NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ADP
Polymerizes into bundles of filaments, forming a helix with a filament width of 5.5 nm and an axial repeating unit of 5.5 nm. Polymerization of Ta0583 requires NTP and is optimal with ATP, but GTP, UTP, CTP, and even the deoxy form of NTP can also support the polymerization reaction. Nucleoside diphosphate or AMP-PNP does not support polymerization.
289 uM for ATP (when assaying the ATPase activity)
Optimum pH is 4.5-5.5 for the polymerization reaction.
Optimum temperature is 50-56 degrees Celsius for the polymerization reaction.
Mg(2+) is required for polymerization. 4 mM MgCl(2) is sufficient to enhance the polymerization; however, higher concentrations of MgCl(2) suppresses polymerization. Polymerization is also suppressed by addition of NaCl, KCl or CaCl(2), with half suppression by about 100 mM, 10 mM and 18 mM, respectively.
Belongs to the thermophilic archaeal actin family.
Polymerizes into bundles of filaments. Polymerization requires NTP and is optimal with ATP, but GTP, UTP, CTP, and even the deoxy form of NTP can also support the polymerization reaction (By similarity).
Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.
Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity.
Belongs to the histone-like Alba family.
COFACTOR-INDEPENDENT PHOSPHOGLYCERATE MUTASE
2,3-bisphosphoglycerate-independent phosphoglycerate mutase
Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.
Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently (By similarity).
Archaeosine synthase, lysine transferase subunit
Functions in the biosynthesis of archaeosine, a modified nucleoside present in the dihydrouridine loop (D-loop) of archaeal tRNAs. Catalyzes the addition of L-lysine to the cyano group of 7-cyano-7-deazaguanine (preQ0)-modified tRNAs at position 15, to generate q0kN15-tRNA, a q0N lysine adduct identified as 7-N-[(5S)-5-amino-5-carboxypentyl]formamidino-7-deazaguanosine.
Forms a robust complex with the archaeosine synthase beta subunit RaSEA, likely an alpha(2)beta(2) heterotetrameric structure. Formation of this complex highly increases lysine transfer activity.
Belongs to the archaeosine synthase type 1 family.
3-phosphoshikimate 1-carboxyvinyltransferase
5-enolpyruvylshikimate-3-phosphate synthase
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.
Dehydroquinate synthase-like - alpha domain
Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).
Belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family.
5-enolpyruvylshikimate-3-phosphate phospholyase
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 chorismate synthase 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 type-I 3-dehydroquinase family.
Leucine Dehydrogenase, chain A, domain 1
BIFUNCTIONAL 3-DEHYDROQUINATE DEHYDRATASE/SHIKIMATE DEHYDROGENASE, CHLOROPLASTIC
Aminoacid dehydrogenase-like, N-terminal domain
Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
Belongs to the shikimate dehydrogenase family.
HOMOSERINE/4-DIPHOSPHOCYTIDYL-2-C-METHYL-D-ERYTHRITOL KINASE
Belongs to the GHMP kinase family. Archaeal shikimate kinase subfamily.
Argininosuccinate synthetase, chain A, domain 2
Adenine nucleotide alpha hydrolases-like
Argininosuccinate synthetase, C-terminal domain
Belongs to the argininosuccinate synthase family. Type 1 subfamily.
7-cyano-7-deazaguanine tRNA-ribosyltransferase
Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.
Belongs to the archaeosine tRNA-ribosyltransferase family.
Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
Carbamoyl-phosphate synthase small subunit, N-terminal domain
CARBAMOYL-PHOSPHATE SYNTHASE SMALL CHAIN
MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN-RELATED
Carbamoyl phosphate synthetase, small subunit N-terminal domain
Carbamoyl-phosphate synthetase glutamine chain
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.
Carbamoyl-phosphate synthetase, large subunit oligomerisation domain
Carbamoyl phosphate synthetase, large subunit connection domain
Glutathione synthetase ATP-binding domain-like
Carbamoyl-phosphate synthase large chain
Carbamoyl-phosphate synthetase ammonia chain
Binds 4 Mg(2+) or Mn(2+) ions per subunit.
P-loop containing nucleotide triphosphate hydrolases
P-loop containing nucleoside triphosphate hydrolases
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.
Increases nucleophilicity of active site Cys
COBALT-PRECORRIN-5B C(1)-METHYLTRANSFERASE
Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.
COBALT-PRECORRIN-6B C(15)-METHYLTRANSFERASE (DECARBOXYLATING)
COBALT-PRECORRIN-7 C(5)-METHYLTRANSFERASE
S-adenosyl-L-methionine-dependent methyltransferases
Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)
Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.
Belongs to the methyltransferase superfamily. Archaeal-type CbiT family.
Archaeal tRNA CCA-adding enzyme catalytic domain
CCA tRNA nucleotidyltransferase, domain 2
Poly(A) polymerase predicted RNA binding domain
PAP/Archaeal CCA-adding enzyme, C-terminal domain
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.
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.
Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain
Putative ORC1-type DNA replication protein 1
Involved in regulation of DNA replication (By similarity). Has no effect on MCM helicase activity, either stimulatory or inhibitory. Does not bind DNA.
orc1/cdc6 family replication initiation protein
Involved in regulation of DNA replication. Stimulates the helicase activity of MCM via stimulation of its ATPase activity. Binding to MCM may result in conformational changes in MCM, leading to catalytic ATP hydrolysis by the helicase. Directly stimulates MCM movement along single-stranded and double-stranded DNA. Does not bind DNA.
The N-terminal AAA+ ATPase domain and the C-terminal winged-helix (WH) domain are both required for stimulation of MCM activity.
Does not affect stimulation of helicase activity.
Involved in regulation of DNA replication.
CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase
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 CDP-archaeol synthase family.
Citrate synthase is found in nearly all cells capable of oxidative metabolism.
Probable cobalamin biosynthesis protein CobD
Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.
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.
Belongs to the CobB/CobQ family. CobQ subfamily.
Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation (By similarity).
ADENOSYLCOBINAMIDE-GDP RIBAZOLETRANSFERASE
Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
2-PHOSPHOSULFOLACTATE PHOSPHATASE-RELATED
Probable 2-phosphosulfolactate phosphatase
Bifunctional phosphopantetheine adenylyltransferase/NTP phosphatase
Pantetheine-phosphate adenylyltransferase
Probable inosine/xanthosine triphosphatase
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
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.
Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+).
In the N-terminal section; belongs to the eukaryotic CoaD family.
In the C-terminal section; belongs to the YjjX NTPase family.
PROTOHEME IX FARNESYLTRANSFERASE, MITOCHONDRIAL
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.
Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.
Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.
4-HYDROXY-2-OXOGLUTARATE ALDOLASE, MITOCHONDRIAL
Histone-like DNA-binding protein which is capable of wrapping DNA to stabilize it, and thus to prevent its denaturation under extreme environmental conditions.
Belongs to the bacterial histone-like protein family.
DIAMINOPIMELATE DECARBOXYLASE 1, CHLOROPLASTIC-RELATED
Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine.
Belongs to the Orn/Lys/Arg decarboxylase class-II family. LysA subfamily.
Catalyzes the deamination of dCTP to dUTP.
METHYLTETRAHYDROFOLATE:HOMOCYSTEINE METHYLTRANSFERASE RELATED
Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Belongs to the uroporphyrinogen decarboxylase family.
Complete sequence of Aciduliprofundum boonei T469.
Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Shows high stability to high concentrations of acetaldehyde.
0.12 mM for 2-deoxy-D-ribose 5-phosphate
Optimum pH is 7.0. Extremely stable over a wide range of pH levels.
Optimum temperature is 80 degrees Celsius.
Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.
Schiff-base intermediate with acetaldehyde
Fumarate reductase/succinate dehydrogenase, transmembrane subunit
Fumarate reductase respiratory complex transmembrane subunits
Succinate dehydrogenase hydrophobic membrane anchor subunit
Membrane-anchoring subunit of succinate dehydrogenase (SDH).
The heme is bound between the two transmembrane subunits.
Part of an enzyme complex containing four subunits: a flavoprotein, an iron-sulfur protein, plus two membrane-anchoring proteins, SdhC and SdhD.
ligand shared with second transmembrane subunit
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.
Belongs to the deoxyhypusine synthase family.
RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.
Forms a ternary complex with MCM helicase and DNA. Component of the archaeal exosome complex.
Belongs to the archaeal DnaG primase family.
Heat shock protein DnaJ, cysteine-rich domain
Urease metallochaperone UreE, N-terminal domain
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.
Heat shock protein 70kD (HSP70), C-terminal subdomain
Heat shock protein 70kD (HSP70), peptide-binding domain
Belongs to the heat shock protein 70 family.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-594
DNA ligase, ATP-dependent, N-terminal domain
ATP-dependent DNA ligase DNA-binding domain
DNA ligase/mRNA capping enzyme, catalytic domain
DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.
Belongs to the ATP-dependent DNA ligase 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 (By similarity).
Heterodimer of a large subunit and a small subunit.
Belongs to the archaeal DNA polymerase II 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 (By similarity).
Belongs to the DNA polymerase delta/II small subunit family.
Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).
Belongs to the GTP-dependent DPCK family.
Diphthamide biosynthesis methyltransferase
S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.
Belongs to the diphthine synthase family.
5' to 3' exonuclease, C-terminal subdomain
DNA polymerase, Y-family, little finger domain
DNA REPAIR POLYMERASE UMUC / TRANSFERASE FAMILY MEMBER
Lesion bypass DNA polymerase (Y-family), little finger domain
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.
Belongs to the DNA polymerase type-Y family.
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.
EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.
Promotes the exchange of GDP for GTP in EF-1-alpha/GDP, thus allowing the regeneration of EF-1-alpha/GTP that could then be used to form the ternary complex EF-1-alpha/GTP/AAtRNA.
Belongs to the EF-1-beta/EF-1-delta family.
Elongation Factor G (Translational Gtpase), domain 3
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 TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity).
Divalent-metal-dependent TIM barrel enzymes
AP_ENDONUC_2 DOMAIN-CONTAINING PROTEIN-RELATED
ENDONUCLEASE IV ENDODEOXYRIBONUCLEASE IV
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.
Belongs to the AP endonuclease 2 family.
tRNA-intron endonuclease catalytic domain-like
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 (By similarity).
Belongs to the tRNA-intron endonuclease family. Archaeal long subfamily.
tRNA-intron endonuclease N-terminal domain-like
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.
Fractions of enolase are present in both the cytoplasm and on the cell surface. The export of enolase possibly depends on the covalent binding to the substrate; once secreted, it remains attached to the cell surface.
Required for formate dehydrogenase (FDH) activity. Acts as a sulfur carrier protein that transfers sulfur from IscS to the molybdenum cofactor prior to its insertion into FDH.
Belongs to the ferredoxin--NADP reductase type 2 family.
Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Binds the unpaired 3'-DNA end and kinks the DNA to facilitate 5' cleavage specificity. Cleaves one nucleotide into the double-stranded DNA from the junction in flap DNA, leaving a nick for ligation. Also involved in the base excision repair (BER) pathway. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA (By similarity).
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.
Belongs to the XPG/RAD2 endonuclease family. FEN1 subfamily.
L-ASPARTATE SEMIALDEHYDE SULFURTRANSFERASE IRON-SULFUR SUBUNIT
Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Flagellin is the subunit protein which polymerizes to form the filaments of archaeal flagella.
Belongs to the archaeal flagellin family.
Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase
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.
Interacts with nop5. Component of box C/D small ribonucleoprotein (sRNP) particles that contain rpl7ae, FlpA and nop5, plus a guide RNA.
Belongs to the methyltransferase superfamily. Fibrillarin family.
C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC
C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC-RELATED
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 tetrahydrofolate dehydrogenase/cyclohydrolase family.
