NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]
2-oxoglutarate carboxylase large subunit
2-oxoglutarate carboxylase alpha subunit
Heterohexadecamer of 8 large subunits and 8 small subunits.
Glutathione synthetase ATP-binding domain-like
2-oxoglutarate carboxylase small subunit
Type I PLP-dependent aspartate aminotransferase-like (Major domain)
Probable aspartate/prephenate aminotransferase
Catalyzes the reversible conversion of aspartate and 2-oxoglutarate to glutamate and oxaloacetate. Can also transaminate prephenate in the presence of aspartate.
Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.
Important for prephenate aminotransferase activity
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 443-824 IN COMPLEX WITH ATP ANALOG
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 428-824 IN COMPLEXES WITH ATP; CTP; TRNA AND MAGNESIUM
inorganic pyrophosphatase (n-terminal core)
Poly A polymerase C-terminal region-like
tRNA nucleotidyltransferase involved in the synthesis of the tRNA CCA terminus. Adds the terminal adenosine residue to tRNA (PubMed:11701927, PubMed:25914059). Can incorporate CMP into tRNA ending with C74C75 (tRNACC), with very weak efficiency (PubMed:25914059).
kcat is 0.10 min(-1) for incorporation of AMP into tRNACC. kcat is 0.00015 min(-1) for incorporation of CMP into tRNACC.
Adopts a seahorse-like shape and consists of four domains: head, neck, body, and tail.
Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family.
ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT ALPHA
ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT ALPHA, CHLOROPLASTIC
Acetyl-CoA carboxylase carboxyltransferase subunit alpha
Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA.
Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD).
ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT BETA, CHLOROPLASTIC
Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta
Acetyl-CoA carboxylase carboxyltransferase subunit beta
Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
4'-phosphopantetheinyl transferase domain
Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Belongs to the P-Pant transferase superfamily. AcpS family.
Carrier of the growing fatty acid chain in fatty acid biosynthesis.
4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Belongs to the acyl carrier protein (ACP) family.
3-HYDROXY-5-PHOSPHONOOXYPENTANE-2,4-DIONE THIOLASE-RELATED
2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase
Catalyzes a transaldol reaction between 6-deoxy-5-ketofructose 1-phosphate (DKFP) and L-aspartate semialdehyde (ASA) with an elimination of hydroxypyruvaldehyde phosphate to yield 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate (ADH). Plays a key role in an alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ), which is involved in the canonical pathway for the biosynthesis of aromatic amino acids.
Belongs to the DeoC/FbaB aldolase family. ADHS subfamily.
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH CALCIUM
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN COMPLEX WITH RNA
Ribonuclease H-like superfamily/Ribonuclease H
A DNA-guided RNA endonuclease. Uses short ssDNA sequences as guides (gDNA) to bind complementary target strands, resulting in cleavage of the target RNA. The cleavage site is 10 nucleotides downstream of the residue base paired with the 5'-end of the gDNA (PubMed:16061186). Binds ssDNA better than ssRNA, binds dsDNA and DNA-RNA hybrids but does not bind dsRNA (PubMed:16061186). A 2 nucleotide 3'-overhang (possibly on the guide strand) may help load nucleic acids into the complex (PubMed:17027504) (Probable).
Mg(2+) is the preferred cation for DNA-guided cleavage while Mn(2+) supports both DNA- and RNA-guided cleavage of an RNA target. Ca(2+), which is found in the structure, does not support cleavage (PubMed:16061186). Cleavage probaby requires 2 divalent metal cations (By similarity).
Optimum temperature is 55 degrees Celsius.
Has 4 domains; N-terminal, PAZ, Mid and PIWI. The N-terminal and PAZ domain are joined by linker 1, the PAZ and Mid domain are joined by linker 2. The domains assemble in 2 lobes; the PAZ lobe consists of the N-terminal, L1, PAZ and L2 domains, while the PIWI lobe has the Mid and PIWI domains. The PIWI box is exposed on the surface of the protein. The PIWI domain assumes an RNase H fold and has the catalytic residues (PubMed:16061186, PubMed:17027504, PubMed:17130125). The N-terminal and PAZ domains are relatively mobile and move further apart when in complex with RNA (PubMed:17027504, PubMed:17130125).
