamily.
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
Belongs to the 2Fe2S plant-type ferredoxin family.
Belongs to the protein kinase superfamily. RIO-type Ser/Thr kinase family.
Serine/threonine-protein kinase that is able to autophosphorylate as well as to phosphorylate proteasome subunit alpha 1 (PsmA1) in vitro (PubMed:20671954). Despite the protein kinase domain is proposed to act predominantly as an ATPase (By similarity).
ATPase activity is inhibited by EDTA 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-terminus of the proteasomal ATPase functions 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 (Probable). Is also able to cleave other nucleoside triphosphates including GTP and TTP, but the rate of hydrolysis is 4- to 5-fold slower than for ATP.
Homododecamer, in a proposed two stacked hexameric ring configuration, but may also form homohexamer. The hexameric complex has likely a two-ring architecture resembling a top hat that caps the 20S proteasome core at one or both ends. Upon ATP-binding, the C-terminus of PAN probably interacts with the alpha-rings of the proteasome core by binding to the intersubunit pockets. Interacts with SAMP1-MoaE conjugate in vitro, but does not bind to SAMP1 or MoaE alone (PubMed:24343376). Interacts with NcsA (PubMed:24906001).
Strains lacking panA gene alone display relatively normal growth rate and overall cell yield, but they are more sensitive to growth on organic versus inorganic nitrogen sources and hypo-osmotic stress, they show limited growth in the presence of L-canavanine and display enhanced thermotolerance. Moreover, strains lackings both panA and panB still show robust growth, demonstrating that the PAN proteins are not essential.
The biochemical properties of PAN 1 are highly dependent on molar concentrations of salt with a significant loss of ATPase activity and complex dissociation detected at 0.75 M NaCl.
Up-regulated at the mRNA level during transition from exponential to stationary phase. However, at the protein level, PanA is expressed at a high and relatively constant level throughout growth.
Might regulate the synthesis and function of enzymes involved in later enzymatic steps of Krebs cycle.
When expressed in E.coli, CitZ is produced in a soluble but inactive form that can be reactivated by incubating with 2 M KCl (PubMed:10397837). Citrate synthase is found in nearly all cells capable of oxidative metabolism.
Belongs to the imidazoleglycerol-phosphate dehydratase family.
By glycerol. Not subjected to glucose catabolite repression.
Incapable of growth on glycerol. Causes a reduction in growth on dihydroxyacetone.
Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone (DHA). Involved, together with the DHA kinase DhaKLM, in the metabolism of DHA.
Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 2 subfamily.
Belongs to the universal ribosomal protein uS9 family.
Cells lacking this gene grow as the wild-type in complex medium and in synthetic medium with glucose as sole carbon and energy source, but the mutant cells are not capable of swarming and have severe defects in forming biofilms.
Zinc-binding protein. Binds 1 zinc ion. Required for swarming. Involved in biofilm formation.
Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
Belongs to the IPP isomerase type 1 family.
Catalyzes the conversion of urocanate to 4-imidazolone-5-propionate.
Plays a role in the regulation of phosphate uptake.
Catalyzes the hydrolysis of methenyl-H(4)MPT(+) to 5-formyl-H(4)MPT.
Up-regulated at the mRNA level during transition from exponential to stationary phase. However, at the protein level, PsmB is expressed at a high and relatively constant level throughout growth.
Belongs to the archaeosine synthase type 1 family.
Cells lacking this gene lack archaeosine in tRNA and accumulate preQ0-modified tRNA.
Is responsible for the final step in the biosynthesis of archaeosine, a modified nucleoside present in the dihydrouridine loop (D-loop) of archaeal tRNA. Catalyzes the conversion of 7-cyano-7-deazaguanine (preQ0)-modified tRNA to archaeosine-tRNA, transforming a nitrile group to a formamidine group.
Belongs to the archaeal DnaG primase family.
Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.
RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteropolymeric, adenine-rich transcripts and the exosome.
Belongs to the methyltransferase superfamily. Archaeal-type CbiT family.
Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.
Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The H.volcanii alpha1-beta-alpha2 proteasome is able to cleave oligopeptides after Tyr and thus displays chymotrypsin-like activity.