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-82
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH NADP
Domain 2, N(10)-formyltetrahydrofolate synthetase
Formyltetrahydrofolate synthetase, domain 3
Belongs to the formate--tetrahydrofolate ligase family.
Signal recognition particle SRP54, nucleotide-binding domain
SIGNAL RECOGNITION PARTICLE RECEPTOR SUBUNIT ALPHA
Domain of the SRP/SRP receptor G-proteins
Signal recognition particle receptor FtsY
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 GTP-binding SRP family. FtsY subfamily.
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.
Assembles at midcell at the inner surface of the cytoplasmic membrane.
Glycerol-1-phosphate dehydrogenase [NAD(P)+]
Catalyzes the NAD(P)H-dependent reduction of dihydroxyacetonephosphate (DHAP or glycerone phosphate) to glycerol 1-phosphate (G1P). The G1P thus generated is used as the glycerophosphate backbone of phospholipids in the cellular membranes of Archaea.
Belongs to the glycerol-1-phosphate dehydrogenase family.
Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain
Glyceraldehyde-3-phosphate dehydrogenase
NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase
Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL
D-glyceraldehyde dehydrogenase (NADP(+))
NADP-dependent dehydrogenase of the nED (non-phosphorylated Entner-Doudoroff) pathway with highest activity towards glyceraldehydes (e.g. D,L-glyceraldehyde and D-glyceraldehyde), to a lesser extent towards D,L-glyceraldehyde-3-phosphate and glycolaldehyde, but no activity towards aliphatic or aromatic aldehydes.
Stable for 2 hours at 60 degrees Celsius but activity is decreased to less than 50 percent within 15 minutes at 70 degrees Celsius.
kcat is 10 sec(-1) with glyceraldehyde as substrate, 12 sec(-1) with glyceraldehyde-3-phosphate as substrate, 20 sec(-1) with glycolaldehyde as substrate and 10 sec(-1) with NADP as substrate (at pH 6.9 and 58 degrees Celsius).
0.06 mM for glyceraldehyde (at pH 6.9 and 58 degrees Celsius)
5.1 mM for glyceraldehyde-3-phosphate (at pH 6.9 and 58 degrees Celsius)
11.1 mM for glycolaldehyde (at pH 6.9 and 58 degrees Celsius)
0.42 mM for NADP (at pH 6.9 and 58 degrees Celsius)
Optimum temperature is 63 degrees Celsius.
Homotetramer (By similarity). Dimer of dimers.
Belongs to the aldehyde dehydrogenase family. Glyceraldehyde dehydrogenase subfamily.
Inhibited by calcium, cadmium, copper and mercury ions. Stable for 2 hours at 60 degrees Celsius but activity is decreased to less than 50 percent within 20 minutes at 80 degrees Celsius. Two folds activity enhancement in the presence of 1 mM glutathione, DTT, or 2-mercaptoethanol. Complete activity inhibition by thiol-modifying reagents such as p-chloromercuribenzoic acid or p-hydroxy-mercuribenzoic acid.
kcat is 26 sec(-1) with glyceraldehyde as substrate, 20 sec(-1) with glyceraldehyde-3-phosphate as substrate, 37 sec(-1) with glycolaldehyde as substrate and 25 sec(-1) with NADP as substrate (at pH 7.9 and 58 degrees Celsius).
0.2 mM for glyceraldehyde (at pH 7.9 and 58 degrees Celsius)
18.3 mM for glyceraldehyde-3-phosphate (at pH 7.9 and 58 degrees Celsius)
12.3 mM for glycolaldehyde (at pH 7.9 and 58 degrees Celsius)
0.36 mM for NADP (at pH 7.9 and 58 degrees Celsius)
0.33 mM for D,L-glyceraldehyde (at pH 8 and 50 degrees Celsius)
0.017 mM for NADP (at pH 8 and 50 degrees Celsius)
0.3 umol/min/mg enzyme with D,L-glyceraldehyde as substrate (at pH 8 and 50 degrees Celsius)
0.3 umol/min/mg enzyme with NADP as substrate (at pH 8 and 50 degrees Celsius)
Optimum temperature is 50-55 degrees Celsius at pH 8 and 63 degrees Celsius at pH 7.6.
Involved in the degradation of glucose and galactose via the nonphosphorylative variant of Entner-Doudoroff pathway. Catalyzes the dehydration of gluconate to produce 2-keto-3-deoxygluconate (KDG). It is also able to catalyze the dehydration of galactonate to produce 2-keto-3-deoxygalactonate (KDGal).
2 mM for galactonate (at 60 degrees Celsius and pH 6.2)
2.5 mM for gluconate (at 60 degrees Celsius and pH 6.2)
15 umol/min/mg enzyme with gluconate as substrate (at 60 degrees Celsius and pH 6.2)
1 umol/min/mg enzyme with galactonate as substrate (at 60 degrees Celsius and pH 6.2)
Optimum temperature is 70 degrees Celsius.
Belongs to the mandelate racemase/muconate lactonizing enzyme family. GaD subfamily.
Glutamyl-tRNA(Gln) amidotransferase subunit D
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.
GLUTAMYL-TRNA GLN AMIDOTRANSFERASE SUBUNIT B MITOCHONDRIAL AND PROKARYOTIC PET112-RELATED
GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT E
Belongs to the GatB/GatE family. GatE subfamily.
Glycerate kinase, MOFRL-like N-terminal domain
2-phosphoglycerate forming glycerate kinase
Catalyzes the ATP-dependent phosphorylation of D-glycerate to 2-phosphoglycerate. It can also partially utilize GTP, CTP or UTP as phosphate donor.
Magnesium. It could be replaced to some extent by nickel, manganese or cobalt.
340 uM for glycerate (at 50 degrees Celsius and at pH 7.3)
500 uM for ATP (at 50 degrees Celsius and at pH 7.3)
435 umol/min/mg enzyme (at 50 degrees Celsius and at pH 7.3)
Optimum pH is 7.3 and 50% of activity at pH 5.6 and at pH 8.6.
Optimum temperature is 60 degrees Celsius. It does not lose activity upon incubation at 60 degrees Celsius for 2 h. The half time at 70 degrees Celsius is about 5 min.
Belongs to the glycerate kinase type-1 family.
GLYCINE CLEAVAGE SYSTEM H PROTEIN, MITOCHONDRIAL
Probable glycine cleavage system H protein
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.
Type I PLP-dependent aspartate aminotransferase-like (Major domain)
Probable glycine dehydrogenase (decarboxylating) subunit 1
Glycine cleavage system P-protein subunit 1
Glycine dehydrogenase (aminomethyl-transferring) subunit 1
The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
The glycine cleavage system is composed of four proteins: P, T, L and H. In this organism, the P 'protein' is a heterodimer of two subunits.
Belongs to the GcvP family. N-terminal subunit subfamily.
GLYCINE DEHYDROGENASE (DECARBOXYLATING), MITOCHONDRIAL
Probable glycine dehydrogenase (decarboxylating) subunit 2
Glycine cleavage system P-protein subunit 2
Glycine dehydrogenase (aminomethyl-transferring) subunit 2
Belongs to the GcvP family. C-terminal subunit subfamily.
Geranylgeranylglyceryl phosphate synthase
(S)-3-O-geranylgeranylglyceryl phosphate synthase
Phosphoglycerol geranylgeranyltransferase
Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P). This reaction is the first ether-bond-formation step in the biosynthesis of archaeal membrane lipids.
Belongs to the GGGP/HepGP synthase family. Group II subfamily.
Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P). This reaction is the first ether-bond-formation step in the biosynthesis of archaeal membrane lipids. Cannot use sn-glycerol-3-phosphate (G3P) as substrate.
Inhibited by high concentrations of magnesium (>10 mM) and by EDTA in vitro.
21.2 uM for G-1,3-P (at 55 degrees Celsius and pH 7)
75 nM for GGPP (at 55 degrees Celsius and pH 7)
13.5 umol/min/mg enzyme (at 55 degrees Celsius and pH 7)
Optimum pH is about 7.0. Active from pH 6 to 9.
Optimum temperature is 55 degrees Celsius.
D-Amino Acid Oxidase, subunit A, domain 2
DIGERANYLGERANYLGLYCEROPHOSPHOLIPID REDUCTASE
2,3-bis-O-geranylgeranylglyceryl phosphate reductase
Is involved in the reduction of 2,3-digeranylgeranylglycerophospholipids (unsaturated archaeols) into 2,3-diphytanylglycerophospholipids (saturated archaeols) in the biosynthesis of archaeal membrane lipids. Catalyzes the formation of archaetidic acid (2,3-di-O-phytanyl-sn-glyceryl phosphate) from 2,3-di-O-geranylgeranylglyceryl phosphate (DGGGP) via the hydrogenation of each double bond of the isoprenoid chains.
Reduction reaction proceeds via syn addition of hydrogen for double bonds.
Belongs to the geranylgeranyl reductase family. DGGGPL reductase subfamily.
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH FAD AND LIPID
Is involved in the reduction of 2,3-digeranylgeranylglycerophospholipids (unsaturated archaeols) into 2,3-diphytanylglycerophospholipids (saturated archaeols) in the biosynthesis of archaeal membrane lipids. Catalyzes the formation of archaetidic acid (2,3-di-O-phytanyl-sn-glyceryl phosphate) from 2,3-di-O-geranylgeranylglyceryl phosphate (DGGGP) via the hydrogenation of each double bond of the isoprenoid chains. Can use both NADH and NADPH as electron donors. Also catalyzes the reduction of the naturally occurring 2,3-di-O-geranylgeranylglyceryl phosphate derivatives such as 2,3-di-O-phytyl-sn-glyceryl phosphate (DPHGP), 3-O-(2,3-di-O-phytyl-sn-glycero-phospho)-sn-glycerol (DPHGPG) and 2,3-di-O-phytyl-sn-glycero-phosphoethanolamine (DPHGPE). Is not active toward 2,3-di-O-geranylgeranylglycerol.
Medium-chain alcohol dehydrogenases, catalytic domain
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 non-phosphorylative variant of the Entner-Doudoroff pathway.
Binds 2 Zn(2+) ions per subunit. One of the zinc atoms is essential for catalytic activity while the other has a structural function.
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. Is also significantly active with D-galactose as substrate, but not with D-xylose, L-arabinose, D-ribose, D-mannose, D-allose, D-glucosamine, 2-deoxy-D-glucose, or glucose-6-phosphate. Can utilize both NAD(+) and NADP(+) as electron acceptor, with a marked preference for NADP(+) (20-fold higher activity). Physiologically, may be involved in the degradation of both glucose and galactose through a non-phosphorylative variant of the Entner-Doudoroff pathway.
Zn(2+) is of critical importance for the stability of the enzyme.
Optimum pH is 6.5 for the oxidation of D-glucose by NADP(+). At the physiological pH of 4.6 found in the cytoplasm of Picrophilus cells, the enzyme shows merely 10% of its maximal activity.
Optimum temperature is 55 degrees Celsius for the oxidation of D-glucose by NADP(+).
ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE PROTEIN C1198.01-RELATED
Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to D-gluconate via gluconolactone. Is also significantly active with galactose as substrate, but not with mannose or glucose 6-phosphate. Can utilize both NAD(+) and NADP(+) as electron acceptor, with a marked preference for NADP(+). Physiologically, may be involved in the degradation of both glucose and galactose through a non-phosphorylative variant of the Entner-Doudoroff pathway.
The KM value for NAD(+) is superior to 30 mM, it could not be defined precisely as it was impossible to reach saturation of the enzyme.
Thermostable. Retains full catalytic activity after 9 hours at 55 degrees Celsius, and at 75 degrees Celsius the half-life is approximately 3 hours.
Formiminotransferase, C-terminal subdomain
Formiminotransferase, N-terminal subdomain
FORMIMINOTRANSFERASE N-TERMINAL SUBDOMAIN-CONTAINING PROTEIN
Formiminotransferase domain of formiminotransferase-cyclodeaminase
Catalyzes the transfer of the formyl group from N-formylglutamate to tetrahydrofolate (THF) to yield 5-formyltetrahydrofolate (5-CHO-THF) and glutamate (Glu). The triglutamate form of 5-CHO-THF (5-CHO-THF-Glu3) can also be used as substrate. It can also catalyzes the transfer of the formimino group from N-formiminoglutamate to tetrahydrofolate (THF) to yield 5-formiminotetrahydrofolate (5-NH=CH-THF) and glutamate (Glu). It can replace YgfA to catalyzes the irreversible ATP-dependent transformation of 5-CHO-THF to form 5,10-methenyltetrahydrofolate (5,10-CH=THF).
kcat is 1.16 sec(-1) for formyltransferase with 5-CHO-THF or 5-CHO-THF-Glu3 as substrates (at pH 7.3 and 30 degrees Celsius).
0.4 uM for 5-CHO-THF (at pH 7.3 and 30 degrees Celsius)
0.7 uM for 5-CHO-THF-Glu3 (at pH 7.3 and 30 degrees Celsius)
34 uM for Glu (at pH 7.3 and 30 degrees Celsius)
Belongs to the formiminotransferase family.
kcat is 0.27 sec(-1) for formyltransferase with 5-CHO-THF or 5-CHO-THF-Glu3 as substrates (at pH 7.3 and 30 degrees Celsius).
3.7 uM for 5-CHO-THF (at pH 7.3 and 30 degrees Celsius)
3.8 uM for 5-CHO-THF-Glu3 (at pH 7.3 and 30 degrees Celsius)
113 uM for Glu (at pH 7.3 and 30 degrees Celsius)
1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase
Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
Belongs to the glycosyl hydrolase 13 family. GlgB subfamily.
Phosphotransferase system, lactose/cellobiose-type IIA subunit
ALPHA-1,4-GLUCAN:MALTOSE-1-PHOSPHATE MALTOSYLTRANSFERASE
(1->4)-alpha-D-glucan:maltose-1-phosphate alpha-D-maltosyltransferase
Maltosyltransferase that uses maltose 1-phosphate (M1P) as the sugar donor to elongate linear or branched alpha-(1->4)-glucans. Is involved in a branched alpha-glucan biosynthetic pathway from trehalose, together with TreS, Mak and GlgB.
Belongs to the glycosyl hydrolase 13 family. GlgE subfamily.
SERINE HYDROXYMETHYLTRANSFERASE, MITOCHONDRIAL
Catalyzes the reversible interconversion of serine and glycine with a modified folate serving as the one-carbon carrier. Also exhibits a pteridine-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
Plays an important role in substrate specificity
SEDOHEPTULOSE 7-PHOSPHATE ISOMERASE / DNAA INITIATOR-ASSOCIATING FACTOR FOR REPLICATION INITIATION
Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate.
The reaction produces a racemic mixture of D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate.
Belongs to the SIS family. GmhA subfamily.
D-GLYCERO-BETA-D-MANNO-HEPTOSE-1,7-BISPHOSPHATE 7-PHOSPHATASE
Probable D-glycero-D-manno-heptose-1,7-bisphosphate 7-phosphatase
D,D-heptose 1,7-bisphosphate phosphatase
Converts the D-glycero-D-manno-heptose 1,7-bisphosphate intermediate into D-glycero-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position.
BROAD-SPECIFICITY PHOSPHATASE YOR283W-RELATED
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
Inhibited by vanadate. Inhibition can partially be relieved by EDTA.
Belongs to the phosphoglycerate mutase family.
The original start site is 14 aa downstream of the start site shown here. Experiments from PubMed:17576516 were carried out with the original sequence.
Head domain of nucleotide exchange factor GrpE
Coiled-coil domain of nucleotide exchange factor GrpE
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.
GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE
GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE 1, CHLOROPLASTIC-RELATED
Glutamate-1-semialdehyde aminotransferase
Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily.
GMP synthase [glutamine-hydrolyzing] subunit A
Catalyzes the synthesis of GMP from XMP.
Heterodimer composed of a glutamine amidotransferase subunit (A) and a GMP-binding subunit (B).
GMP synthetase C-terminal dimerisation domain
GMP synthase [glutamine-hydrolyzing] subunit B
DNA POLYMERASE THETA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05260)-RELATED
DNA-dependent ATPase and 3'-5' DNA helicase that may be involved in repair of stalled replication forks.
Belongs to the helicase family. Hel308 subfamily.
Glutamyl-tRNA reductase, N-terminal domain
Glutamyl tRNA-reductase catalytic, N-terminal domain
Glutamyl tRNA-reductase dimerization domain
Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (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.
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.
Belongs to the glutamyl-tRNA reductase family.
Porphobilinogen deaminase (hydroxymethylbilane synthase), C-terminal domain
Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Binds 1 dipyrromethane group covalently.
The porphobilinogen subunits are added to the dipyrromethane group.
Porphobilinogen deaminase, C-terminal domain
Catalyzes the ferrous insertion into protoporphyrin IX.
IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISH
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.
Nitrogenase molybdenum iron protein domain
HISTIDINE BIOSYNTHESIS TRIFUNCTIONAL PROTEIN
Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
Belongs to the histidinol dehydrogenase family.
HYPOXANTHINE/GUANINE PHOSPHORIBOSYLTRANSFERASE
Catalyzes a salvage reaction resulting in the formation of IMP that is energically less costly than de novo synthesis.
Belongs to the purine/pyrimidine phosphoribosyltransferase family. Archaeal HPRT subfamily.
Metalloproteases ('zincins'), catalytic domain
Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly.
Composite domain of metallo-dependent hydrolases
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.
Belongs to the metallo-dependent hydrolases superfamily. HutI family.
Catalyzes the conversion of urocanate to 4-imidazolone-5-propionate.
Isopentenyl diphosphate:dimethylallyl diphosphate isomerase
Type 2 isopentenyl diphosphate isomerase
Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP).
Belongs to the IPP isomerase type 2 family.
EUKARYOTIC TRANSLATION INITIATION FACTOR 4C
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.
Seems to be required for maximal rate of protein biosynthesis. Enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal subunits (By similarity).
EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 1
Translation initiation factor 2 subunit alpha
eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA.
Heterotrimer composed of an alpha, a beta and a gamma chain.
EUKARYOTIC TRANSLATION INITIATION FACTOR
EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 2
Translation initiation factor 2 beta, aIF2beta, N-terminal domain
Zinc-binding domain of translation initiation factor 2 beta
Translation initiation factor 2 subunit beta
EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 3 FAMILY MEMBER
EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 3-RELATED
Translation initiation factor 2 subunit gamma
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EIF2G subfamily.
Translation initiation factor IF- 2, domain 3
EUKARYOTIC TRANSLATION INITIATION FACTOR 5B
TRANSLATION INITIATION FACTOR IF-2-RELATED
Probable translation initiation factor IF-2
Function in general translation initiation by promoting the binding of the formylmethionine-tRNA to ribosomes. Seems to function along with eIF-2 (By similarity).
Belongs to the 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.
EUKARYOTIC TRANSLATION INITIATION FACTOR 5A
TRANSLATION INITIATION FACTOR 5A FAMILY MEMBER
Functions by promoting the formation of the first peptide bond.
EUKARYOTIC TRANSLATION INITIATION FACTOR 6
Binds to the 50S ribosomal subunit and prevents its association with the 30S ribosomal subunit to form the 70S initiation complex.
DIHYDROXY-ACID DEHYDRATASE, MITOCHONDRIAL
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.
Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis acid cofactor.
INOSINE-5-MONOPHOSPHATE DEHYDROGENASE RELATED
Inosine monophosphate dehydrogenase (IMPDH)
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.
ligand shared between two tetrameric partners
X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) IN COMPLEXES WITH ISOPENTENYL PHOSPHATE AND ATP
Catalyzes the formation of isopentenyl diphosphate (IPP), the building block of all isoprenoids. Has lower activity with isopentenyl thiolophosphate (ISP). Has low activity with dimethylallyl phosphate (DMAP), 1-butyl phosphate (BP) and 3-buten-1-yl phosphate (BEP). Has no significant activity with geranyl phosphate (in vitro).
Belongs to the isopentenyl phosphate kinase family.
Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
INOSINE TRIPHOSPHATE PYROPHOSPHATASE/HAM1 PROTEIN
non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family
Non-canonical purine NTP pyrophosphatase
Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Broad-specificity nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates.
Belongs to the adenylate kinase family. AK6 subfamily.
Belongs to the archaeal adenylate kinase family.
Transferase(Phosphotransferase) domain 1
TRNA N6-ADENOSINE THREONYLCARBAMOYLTRANSFERASE
TRNA N6-ADENOSINE THREONYLCARBAMOYLTRANSFERASE-RELATED
Probable bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein
t(6)A37 threonylcarbamoyladenosine biosynthesis protein Kae1
tRNA threonylcarbamoyladenosine biosynthesis protein Kae1
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.
Component of the KEOPS complex that consists of Kae1, Bud32, Cgi121 and Pcc1; the whole complex dimerizes.
In the N-terminal section; belongs to the KAE1 / TsaD family.
In the C-terminal section; belongs to the protein kinase superfamily. Tyr protein kinase family. BUD32 subfamily.
X-RAY CRYSTALLOGRAPHY (3.02 ANGSTROMS) OF 1-329
Belongs to the cytidylate kinase family. Type 2 subfamily.
2-dehydro-3-deoxy-D-gluconate/2-dehydro-3-deoxy-phosphogluconate aldolase
2-dehydro-3-deoxy-galactonate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase
Involved in the degradation of glucose via the Entner-Doudoroff pathway. Catalyzes the reversible cleavage of 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-3-deoxygluconate (KDG) forming pyruvate and glyceraldehyde 3-phosphate or glyceraldehyde, respectively. It is also able to catalyze the reversible cleavage of 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) and 2-keto-3-deoxygalactonate (KDGal). It is equally active with both D- and L-glyceraldehyde.
0.3 mM for KDG (at 60 degrees Celsius and pH 6.2)
2.7 mM for pyruvate (at 60 degrees Celsius and pH 6.2)
4.6 mM for glyceraldehyde (at 60 degrees Celsius and pH 6.2)
8 mM for KDPG (at 60 degrees Celsius and pH 6.2)
67 umol/min/mg enzyme with KDG as D-glyceraldehyde (at 60 degrees Celsius and pH 6.2)
59 umol/min/mg enzyme with KDG as L-glyceraldehyde (at 60 degrees Celsius and pH 6.2)
50 umol/min/mg enzyme with KDG as substrate (at 60 degrees Celsius and pH 6.2)
0.63 umol/min/mg enzyme with KDPG as substrate (at 60 degrees Celsius and pH 6.2)
Optimum pH is 5.5, and 50% of activity is found at pH 4.5 and 7.5.
Optimum temperature is 65 degrees Celsius. It shows high thermostability. At 70 degrees Celsius, the enzyme does not lose activity upon incubation for 2 hours. The half-lives of the enzyme at 80 degrees Celsius and 90 degrees Celsius are 20 minutes and 15 minutes, respectively.
Belongs to the DapA family. KDPG aldolase subfamily.
Catalyzes the phosphorylation of 2-keto-3-deoxygluconate (KDG) to produce 2-keto-3-deoxy-6-phosphogluconate (KDPG). Is specific for KDG.
Probably activated by phosphorylation and inhibited by dephosphorylation.
Belongs to the eukaryotic-type N-acetylglucosamine kinase family.
POTASSIUM-TRANSPORTING ATPASE POTASSIUM-BINDING SUBUNIT
ATP phosphohydrolase [potassium-transporting] A chain
Potassium-binding and translocating subunit A
Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit binds the extracellular potassium ions and delivers the ions to the membrane domain of KdpB through an intramembrane tunnel.