Strains lacking psmA2 gene alone display relatively normal growth rate and overall cell yield. However, depletion of psmA1 and psmA2 together renders the cells inviable.
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.
Cells lacking this gene do not grow anaerobically with DMSO and do not show DMSO reductase activity, but their growth in the presence of oxygen and at 50 degrees Celsius is not affected. SAMP2 and SAMP3 cannot complement the samp1 mutation. tRNA thiolation is not affected.
Functions as a protein modifier covalently attached to lysine residues of substrate proteins, as well as a sulfur carrier in molybdenum cofactor (MoCo) biosynthesis. The protein modification process is termed sampylation and involves the formation of an isopeptide bond between the SAMP1 C-terminal glycine carboxylate and the epsilon-amino group of lysine residues on target proteins. May serve as a proteolytic signal in the cell to target proteins for degradation by proteasomes.
Belongs to the eukaryotic/archaeal RNase P protein component 2 family.
Component of the dihydroxyacetone kinase complex, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent reaction, and a phosphorelay system on histidine residues finally leads to phosphoryl transfer to DhaL and dihydroxyacetone.
Belongs to the universal ribosomal protein uL29 family.
Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
Belongs to the NAD-dependent DNA ligase family. LigA subfamily.
DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
Deletion of both ligA and ligN is lethal.
Displays maximal in vitro activity at high salt levels.
NADP-dependent D-xylose dehydrogenase involved in the degradation of D-xylose, a major component of hemicelluloses such as xylan. Catalyzes the third reaction in the xylose utilization pathway through dehydratation of D-xylonate into 2-dehydro-3-deoxy-D-xylonate.
Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 3 subfamily.
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro).
Consists of three domains: the N-terminal catalytic domain, the anticodon-binding domain and the C-terminal extension.
Belongs to the 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 GHMP kinase family. Homoserine kinase subfamily.
Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with geranylgeranyl diphosphate (GGPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30E,34E,38E)-undecaprenyl diphosphate (tritrans,heptacis-UPP). It is probably the precursor of glycosyl carrier lipids.
Belongs to the universal ribosomal protein uL13 family.
This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.
Belongs to the CRISPR-associated endoribonuclease Cas2 protein family.
CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease. Involved in the integration of spacer DNA into the CRISPR cassette. Plasmid targeted by CRISPR locus P1 transform wild-type cells very poorly (PubMed:22767603).
Homodimer, forms a heterotetramer with a Cas1 homodimer.
Contains two rhodanese domains with different primary structures but with near identical secondary structure conformations suggesting a common evolutionary origin. Only the C-terminal rhodanese domain contains the catalytic cysteine residue (By similarity).
May be a sulfotransferase involved in the formation of thiosulfate.
Part of an ABC transporter complex involved in glucose import (Probable). Responsible for the translocation of the substrate across the membrane (By similarity).
Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.
Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.
Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
In the C-terminal section; belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.
Belongs to the urease beta subunit family.
Belongs to the major facilitator superfamily. Nitrate/nitrite porter (TC 2.A.1.8) family.
Belongs to the pseudouridine synthase TruB family. Type 2 subfamily.
Could be responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalyzes the 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.
Belongs to the AP endonuclease 2 family.
Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
Activity unstable at KCl and NaCl concentrations lower than 2 M and activity increases with increasing concentrations of KCl or NaCl.
Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
Belongs to the HAD-like hydrolase superfamily. S-2-haloalkanoic acid dehalogenase family.
Belongs to the SecD/SecF family. SecD subfamily.
Part of the protein translocation apparatus. Forms a complex with SecF.
Part of the protein translocation apparatus. Forms a homodimer and complexes with SecF.
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.
DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Forms the clamp head domain.
Belongs to the group II decarboxylase family.
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. Mre11 binds to DSB ends and has both double-stranded 3'-5' exonuclease activity and single-stranded endonuclease activity (By similarity). In polyploid organisms, the Rad50/Mre11 complex appears to restrain the repair of double-strand breaks by homologous recombination, allowing another pathway to act as the primary mode of repair (PubMed:19593371).
Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.
Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.