The system is composed of three essential subunits: KdpA, KdpB and KdpC.
Calcium-transporting ATPase, cytoplasmic domain N
Calcium-transporting ATPase, cytoplasmic transduction domain A
POTASSIUM-TRANSPORTING ATPASE ATP-BINDING SUBUNIT
ATP phosphohydrolase [potassium-transporting] B chain
Potassium-binding and translocating subunit B
Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit is responsible for energy coupling to the transport system and for the release of the potassium ions to the cytoplasm.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IA subfamily.
POTASSIUM-TRANSPORTING ATPASE KDPC SUBUNIT
ATP phosphohydrolase [potassium-transporting] C chain
Potassium-binding and translocating subunit C
Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the formation of a transient KdpB/KdpC/ATP ternary complex.
Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Belongs to the GHMP kinase family. Homoserine kinase subfamily.
RIBOSE-PHOSPHATE DIPHOSPHOKINASE FAMILY MEMBER
5-phospho-D-ribosyl alpha-1-diphosphate synthase
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 ribose-phosphate pyrophosphokinase family. Class III (archaeal) subfamily.
X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS
RNA 2'-phosphotransferase, Tpt1/KptA family, N-terminal domain
Removes the 2'-phosphate from RNA via an intermediate in which the phosphate is ADP-ribosylated by NAD followed by a presumed transesterification to release the RNA and generate ADP-ribose 1''-2''-cyclic phosphate (APPR>P). May function as an ADP-ribosylase (By similarity).
Removes the 2'-phosphate from RNA via an intermediate in which the phosphate is ADP-ribosylated by NAD followed by a presumed transesterification to release the RNA and generate ADP-ribose 1''-2''-cyclic phosphate (APPR>P). May function as an ADP-ribosylase.
PubMed:1426985 has published some partial sequence, these sequences do not originate from T.acidophilum, rather they seem to be contaminated with human samples.
Belongs to the thymidylate kinase family.
3-isopropylmalate dehydratase large subunit
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Belongs to the aconitase/IPM isomerase family. LeuC type 2 subfamily.
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.
Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Belongs to the radical SAM superfamily. Lipoyl synthase family.
LIPOYLTRANSFERASE 2, MITOCHONDRIAL-RELATED
Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase 1
Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
In the reaction, the free carboxyl group of octanoic acid is attached via an amide linkage to the epsilon-amino group of a specific lysine residue of lipoyl domains of lipoate-dependent enzymes.
Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase 2
MUTAGENESIS OF LYS-63; ASP-241; ASN-293; ARG-305; ARG-375 AND ARG-382
ATP DEPENDENT LON PROTEASE FAMILY MEMBER
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.
Homohexamer. Organized in a ring with a central cavity.
Belongs to the peptidase S16 family. Archaeal LonB subfamily.
Completely abolishes ATPase activity and makes peptidase activity independent on ATP stimulus.
Retains 5% ATPase activity. Proteolytic activity is greatly impaired and cannot be stimulated by nucleotides.
Severely reduces ATPase and proteolytic activity.
Decreases ATPase activity. Completely abolishes peptidase activity in the absence of ATP, but ATP-stimulated peptidase activity i close to wild-type levels.
Almost completely abolishes ATPase activity and severely reduces proteolytic activity.
Abolishes peptidase activity, but retains ATPase activity.
ATP-dependent protease La homolog type 1
ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Degrades polypeptides processively (By similarity).
Homohexamer. Organized in a ring with a central cavity (By similarity).
Lacks the conserved Ser-Lys catalytic dyad essential for proteolytic activity. Its enzyme activity is therefore unsure.
CO dehydrogenase flavoprotein, C-terminal domain
Part of a lipoate-protein ligase complex that catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. Can also use octanoate as substrate.
In contrast to E.coli, where the lipoate-protein ligase is encoded by a single gene product (LplA) with a large N-terminal domain and a small C-terminal domain, the same activity in T.acidophilum is dependent on two separate proteins, corresponding to the two domains of E.coli LplA, respectively.
X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH LIPOIC ACID AND MAGNESIUM
LACK OF FUNCTION AS A LIPOYL TRANSFERASE
X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH SUBSTRATES AND MAGNESIUM
OCTANOYL-[GCVH]:PROTEIN N-OCTANOYLTRANSFERASE
[LYSW]-L-2-AMINOADIPATE/[LYSW]-L-GLUTAMATE PHOSPHATE REDUCTASE-RELATED
N-ACETYL-GAMMA-GLUTAMYL-PHOSPHATE REDUCTASE, CHLOROPLASTIC-RELATED-RELATED
Putative [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase
Involved in both the arginine and lysine biosynthetic pathways.
Belongs to the NAGSA dehydrogenase family. Type 1 subfamily. LysY sub-subfamily.
Mevalonate 3,5-bisphosphate decarboxylase
Catalyzes the ATP-independent decarboxylation of (R)-mevalonate 3,5-bisphosphate to isopentenyl phosphate. Functions in an alternative mevalonate pathway, only present in extreme acidophiles of the Thermoplasmatales order, which passes through mevalonate 3-phosphate rather than mevalonate 5-phosphate. Shows no detectable decarboxylase activity on mevalonate, mevalonate 3-phosphate, mevalonate 5-phosphate or mevalonate 5-pyrophosphate.
It is proposed that Thermoplasmatales adapted the classical archaeal mevalonate pathway by replacing mevalonate 5-phosphate decarboxylase (MMD) with two specialized enzymes (mevalonate-3-phosphate 5-kinase and mevalonate 3,5-bisphosphate decarboxylase) in order to produce isoprenoids in extremely acidic environments. It was found that at low pH, the dual function enzyme MMD is unable to carry out the first phosphorylation step, yet retains its ability to perform decarboxylation.
Belongs to the mevalonate 3,5-bisphosphate decarboxylase family.
Catalyzes the ATP-independent decarboxylation of (R)-mevalonate 3,5-bisphosphate to isopentenyl phosphate. Functions in an alternative mevalonate pathway, only present in extreme acidophiles of the Thermoplasmatales order, which passes through mevalonate 3-phosphate rather than mevalonate 5-phosphate.
Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal
L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+))
Catalyzes the reversible oxidation of malate to oxaloacetate.
Cloning and sequencing of the gene for the L-malate dehydrogenase from the thermoacidophilic archaebacterium Thermoplasma acidophilum.
Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
Thermoplasmatales-like gut symbionts are pyrrolysine dependent-methanogens.
5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE--HOMOCYSTEINE METHYLTRANSFERASE
Catalyzes the transfer of a methyl group to L-homocysteine resulting in methionine formation. The physiological methyl donor is unknown.
S-adenosylmethionine synthetase, C-terminal domain
S-adenosylmethionine synthetase, N-terminal domain
Catalyzes the formation of S-adenosylmethionine from methionine and ATP.
Belongs to the AdoMet synthase 2 family.
MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN 1
MOLYBDOPTERIN COFACTOR SYNTHESIS PROTEIN A
Molybdenum cofactor biosynthesis protein A
Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate.
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.
Belongs to the radical SAM superfamily. MoaA family.
Molybdopterin cofactor biosynthesis C (MoaC) domain
Molybdenum cofactor biosynthesis protein C, MoaC
Probable cyclic pyranopterin monophosphate synthase
Molybdenum cofactor biosynthesis protein C
Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
MOLYBDOPTERIN SYNTHASE CATALYTIC SUBUNIT
Molybdenum cofactor biosynthesis protein E
Molybdopterin-converting factor large subunit
Molybdopterin-converting factor subunit 2
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 MoaD (By similarity).
Heterotetramer of 2 MoaD subunits and 2 MoaE subunits. Also stable as homodimer. The enzyme changes between these two forms during catalysis (By similarity).
Converts GTP to 7,8-dihydro-D-neopterin 2',3'-cyclic phosphate, the first intermediate in the biosynthesis of coenzyme methanopterin.
Belongs to the GTP cyclohydrolase IV family.
Structure of hypothetical protein PTO0218 from Picrophilus torridus.
New York structural genomix research consortium (NYSGXRC)
X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 2-120
Catalyzes the conversion of 7,8-dihydroneopterin (H2Neo) to 6-hydroxymethyl-7,8-dihydropterin (6-HMD).
Belongs to the archaeal dihydroneopterin aldolase family.
COMPONENT OF ATP-DEPENDENT DSDNA EXONUCLEASE
DNA double-strand break repair protein Mre11
Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Mre11 binds to DSB ends and has both double-stranded 3'-5' exonuclease activity and single-stranded endonuclease activity.
Nuclease activity is regulated by Rad50.
Homodimer. Forms a heterotetramer composed of two Mre11 subunits and two Rad50 subunits.
Peptide methionine sulphoxide reductase MsrA
PEPTIDE METHIONINE SULFOXIDE REDUCTASE MSRA 2
Peptide methionine sulfoxide reductase MsrA
Peptide-methionine (S)-S-oxide reductase
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.
Belongs to the MsrA Met sulfoxide reductase family.
Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates.
Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.
Catalyzes the phosphorylation of mevalonate (MVA) to yield mevalonate-3-phosphate. Functions in an alternative mevalonate pathway, which passes through mevalonate 3-phosphate rather than mevalonate 5-phosphate. Also able to catalyze the formation of isobutene via the conversion of 3-hydroxyisovalerate (3-HIV) to an unstable 3-phosphate intermediate that undergoes a spontaneous decarboxylation.
kcat is 1.9 sec(-1) for mevalonate as substrate. kcat is 0.1 sec(-1) for 3-hydroxyisovalerate (3-HIV) as substrate. kcat is 0.1 sec(-1) for 3-hydroxybutyrate (3-HB) as substrate.
2348 uM for 3-hydroxyisovalerate (3-HIV)
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND ATP ANALOG
MUTAGENESIS OF LEU-18; SER-105 AND ARG-185
Catalyzes the phosphorylation of mevalonate (MVA) to yield mevalonate-3-phosphate. Functions in an alternative mevalonate pathway, only present in extreme acidophiles of the Thermoplasmatales order, which passes through mevalonate 3-phosphate rather than mevalonate 5-phosphate.
kcat is 5.3 sec(-1) for ATP as substrate (PubMed:25422158). kcat is 5 sec(-1) for (R)-mevalonate as substrate (PubMed:24914732).
Strong decrease of the affinity for ATP, but almost the same catalytic efficiency compared to the wild-type.
4.6-fold decrease in the catalytic efficiency for ATP, with only a marginal decrease in affinity compared to the wild-type.
Strong decrease of the affinity for ATP and 17-fold decrease of the catalytic efficiency compared to the wild-type.
P-LOOP NTPASE DOMAIN-CONTAINING PROTEIN LPA1 HOMOLOG 1
Phosphorylates mevalonate 3-phosphate to form mevalonate 3,5-bisphosphate. Functions in an alternative mevalonate pathway, only present in extreme acidophiles of the Thermoplasmatales order, which passes through mevalonate 3-phosphate rather than mevalonate 5-phosphate.
Does not demonstrate significant pH dependence in the pH range of 6.5-9.0.
Optimum temperature is 60 degrees Celsius.
DNA helicase RuvA subunit, C-terminal domain
Nascent polypeptide-associated complex domain
Nascent polypeptide-associated complex protein
Contacts the emerging nascent chain on the ribosome.
Homodimer. Interacts with the ribosome. Binds ribosomal RNA.
NH 3 /GLUTAMINE-DEPENDENT NAD + SYNTHETASE
Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
BIFUNCTIONAL NADP PHOSPHATASE/NAD KINASE
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.
BIFUNCTIONAL NMN ADENYLYLTRANSFERASE/NUDIX HYDROLASE
Nicotinamide-nucleotide adenylyltransferase
Belongs to the archaeal NMN adenylyltransferase family.
Nucleoside diphosphate kinase-like domain
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.
PROTEIN SEQUENCE OF 2-10; 71-92 AND 140-150
VITAMIN B12-DEPENDENT RIBONUCLEOTIDE REDUCTASE
R1 subunit of ribonucleotide reductase, N-terminal domain
Vitamin B12-dependent ribonucleoside-diphosphate reductase
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
5'-deoxyadenosylcobalamine (coenzyme B12).
Belongs to the ribonucleoside diphosphate reductase class-2 family.
RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE NEP1
16S rRNA (pseudouridine-N1-)-methyltransferase Nep1
Methyltransferase involved in ribosomal biogenesis. Specifically catalyzes the N1-methylation of the pseudouridine corresponding to position 914 in M.jannaschii 16S rRNA.
Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase NEP1 family.
archaeoglobus fulgidus dsm 4304 superfamily
Methylated DNA-protein cysteine methyltransferase, C-terminal domain
Bifunctional methyltransferase/endonuclease
Probable methylated-DNA--protein-cysteine methyltransferase
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 (By similarity).
In the N-terminal section; belongs to the MGMT family.
In the C-terminal section; belongs to the endonuclease V family.
putative 5-dehydro-2- deoxygluconokinase
Nucleoside kinase with broad substrate specificity. Catalyzes the phosphorylation of a variety of nucleosides to the corresponding nucleoside 5'-mono-phosphate in the presence of phosphate donors and divalent cations. Displays the most efficient activity with guanosine, followed by inosine, cytidine, and adenosine. Negligible enzymatic activity is detected with thymidine, uridine, and 2-deoxyadenosine. ATP is the most efficient phosphate donor, but can also use GTP and ITP. Shows no sugar kinase activity, since it is unable to phosphorylate ribose, fructose-1-phosphate, or fructose-6-phosphate.
Can use Mg(2+) and Co(2+) with equal efficiency in vitro, and to a lesser extent, Mn(2+), but not Ni(2+).
kcat is 0.072 sec(-1) with ATP and guanosine as substrates. kcat is 0.16 sec(-1) with ATP and inosine as substrates. kcat is 0.064 sec(-1) with ATP and cytidine as substrates. kcat is 0.084 sec(-1) with ATP and adenosine as substrates. kcat is 0.27 sec(-1) with GTP and inosine as substrates (at pH 8.0 and 22 degrees Celsius).
0.208 uM for guanosine (at pH 8.0 and 22 degrees Celsius)
0.712 uM for inosine (at pH 8.0 and 22 degrees Celsius)
0.411 uM for cytidine (at pH 8.0 and 22 degrees Celsius)
1.12 uM for adenosine (at pH 8.0 and 22 degrees Celsius)
46.9 uM for ATP (at pH 8.0 and 22 degrees Celsius)
185 uM for GTP (at pH 8.0 and 22 degrees Celsius)
Optimum pH is 6.6. Significant activity is observed over the pH range of 6.4 to 7.8. Enzymatic activity decreases markedly at pH 8.0 and at pH 6.2 and below.
Belongs to the carbohydrate kinase PfkB family.
H/ACA ribonucleoprotein complex, subunit Nop10
Involved in ribosome biogenesis; more specifically in 18S rRNA pseudouridylation and in cleavage of pre-rRNA.
CANCER-RELATED NUCLEOSIDE-TRIPHOSPHATASE
Nucleoside triphosphate phosphohydrolase
Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. May hydrolyze nucleoside diphosphates with lower efficiency.
Prokaryotic type KH domain (KH-domain type II)
Probable transcription termination protein NusA
Participates in transcription termination.
Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal)
DNA-(apurinic or apyrimidinic site) lyase
Catalyzes the excision of an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine = 8-oxoG) from DNA. Also cleaves the DNA backbone at apurinic/apyrimidinic sites (AP sites).
Important for guanine/8-oxoguanine distinction
Catalyzes the excision of an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine = 8-oxoG) from DNA. Also cleaves the DNA backbone at apurinic/apyrimidinic sites (AP sites). Prefers oligomers containing 8-oxoG:C, 8-oxoG:T and 8-oxoG:G base pairs, and is less effective on oligomers containing 8-oxoG:A mispairs.
Aspartate/ornithine carbamoyltransferase
ORNITHINE CARBAMOYLTRANSFERASE, MITOCHONDRIAL
ORNITHINE TRANSCARBAMYLASE, MITOCHONDRIAL
Ornithine carbamoyltransferase, catabolic
Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline.
Belongs to the aspartate/ornithine carbamoyltransferase superfamily. OTCase family.
X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) IN COMPLEX WITH MAGNESIUM
Trehalose-6-phosphate phosphatase-related protein
Removes the phosphate from trehalose 6-phosphate (Tre6P) to produce free trehalose. Also catalyzes the dephosphorylation of para-nitrophenyl phosphate (pNPP), but with lesser efficiency (in vitro).
kcat is 10 sec(-1) and 0.8 sec(-1) for Tre6P and pNPP, respectively (at pH 8 and 50 degrees Celsius).
2.7 mM for Tre6P (at pH 8 and 50 degrees Celsius)
18 mM for pNPP (at pH 8 and 50 degrees Celsius)
Belongs to the trehalose phosphatase family.
PHOSPHATASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_7G00760)-RELATED
Catalyzes the dephosphorylation of the artificial chromogenic substrate p-nitrophenyl phosphate (pNPP).
Belongs to the HAD-like hydrolase superfamily.
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-159 IN COMPLEX WITH COENZYME A
Protease synthase and sporulation negative regulatory protein PAI 1
Involved in the protection against polyamine toxicity by regulating their concentration. Could also be involved in the negative control of sporulation as well as production of degradative enzymes such as alpha-amylase, levansucrase and alkaline phosphatase. Catalyzes the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to an acceptor substrate and release both CoA and the acetylated product. It can use a variety of substrates including spermidine, L-tryptophan, L-leucine, L-lysine, dopamine and tyramine.
kcat is 42 min(-1) for acetyltransferase activity with acetylspermidine as substrate (at pH 8.3). kcat is 31 min(-1) for acetyltransferase activity with AcCoA as substrate (at pH 8.3).
Belongs to the acetyltransferase family.
May have an important role in the acetylation of the polyamine
Phosphoenolpyruvate Carboxykinase, domain 1
Phosphoenolpyruvate Carboxykinase, domain 2
PHOSPHOENOLPYRUVATE CARBOXYKINASE, CYTOSOLIC [GTP]
Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle.
Belongs to the phosphoenolpyruvate carboxykinase [GTP] family.
Proliferating cell nuclear antigen homolog
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.
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.
Pyruvoyl-Dependent Histidine Decarboxylase, subunit B
PYRUVOYL-DEPENDENT ARGININE DECARBOXYLASE
Pyruvoyl-dependent histidine and arginine decarboxylases
arginine decarboxylase, pyruvoyl-dependent
Pyruvoyl-dependent arginine decarboxylase subunit beta
Pyruvoyl-dependent arginine decarboxylase subunit alpha
Binds 1 pyruvoyl group covalently per subunit.
PYRIDOXAL 5'-PHOSPHATE SYNTHASE SUBUNIT SNZ1-RELATED
pyridoxal 5'-phosphate synthase, synthase subunit Pdx1
Pyridoxal 5'-phosphate synthase subunit PdxS
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.
Schiff-base intermediate with D-ribose 5-phosphate
PYRIDOXAL 5'-PHOSPHATE SYNTHASE SUBUNIT SNO
PYRIDOXAL 5'-PHOSPHATE SYNTHASE SUBUNIT SNO1-RELATED
Pyridoxal 5'-phosphate synthase subunit PdxT
Pyridoxal 5'-phosphate synthase glutaminase subunit
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 glutaminase PdxT/SNO family.
May function in recognizing stalled ribosomes, interact with stem-loop structures in stalled mRNA molecules, and effect endonucleolytic cleavage of the mRNA. May play a role in the release non-functional ribosomes and degradation of damaged mRNAs. Has endoribonuclease activity.
The N-terminal domain has the RNA-binding Sm fold. It harbors the endoribonuclease activity.
Belongs to the eukaryotic release factor 1 family. Pelota subfamily.
MUTAGENESIS OF GLU-18; ASP-21; ASP-22 AND GLU-231
Cell division protein pelota-related protein
No effect. Strongly reduced ribonuclease activity; when associated with A-22.
No effect. Strongly reduced ribonuclease activity; when associated with A-21.
Molecular chaperone capable of stabilizing a range of proteins. Seems to fulfill an ATP-independent, HSP70-like function in archaeal de novo protein folding.
Heterohexamer of two alpha and four beta subunits.
Belongs to the prefoldin subunit alpha family.
Molecular chaperone capable of stabilizing a range of proteins. Seems to fulfill an ATP-independent, HSP70-like function in archaeal de novo protein folding (By similarity).
Belongs to the prefoldin subunit beta family.
Phosphoglycerate kinase, N-terminal domain
PHOSPHOGLYCERATE KINASE 1, CHLOROPLASTIC-RELATED
Belongs to the phosphoglycerate kinase family.
Bifunctional phosphoglucose/phosphomannose isomerase
Catalyzes the isomerization of both glucose 6-phosphate and epimeric mannose 6-phosphate at a similar catalytic efficiency.
Inhibited by erythrose 4-phosphate and 6-phosphogluconate.
83 mmol/min/mg enzyme with glucose 6-phosphate as substrate (at 50 degrees Celsius)
57 mmol/min/mg enzyme with fructose 6-phosphate as substrate (at 50 degrees Celsius)
75 mmol/min/mg enzyme with mannose 6-phosphate as substrate (at 50 degrees Celsius)
Optimum temperature is 75 degrees Celsius.
PYRIDOXAL PHOSPHATE PHOSPHATASE YBHA-RELATED
Catalyzes the dephosphorylation of 2-phosphoglycolate.
Belongs to the archaeal SPP-like hydrolase family.
Catalyzes the dephosphorylation of 2-phosphoglycolate. Also has significant, but less efficient, pyrophosphatase activity, since it is able to catalyze the release of phosphate from inorganic pyrophosphate (PPi).
Inhibited by Ca(2+) ions and by high chloride ion concentration. By contrast, low chloride concentration (up to 50 mM) slightly activate the enzyme.
Belongs to the HAD-like hydrolase superfamily. Archaeal SPP-like hydrolase family.
Cleaves H-Pro-AMC as well as a wide spectrum of amino acid substrates and several peptide substrates without a proline at the N-terminus. Proteases F1, F2 and F3 degrade oligopeptides produced by Tricorn (themselves probably produced by the proteasome) yielding free amino acids.
Part of the tricorn proteolytic complex.
Cleaves H-Pro-AMC as well as a wide spectrum of amino acid substrates and several peptide substrates without a proline at the N-terminus. In conjunction with the three factors F1, F2 and F3, Tricorn degrades oligopeptides in a sequential manner, yielding free amino acids (By similarity).
X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF APOPROTEIN AND IN COMPLEXES WITH NICOTINATE MONONUCLEOTIDE AND PRPP
Crystal structure of a zinc ion bound nicotinate phosphoribosyltransferase from Thermoplasma acidophilum.
Berkeley structural genomics center (BSGC)
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH ZINC
Quinolinate phosphoribosyl transferase, N-terminal domain
Nicotinate/Quinolinate PRTase C-terminal domain-like
Nicotinate/Quinolinate PRTase N-terminal domain-like
Putative nicotinate phosphoribosyltransferase
Catalyzes the synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP.
Homodimer. Forms a trimer of dimers in the crystal.
Consists of three domains, an N-terminal domain, a central functional domain, and a unique C-terminal domain containing a zinc knuckle-like motif containing 4 cysteines.
Transiently phosphorylated on a His residue during the reaction cycle. Phosphorylation strongly increases the affinity for substrates and increases the rate of nicotinate D-ribonucleotide production. Dephosphorylation regenerates the low-affinity form of the enzyme, leading to product release.
Belongs to the NAPRTase family. Highly divergent.
Although this protein is stated to be a nicotinate phosphoribosyltransferase, it has not been functionally characterized, and it might be a quinolinate phosphoribosyltransferase (QPRTase).
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.
Heterodimer of a small subunit (PriS) and a large subunit (PriL).
Belongs to the eukaryotic-type primase large 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.
Belongs to the eukaryotic-type primase small subunit family.
Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
PROTEASOME SUBUNIT ALPHA TYPE-7-1-RELATED
N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.
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.
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.
PROTEIN SEQUENCE OF 21-28; 41-54 AND 88-93
X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) IN COMPLEX WITH BETA SUBUNIT
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH BETA SUBUNIT AND T.BRUCEI PA26
STRUCTURE BY ELECTRON MICROSCOPY (6.8 ANGSTROMS) OF THE OPEN-GATE AND CLOSED-GATE CONFORMATIONS
X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) IN COMPLEX WITH THE BETA SUBUNIT AND THE C-TERMINUS OF PAN FROM M.JANNASCHII
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH BETA SUBUNIT AND CHIMERIC PA26 CONSTRUCTS
Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The T.acidophilum proteasome is able to cleave oligopeptides after Tyr, Leu, Phe, and to a lesser extent after Glu and Arg. Thus, displays chymotrypsin-like activity and low level of caspase-like and trypsin-like activities.
39 uM for Suc-LLVY-Amc (at 55 degrees Celsius)
28 nmol/min/mg enzyme with Suc-LLVY-Amc as substrate (at 55 degrees Celsius)
The configuration of the closed gate contains an opening large enough to allow rapid entry of tetrapeptides but able to impede the entry of proteins and longer peptides.
Markedly increases peptidolytic activity. Designated open-gate mutant.
Prevents PAN to associate with the proteasome and stimulate gate opening.
No effect on PAN's ability to stimulate gate opening.
Removed in mature form; by autocatalysis
X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) IN COMPLEX WITH ALPHA SUBUNIT
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ALPHA SUBUNIT AND T.BRUCEI PA26
X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) IN COMPLEX WITH THE ALPHA SUBUNIT AND THE C-TERMINUS OF PAN FROM M.JANNASCHII
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH ALPHA SUBUNIT AND CHIMERIC PA26 CONSTRUCTS
PEPTIDYL-TRNA HYDROLASE 2, MITOCHONDRIAL
The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3
TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3-RELATED
Phosphoribosylformylglycinamidine cyclo-ligase
Phosphoribosyl-aminoimidazole synthetase
PHOSPHORIBOSYLAMINOIMIDAZOLE-SUCCINOCARBOXAMIDE SYNTHASE
Belongs to the SAICAR synthetase family.
Adenylosuccinate Synthetase, subunit A, domain 1
Adenylosuccinate Synthetase, subunit A, domain 2
Adenylosuccinate Synthetase, subunit A, domain 3
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 adenylosuccinate synthetase family.
Phosphoribosylformylglycinamidine synthase, linker domain
PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURL
Formylglycinamide ribonucleotide amidotransferase subunit II
Phosphoribosylformylglycinamidine synthase subunit II
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.
Monomer. Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ and 2 PurS subunits.
PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE
Phosphoribosylformylglycinamidine synthase subunit PurQ
Formylglycinamide ribonucleotide amidotransferase subunit I
Phosphoribosylformylglycinamidine synthase subunit I
Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ and 2 PurS subunits.
Responsible for synthesis of pseudouridine from uracil-54 and uracil-55 in the psi GC loop of transfer RNAs.
Belongs to the pseudouridine synthase Pus10 family.
Heterooligomer of catalytic and regulatory chains.
Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Belongs to the metallo-dependent hydrolases superfamily. DHOase family. Class I DHOase subfamily.
DIHYDROOROTATE DEHYDROGENASE (QUINONE), MITOCHONDRIAL-RELATED
Dihydroorotate dehydrogenase B (NAD(+)), catalytic subunit
Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor.
Heterotetramer of 2 PyrK and 2 PyrD type B subunits.
Belongs to the dihydroorotate dehydrogenase family. Type 1 subfamily.
DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]
Belongs to the purine/pyrimidine phosphoribosyltransferase family.
Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrE subfamily.
Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
Belongs to the OMP decarboxylase family. Type 1 subfamily.
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.
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 reversible phosphorylation of UMP to UDP.
Aspartate carbamoyltransferase regulatory subunit, C-terminal domain
Aspartate carbamoyltransferase regulatory subunit, N-terminal domain
ASPARTATE CARBAMOYLTRANSFERASE REGULATORY CHAIN
Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain
Aspartate carbamoyltransferase, Regulatory-chain, N-terminal domain
Involved in allosteric regulation of aspartate carbamoyltransferase.
Contains catalytic and regulatory chains.
Dihydroorotate dehydrogenase, electron transfer subunit
Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module
DIHYDROOROTATE DEHYDROGENASE B (NAD(+)), ELECTRON TRANSFER SUBUNIT
DIHYDROOROTATE DEHYDROGENASE B (NAD(+)), ELECTRON TRANSFER SUBUNIT-RELATED
Ferredoxin reductase-like, C-terminal NADP-linked domain
Probable dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit
Dihydroorotate oxidase B, electron transfer subunit
Responsible for channeling the electrons from the oxidation of dihydroorotate from the FMN redox center in the PyrD type B subunit to the ultimate electron acceptor NAD(+).
Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
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.
Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Binds 1 S-adenosyl-L-methionine per subunit.
Belongs to the radical SAM superfamily. 7-carboxy-7-deazaguanine synthase family.
DNA double-strand break repair Rad50 ATPase
Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Rad50 controls the balance between DNA end bridging and DNA resection via ATP-dependent structural rearrangements of the Rad50/Mre11 complex.
The two conserved Cys that bind zinc constitute the zinc-hook, which separates the large intramolecular coiled coil regions. The 2 Cys residues coordinate one molecule of zinc with the help of the 2 Cys residues of the zinc-hook of another Rad50 molecule, thereby forming a V-shaped homodimer.
Belongs to the SMC family. RAD50 subfamily.
MEIOTIC RECOMBINATION PROTEIN DMC1/LIM15 HOMOLOG
RECA/RAD51/RADA DNA STRAND-PAIRING FAMILY MEMBER
DNA repair and recombination protein RadA
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.
Belongs to the eukaryotic RecA-like protein family.
Involved in DNA repair and in homologous recombination. Binds and assemble on single-stranded DNA to form a nucleoprotein filament. Hydrolyzes ATP in a ssDNA-dependent manner and promotes DNA strand exchange between homologous DNA molecules (By similarity).
DNA REPAIR AND RECOMBINATION PROTEIN RADB
Involved in DNA repair and in homologous recombination. May regulate the cleavage reactions of the branch-structured DNA. Has a very weak ATPase activity that is not stimulated by DNA. Binds DNA but does not promote DNA strands exchange (By similarity).
Belongs to the eukaryotic RecA-like protein family. RadB subfamily.
EUKARYOTIC PEPTIDE CHAIN RELEASE FACTOR SUBUNIT 1
N-terminal domain of eukaryotic peptide chain release factor subunit 1, ERF1
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 eukaryotic release factor 1 family.
CHROMOSOME TRANSMISSION FIDELITY FACTOR 18
Part of the RFC clamp loader complex which loads the PCNA sliding clamp onto DNA.
Heteromultimer composed of small subunits (RfcS) and large subunits (RfcL).
Belongs to the activator 1 small subunits family. RfcL subfamily.
REPLICATION FACTOR C / DNA POLYMERASE III GAMMA-TAU SUBUNIT
Belongs to the activator 1 small subunits family. RfcS subfamily.
Characterization of NADP-specific L-rhamnose dehydrogenase from the hyperthermophilic archaeon Thermoplasma acidophilum.
SHORT-CHAIN DEHYDROGENASES/REDUCTASES FAMILY MEMBER
Involved in the non-phosphorylated metabolic pathway of L-rhamnose catabolism. Catalyzes the oxidation of L-rhamnose to yield L-rhamnono-1,4-lactone. It can also oxidize L-lyxose and L-mannose, and uses only NADP.
kcat is 1.341 min(-1) for dehydrogenase activity with L-rhamnose as substrate (at pH 7 and 60 degrees Celsius). kcat is 1.426 min(-1) for dehydrogenase activity with L-lyxose as substrate (at pH 7 and 60 degrees Celsius). kcat is 892.9 min(-1) for dehydrogenase activity with L-mannose as substrate (at pH 7 and 60 degrees Celsius).
0.10 mM for NADP (at pH 7 and 60 degrees Celsius)
0.46 mM for L-rhamnose (at pH 7 and 60 degrees Celsius)
1.37 mM for L-lyxose (at pH 7 and 60 degrees Celsius)
6.74 mM for L-mannose (at pH 7 and 60 degrees Celsius)
Belongs to the short-chain dehydrogenases/reductases (SDR) family.
3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE SYNTHASE
Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.
Belongs to the GTP cyclohydrolase II family.
GLYCEROL-3-PHOSPHATE CYTIDYLYLTRANSFERASE
Catalyzes the transfer of the AMP portion of ATP to flavin mononucleotide (FMN) to produce flavin adenine dinucleotide (FAD) coenzyme.
Belongs to the archaeal FAD synthase family.
The crystal structure of the lipopolysaccharide core biosynthesis protein from Thermoplasma volcanium GSS1.
Midwest center for structural genomics (MCSG)
X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) IN COMPLEX WITH AMP
Catalyzes the CTP-dependent phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN).
Belongs to the archaeal riboflavin kinase family.
RIO-type serine/threonine-protein kinase Rio1
Despite the protein kinase domain is proposed to act predominantly as an ATPase (By similarity).
Belongs to the protein kinase superfamily. RIO-type Ser/Thr kinase family.
6,7-DIMETHYL-8-RIBITYLLUMAZINE SYNTHASE DMRL SYNTHASE LUMAZINE SYNTHASE
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.
Belongs to the universal ribosomal protein uL16 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. Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Forms a heptameric L10(L12)2(L12)2(L12)2 complex, where L10 forms an elongated spine to which the L12 dimers bind in a sequential fashion.
Belongs to the universal ribosomal protein uL10 family.
Ribosomal protein L11, C-terminal domain
Ribosomal protein L11/L12, N-terminal domain
39S RIBOSOMAL PROTEIN L11, MITOCHONDRIAL
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 universal ribosomal protein uL11 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 universal ribosomal protein uL13 family.
Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome.
Part of the 50S ribosomal subunit. Forms a cluster with proteins L3 and L24e, part of which may contact the 16S rRNA in 2 intersubunit bridges.
Belongs to the universal ribosomal protein uL14 family.
Belongs to the eukaryotic ribosomal protein eL15 family.
Belongs to the universal ribosomal protein uL15 family.
Belongs to the eukaryotic ribosomal protein eL18 family.
This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.
Part of the 50S ribosomal subunit. Contacts the 5S and 23S rRNAs.
Belongs to the universal ribosomal protein uL18 family.
Binds directly to 23S rRNA. Probably involved in E site tRNA release.
Protein L1 is also a translational repressor protein, it controls the translation of its operon by binding to its mRNA.
Belongs to the universal ribosomal protein uL1 family.
Belongs to the eukaryotic ribosomal protein eL21 family.
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.
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.
Belongs to the universal ribosomal protein uL22 family.
RIBOSOMAL_L23EN DOMAIN-CONTAINING PROTEIN
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 universal ribosomal protein uL23 family.
RIBOSOME BIOGENESIS PROTEIN RLP24-RELATED
Glucocorticoid receptor-like (DNA-binding domain)
Part of the 50S ribosomal subunit. Forms a cluster with proteins L3 and L14.
Belongs to the eukaryotic ribosomal protein eL24 family.
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.
Located at the polypeptide exit tunnel on the outside of the subunit.
Belongs to the universal ribosomal protein uL24 family.
50S RIBOSOMAL PROTEIN L29, CHLOROPLASTIC
60S RIBOSOMAL PROTEIN L35/50S RIBOSOMAL PROTEIN L29
Belongs to the universal ribosomal protein uL29 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 universal ribosomal protein uL2 family.
Ribosomal protein L30, ferredoxin-like fold domain
Belongs to the universal ribosomal protein uL30 family.
Belongs to the eukaryotic ribosomal protein eL31 family.
60S RIBOSOMAL PROTEIN L32 AND DNA-DIRECTED RNA POLYMERASE II, SUBUNIT N
Belongs to the eukaryotic ribosomal protein eL32 family.
Belongs to the eukaryotic ribosomal protein eL43 family. Putative zinc-binding subfamily.
Belongs to the eukaryotic ribosomal protein eL37 family.
Belongs to the eukaryotic ribosomal protein eL39 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 universal ribosomal protein uL3 family.
Belongs to the eukaryotic ribosomal protein eL42 family.
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.
Forms part of the polypeptide exit tunnel.
Belongs to the universal ribosomal protein uL4 family.
This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. May contact the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.
Part of the 50S ribosomal subunit; contacts the 5S rRNA and probably tRNA. Forms a bridge to the 30S subunit in the 70S ribosome.
Belongs to the universal ribosomal protein uL5 family.
Nucleotide sequence of the ribosomal protein genes s4e and L5 in the archaeon Thermoplasma acidophilum.
This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.
Belongs to the universal ribosomal protein uL6 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 eukaryotic ribosomal protein eL8 family.
Ribosomal RNA large subunit methyltransferase E
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 class I-like SAM-binding methyltransferase superfamily. RNA methyltransferase RlmE family.
PRE-RRNA 2'-O-RIBOSE RNA METHYLTRANSFERASE FTSJ3
Ribonuclease H-like superfamily/Ribonuclease H
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.
Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Consists of a catalytic RNA component and at least 4-5 protein subunits.
Belongs to the eukaryotic/archaeal RNase P protein component 1 family.
Belongs to the eukaryotic/archaeal RNase P protein component 4 family.
Ribonuclease Z/Hydroxyacylglutathione hydrolase-like
Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
D-ribose-5-phosphate isomerase (RpiA), lid domain
Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
Belongs to the ribose 5-phosphate isomerase family.
DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC5
DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC5 FAMILY MEMBER
DNA-directed RNA polymerase subunit Rpo10
DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Belongs to the archaeal Rpo10/eukaryotic RPB10 RNA polymerase subunit family.
DNA-directed RNA polymerase subunit Rpo11
Belongs to the archaeal Rpo11/eukaryotic RPB11/RPC19 RNA polymerase subunit family.
Crystal structure of TA1416, DNA-directed RNA polymerase subunit L, from Thermoplasma acidophilum.
DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC1
beta and beta-prime subunits of DNA dependent RNA-polymerase
DNA-directed RNA polymerase subunit Rpo1C
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 RNA polymerase beta' chain family.
DNA-directed RNA polymerase subunit Rpo1N
DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Forms the clamp head domain.
DNA-directed RNA polymerase, subunit 2, domain 6
RNA polymerase alpha subunit dimerisation domain
DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB2
DNA-directed RNA polymerase subunit Rpo2
DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit is involved in DNA promoter recognition.
Belongs to the RNA polymerase beta chain family.
DNA-directed RNA polymerase, insert domain
DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB3
Insert subdomain of RNA polymerase alpha subunit
DNA-directed RNA polymerase subunit Rpo3
Belongs to the archaeal Rpo3/eukaryotic RPB3 RNA polymerase subunit family.
DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC1
DNA-directed RNA polymerase subunit Rpo5
Belongs to the archaeal Rpo5/eukaryotic RPB5 RNA polymerase subunit family.
DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC2
DNA-directed RNA polymerase subunit Rpo6
Belongs to the archaeal Rpo6/eukaryotic RPB6 RNA polymerase subunit family.
Catalytic component of the exosome, which is a complex involved in RNA degradation. Has 3'->5' exoribonuclease activity. Can also synthesize heteromeric RNA-tails.
Component of the archaeal exosome complex. Forms a hexameric ring-like arrangement composed of 3 Rrp41-Rrp42 heterodimers. The hexameric ring associates with a trimer of Rrp4 and/or Csl4 subunits.
Belongs to the RNase PH family. Rrp41 subfamily.
EXOSOME COMPLEX EXONUCLEASE RIBOSOMAL RNA PROCESSING PROTEIN
Non-catalytic component of the exosome, which is a complex involved in RNA degradation. Contributes to the structuring of the Rrp41 active site.
Belongs to the RNase PH family. Rrp42 subfamily.
Eukaryotic type KH-domain (KH-domain type I)
Non-catalytic component of the exosome, which is a complex involved in RNA degradation. Increases the RNA binding and the efficiency of RNA degradation. Confers strong poly(A) specificity to the exosome.
Component of the archaeal exosome complex. Forms a trimer of Rrp4 and/or Csl4 subunits. The trimer associates with a hexameric ring-like arrangement composed of 3 Rrp41-Rrp42 heterodimers.
Involved in the binding of tRNA to the ribosomes.
Belongs to the universal ribosomal protein uS10 family.
40S RIBOSOMAL PROTEIN S14/30S RIBOSOMAL PROTEIN S11
Located on the platform of the 30S subunit.
Belongs to the universal ribosomal protein uS11 family.
With S4 and S5 plays an important role in translational accuracy. Located at the interface of the 30S and 50S subunits.
Belongs to the universal ribosomal protein uS12 family.
30S RIBOSOMAL PROTEIN S13/40S RIBOSOMAL PROTEIN S18
Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement.
Part of the 30S ribosomal subunit. Forms a loose heterodimer with protein S19. Forms two bridges to the 50S subunit in the 70S ribosome.
Belongs to the universal ribosomal protein uS13 family.
Binds 16S rRNA, required for the assembly of 30S particles.
Belongs to the universal ribosomal protein uS14 family. Zinc-binding uS14 subfamily.
Belongs to the universal ribosomal protein uS15 family.
Belongs to the eukaryotic ribosomal protein eS17 family.
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
Belongs to the universal ribosomal protein uS17 family.
May be involved in maturation of the 30S ribosomal subunit.
Belongs to the eukaryotic ribosomal protein eS19 family.
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
Belongs to the universal ribosomal protein uS19 family.
Belongs to the eukaryotic ribosomal protein eS24 family.
Belongs to the eukaryotic ribosomal protein eS31 family.
Belongs to the eukaryotic ribosomal protein eS27 family.
Belongs to the eukaryotic ribosomal protein eS28 family.
Belongs to the universal ribosomal protein uS2 family.
Belongs to the eukaryotic ribosomal protein eS1 family.
Binds the lower part of the 30S subunit head.
Belongs to the universal ribosomal protein uS3 family.
Belongs to the eukaryotic ribosomal protein eS4 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.
With S5 and S12 plays an important role in translational accuracy.
Part of the 30S ribosomal subunit. Contacts protein S5. The interaction surface between S4 and S5 is involved in control of translational fidelity.
Belongs to the universal ribosomal protein uS4 family.
With S4 and S12 plays an important role in translational accuracy.
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.
Belongs to the universal ribosomal protein uS5 family.
Belongs to the eukaryotic ribosomal protein eS6 family.
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center.
Belongs to the universal ribosomal protein uS7 family.
Belongs to the eukaryotic ribosomal protein eS8 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 universal ribosomal protein uS8 family.
Belongs to the universal ribosomal protein uS9 family.
SMALL NUCLEAR RIBONUCLEOPROTEIN F SNRNP-F
Belongs to the snRNP Sm proteins family.
Formate/glycerate dehydrogenase catalytic domain-like
May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine.
Belongs to the adenosylhomocysteinase family.
The complete genome sequence of the methanogenic archaeon ISO4-H5 provides insights in to the methylotrophic lifestyle of a ruminal representative of the methanomassiliicoccales.
RADICAL S-ADENOSYL METHIONINE DOMAIN-CONTAINING PROTEIN 2
S-adenosylmethionine-dependent nucleotide dehydratase
Expression of pVip50 in E.coli (strain MG1655) confers resistance to phage P1; has no effect against T7. Catalyzes the conversion of cytosine triphosphate (CTP) to 3'-deoxy-3',4'-didehydro-CTP (ddhCTP), probably via a SAM-dependent radical mechanism (PubMed:32937646). The modified nucleotide represses transcription from T7 RNA polymerase-directed genes (possibly by acting as chain terminators), strongly suggesting these nucleotides block viral polymerase transcription (By similarity). How this protein allows bacteria to resist viruses that do not encode their own RNA polymerase (such as lambda, P1) is unknown (Probable).
Belongs to the radical SAM superfamily. Viperin family.
Protein transport protein Sec61 subunit beta homolog
Involved in protein export. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex.
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 (By similarity).
Component of the protein translocase complex. Heterotrimer consisting of alpha (SecY), beta (SecG) and gamma (SecE) subunits. Can form oligomers of the heterotrimer (By similarity).
SUGAR FERMENTATION STIMULATION PROTEIN A
Sugar fermentation stimulation protein homolog
STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3
Required for chromosome condensation and partitioning.
Contains large globular domains required for ATP hydrolysis at each terminus and a third globular domain forming a flexible SMC hinge near the middle of the molecule. These domains are separated by coiled-coil structures.
Spermidine synthase, tetramerisation domain
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 spermidine/spermine synthase family.
S-ADENOSYLMETHIONINE DECARBOXYLASE PROENZYME
S-adenosylmethionine decarboxylase beta chain
S-adenosylmethionine decarboxylase alpha chain
Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.
Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers.
Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.
Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.
Schiff-base intermediate with substrate; via pyruvic acid
Proton acceptor; for processing activity
Signal recognition particle, SRP54 subunit, M-domain
SIGNAL RECOGNITION PARTICLE 54 KDA PROTEIN
SIGNAL RECOGNITION PARTICLE 54K PROTEIN SRP54
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.
The SRP-RNC complex is targeted to the cytoplasmic membrane.
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.
Belongs to the GTP-binding SRP family. SRP54 subfamily.
Survival protein SurE-like phosphatase/nucleotidase
PHOSPHATASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G01070)-RELATED
Nucleoside 5'-monophosphate phosphohydrolase
Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Binds 1 divalent metal cation per subunit.
Belongs to the SurE nucleotidase family.
Putative anticodon-binding domain of alanyl-tRNA synthetase (AlaRS)
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 class-II aminoacyl-tRNA synthetase family.
Cysteine-tRNA ligase, C-terminal anti-codon recognition domain
Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases
Belongs to the class-I aminoacyl-tRNA synthetase family.
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
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-II aminoacyl-tRNA synthetase family. 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 class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 2 subfamily.
PHENYLALANINE--TRNA LIGASE ALPHA SUBUNIT
Phenylalanyl-tRNA synthetase alpha subunit
Tetramer of two alpha and two beta subunits.
Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 2 subfamily.
Phenylalanyl-trna Synthetase, Chain B, domain 3
PHENYLALANYL-TRNA SYNTHETASE BETA CHAIN AND LEUCINE-RICH REPEAT-CONTAINING PROTEIN 47
Phenylalanyl-tRNA synthetase beta subunit
Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 2 subfamily.
HISTIDINE--TRNA LIGASE, MITOCHONDRIAL-RELATED
Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain
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 class-I aminoacyl-tRNA synthetase family. IleS type 2 subfamily.
An anticodon-binding domain of class I aminoacyl-tRNA synthetases
Lysine tRNA ligase, stem contact fold domain
Methionyl-tRNA synthetase (MetRS), Zn-domain
Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 1 subfamily.
ASPARAGINE--TRNA LIGASE, MITOCHONDRIAL-RELATED
BIFUNCTIONAL GLUTAMATE/PROLINE--TRNA LIGASE
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 class-II aminoacyl-tRNA synthetase family. ProS type 3 subfamily.
Arginyl tRNA synthetase N-terminal domain
Serine-tRNA synthetase, tRNA binding domain
SERINE--TRNA LIGASE, CYTOPLASMIC-RELATED
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).
Homodimer. The tRNA molecule binds across the dimer.
Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding.
Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily.
THREONINE--TRNA LIGASE, CHLOROPLASTIC/MITOCHONDRIAL 2
Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr).
VALINE--TRNA LIGASE, CHLOROPLASTIC/MITOCHONDRIAL 2
Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
ValRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated threonine is translocated from the active site to the editing site.
Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 2 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 class-I aminoacyl-tRNA synthetase family. TyrS type 4 subfamily.
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Belongs to the transaldolase family. Type 3B subfamily.
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.
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).
THIOREDOXIN-DEPENDENT PEROXIDE REDUCTASE, MITOCHONDRIAL
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
Homodecamer. Pentamer of dimers that assemble into a ring structure.
The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this 1-Cys peroxiredoxin, no C(R) is present and C(P) instead forms a disulfide with a cysteine from another protein or with a small thiol molecule.
Belongs to the peroxiredoxin family. Prx6 subfamily.
Cysteine sulfenic acid (-SOH) intermediate
TRANSCRIPTION INITIATION FACTOR IIB-RELATED
Stabilizes TBP binding to an archaeal box-A promoter. Also responsible for recruiting RNA polymerase II to the pre-initiation complex (DNA-TBP-TFIIB).
THIAMINE BIOSYNTHETIC BIFUNCTIONAL ENZYME
Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Belongs to the thiamine-phosphate synthase family.
Rhodanese/Cell cycle control phosphatase
Sulfur carrier protein ThiS sulfurtransferase
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.
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 213-364
TCP-1-like chaperonin intermediate domain
Molecular chaperone; binds unfolded polypeptides in vitro, and has a weak ATPase activity.
Forms a Heterooligomeric complex of two stacked eight-membered rings.
TRNA(ILE2) 2-AGMATINYLCYTIDINE SYNTHETASE TIAS
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.
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 type IA topoisomerase family.
O-(5'-phospho-DNA)-tyrosine intermediate
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Belongs to the triosephosphate isomerase family.
GLYCO_HYDRO_15 DOMAIN-CONTAINING PROTEIN
Catalyzes the hydrolysis of alpha,alpha-trehalose into two molecules of D-glucose.
Optimum pH is 3.7. Active within a narrow range of acidic pH values (pH 3.2 to 3.9).
Optimum temperature is 50 degrees Celsius.
Belongs to the glycosyl hydrolase 15 family.
Optimum pH is 3.7. Active within a narrow range of acidic pH values (pH 3.3 to 4.0).
Leukotriene A4 hydrolase N-terminal domain
Proteases F1, F2 and F3 degrade oligopeptides produced by Tricorn (themselves probably produced by the proteasome), yielding free amino acids.
Monomer. Part of the Tricorn proteolytic complex.
Monomer. Part of the Tricorn proteolytic complex (By similarity).
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH ZINC IONS
THREE-DIMENSIONAL RECONSTRUCTION FROM ELECTRON MICROGRAPHS
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 27-1071
MUTAGENESIS OF 131-ARG-ARG-132; LEU-184; ARG-414; HIS-746 AND SER-965
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEXES WITH INHIBITORS
MUTAGENESIS OF 131-ARG-ARG-132; LEU-184; ARG-414 AND ALA-643
YVTN repeat-like/Quinoprotein amine dehydrogenase
Tricorn degrades oligopeptides (probably derived from the proteasome) and channels the products to F1, F2 and F3 proteases, which then catalyze the terminal degradation step, yielding free amino acids.
Optimum temperature is 65 degrees Celsius.
Part of the Tricorn proteolytic complex. Assembles to form a hexameric toroid, 20 copies of which may then assemble to form an icosahedral supermolecule of 14.6 MDa.
It is thought that substrate reaches the active site through the seven-bladed beta propeller channel, while products exit via the six-bladed beta propeller channel.
Transition state stabilizer; via amide nitrogen
Decreased catalytic activity towards protein substrates. Retains 10% of wild-type activity towards casein and about 30% towards oxidized insulin beta chain. However, there is no change in the activity for a tripeptide substrate.
Both peptidolytic and proteolytic activities doubled, probably due to the increase of the diameter of the channel for product exit. Retains less than 50% of wild-type activity after modification of the thiol group by maleimide, which decreases the diameter of the exit channel and impairs product exit from the catalytic chamber.
Retains 50% of wild-type activity after modification of the thiol group by maleimide, which decreases the diameter of the access channel and impairs substrate access to the active site. Decreased catalytic activity towards fluorogenic substrate and insulin beta chain prior to any modification or oxidation, probably due to the decrease of the diameter of the substrate access channel. Further decreased catalytic activity towards these substrates after modification with fluorescein-5-maleimide or oxidation by oxidized glutathione; when associated with C-643.
Decreased catalytic activity towards fluorogenic substrate and insulin beta chain prior to any modification or oxidation. Further decreased catalytic activity towards these substrates after modification with fluorescein-5-maleimide or oxidation by oxidized glutathione; when associated with C-414.
Tricorn degrades oligopeptides in a sequential manner.
N2,N2-dimethylguanosine tRNA methyltransferase, C-terminal domain
N 2 ,N 2 -DIMETHYLGUANOSINE TRNA METHYLTRANSFERASE
TRNA (GUANINE(26)-N(2))-DIMETHYLTRANSFERASE
tRNA 2,2-dimethylguanosine-26 methyltransferase
tRNA(guanine-26,N(2)-N(2)) methyltransferase
Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.
Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.
TRNA (CYTIDINE(56)-2'-O)-METHYLTRANSFERASE
tRNA ribose 2'-O-methyltransferase aTrm56
Specifically catalyzes the AdoMet-dependent 2'-O-ribose methylation of cytidine at position 56 in tRNAs.
Tryptophan synthase beta subunit-like PLP-dependent enzymes
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Tetramer of two alpha and two beta chains.
Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain
Nucleoside phosphorylase/phosphoribosyltransferase N-terminal domain
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
Belongs to the anthranilate phosphoribosyltransferase family.
N-(5'-PHOSPHORIBOSYL)ANTHRANILATE ISOMERASE
Pseudouridine synthase I, catalytic domain, C-terminal subdomain
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Belongs to the tRNA pseudouridine synthase TruA family.
Pseudouridine synthase I, catalytic domain, N-terminal subdomain
CENTROMERE/MICROTUBULE BINDING PROTEIN CBF5
H/ACA RIBONUCLEOPROTEIN COMPLEX SUBUNIT DKC1
Could be responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Belongs to the pseudouridine synthase TruB family. Type 2 subfamily.
Could be responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
Belongs to the pseudouridine synthase TruD family.
RIBOSOME BIOGENESIS PROTEIN TSR3 HOMOLOG
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.
MUTAGENESIS OF ARG-111; LYS-114; LEU-115 AND LYS-117
the voltage-gated ion channel (vic) superfamily
POTASSIUM CHANNEL PROTEIN 2-RELATED-RELATED
Calcium-gated potassium channel. Can also be activated by Mg(2+), Mn(2+) and Ni(2+).
Heterooctamer composed of four full-length subunits and four soluble RCK domains.
Reduces levels of the soluble RCK domain.
Does not affect levels of the soluble RCK domain.
Abolishes expression of the soluble RCK domain.
FLAVIN PRENYLTRANSFERASE PAD1, MITOCHONDRIAL
Homo-oligomeric flavin-containing Cys decarboxylases, HFCD
Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3-polyprenylbenzoic acid decarboxylase UbiD. The prenyltransferase is metal-independent and links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms of FMN.
DEHYDRODOLICHYL DIPHOSPHATE SYNTHASE COMPLEX SUBUNIT DHDDS
DEHYDRODOLICHYL DIPHOSPHATE SYNTHASE FAMILY MEMBER
Tritrans,polycis-undecaprenyl-diphosphate synthase (geranylgeranyl-diphosphate specific)
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.
Toxic component of a type II toxin-antitoxin (TA) system. An RNase.
Belongs to the PINc/VapC protein family.
V-TYPE PROTON ATPASE CATALYTIC SUBUNIT A
C-terminal domain of alpha and beta subunits of F1 ATP synthase
N-terminal domain of alpha and beta subunits of F1 ATP synthase
Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal alpha chain is a catalytic subunit.
This protein undergoes a protein self splicing that involves a post-translational excision of the VDE intervening region (intein) followed by peptide ligation.
The intein interrupts the ATP-binding site.
Belongs to the ATPase alpha/beta chains family.
V-type ATP synthase alpha chain, 1st part
V-type ATP synthase alpha chain, 2nd part
ATP-SYNT_AB DOMAIN-CONTAINING PROTEIN-RELATED
Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal beta chain is a regulatory subunit.
Produces ATP from ADP in the presence of a proton gradient across the membrane.
Belongs to the V-ATPase V0D/AC39 subunit family.
Belongs to the V-ATPase D subunit family.
Belongs to the V-ATPase E subunit family.
Belongs to the V-ATPase F subunit family.
Belongs to the V-ATPase 116 kDa subunit family.
Homohexamer. Forms a ring-shaped particle.
Belongs to the AAA ATPase family. CDC48 subfamily.
Bacterial XPD DNA helicase, FeS cluster domain
DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER
REGULATOR OF TELOMERE ELONGATION HELICASE 1
ATP-dependent 5'-3' DNA helicase involved in nucleotide excision repair (NER) of DNA.
Belongs to the helicase family. RAD3/XPD subfamily.
Nicotinate mononucleotide:5,6-dimethylbenzimidazole phosphoribosyltransferase (CobT)
MOLYBDATE/TUNGSTATE-BINDING PROTEIN WTPA
Uncharacterized solute-binding protein Ta1052
Belongs to the bacterial solute-binding protein 1 family. WtpA subfamily.
Belongs to the metallo-dependent hydrolases superfamily. Adenine deaminase family.
Leucine Aminopeptidase, subunit E, domain 1
GANGLIOSIDE INDUCED DIFFERENTIATION ASSOCIATED PROTEIN 2-RELATED
UPF0173 METAL-DEPENDENT HYDROLASE MJ1163-RELATED
UPF0173 METAL-DEPENDENT HYDROLASE TM_1162
UPF0173 metal-dependent hydrolase PTO1118
Putative sulfur carrier protein Ta1170/Ta1414
Belongs to the sulfur carrier protein TusA family.
3-HYDROXY-3-METHYLGLUTARYL COENZYME A SYNTHASE
Belongs to the thiolase-like superfamily. UPF0219 family.
Thioesterase/thiol ester dehydrase-isomerase
Belongs to the thioesterase PaaI family.
Putative quercetin 2,3-dioxygenase Ta0133
lambda repressor-like DNA-binding domains
Putative HTH-type transcriptional regulatory protein Ta1363
Thymidylate synthase-complementing protein Thy1
FIBRONECTIN TYPE 3 AND ANKYRIN REPEAT DOMAINS PROTEIN 1
Putative HTH-type transcriptional regulatory protein TV0294
NICOTINAMIDE-NUCLEOTIDE AMIDOHYDROLASE PNCC
Molybdenum cofactor biosynthesis proteins
Uncharacterized solute-binding protein TV0544
Putative HTH-type transcriptional regulatory protein PTO0557
UPF0173 metal-dependent hydrolase Ta0764
UPF0173 metal-dependent hydrolase TV0864