In the structure with dsRNA, the nucleic acid is not found in the expected channel, only the two 3'-terminal residues interact in a possibly physiological manner with the protein.
Belongs to the argonaute family. Long pAgo subfamily.
No change in DNA-guided RNA cleavage or ssRNA binding, decreased recognition of the 3'-overhang of a dsRNA duplex.
Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
Catalyzes the interconversion of L-alanine and D-alanine.
Leucine Aminopeptidase, subunit E, domain 1
Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides (By similarity).
Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
the ammonium transporter channel (amt) family
Involved in the uptake of ammonium/ammonia (NH(4)(+)/NH(3)).
Belongs to the ammonia transporter channel (TC 1.A.11.2) family.
P-loop containing nucleotide triphosphate hydrolases
P-loop containing nucleoside triphosphate hydrolases
Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP.
Belongs to the Mrp/NBP35 ATP-binding proteins family.
COFACTOR-INDEPENDENT PHOSPHOGLYCERATE MUTASE
Probable 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.
N-ACETYLGLUTAMATE SYNTHASE, MITOCHONDRIAL
N-acetyl-L-glutamate 5-phosphotransferase
Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Belongs to the acetylglutamate kinase family. ArgB subfamily.
N-ACETYL-GAMMA-GLUTAMYL-PHOSPHATE REDUCTASE, CHLOROPLASTIC-RELATED
N-ACETYL-GAMMA-GLUTAMYL-PHOSPHATE REDUCTASE, CHLOROPLASTIC-RELATED-RELATED
Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain
N-acetyl-gamma-glutamyl-phosphate reductase
N-acetyl-glutamate semialdehyde dehydrogenase
Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
Belongs to the NAGSA dehydrogenase family. Type 1 subfamily.
Crystal structure of acetylornithine aminotransferase from Aquifex aeolicus vf5.
RIKEN structural genomics initiative (RSGI)
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-376 IN COMPLEX WITH PLP
ACETYLORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL
Binds 1 pyridoxal phosphate per subunit.
May also have succinyldiaminopimelate aminotransferase activity, thus carrying out the corresponding step in lysine biosynthesis.
Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily.
L-amino peptidase D-ALA esterase/amidase
ARGININE BIOSYNTHESIS BIFUNCTIONAL PROTEIN ARGJ
ARGININE BIOSYNTHESIS BIFUNCTIONAL PROTEIN ARGJ, MITOCHONDRIAL
Arginine biosynthesis bifunctional protein ArgJ alpha chain
Arginine biosynthesis bifunctional protein ArgJ beta chain
Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.
Heterotetramer of two alpha and two beta chains.
Some bacteria possess a monofunctional ArgJ, i.e. capable of catalyzing only the fifth step of the arginine biosynthetic pathway.
Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole
Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
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.
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.
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS
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.
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SHIKIMATE AND NADP
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).
kcat is 55.5 sec(-1) for dehydrogenase activity (at pH 9 and 25 degrees Celsius).
42.4 uM for shikimate (at pH 9 and 25 degrees Celsius)
42.4 uM for NADP (at pH 9 and 25 degrees Celsius)
AroE is dependent on the hydrogen ion concentration of the environment. A low pH environment favors the formation of SA and NADP, whereas a high pH condition favors the formation of DHSA and NADPH.
Belongs to the shikimate dehydrogenase family.
Crystal structure of shikimate kinase (aq_2177) from Aquifex aeolicus VF5.
Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
ARSENICAL PUMP-DRIVING ATPASE ARSENITE-TRANSLOCATING ATPASE
Putative arsenical pump-driving ATPase 1
Anion-transporting ATPase. Catalyzes the extrusion of arsenite (By similarity).
Putative arsenical pump-driving ATPase 2
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.
Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains.
ATP synthase alpha/beta chain, C-terminal domain
ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL
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 alpha chain is a regulatory subunit.
Belongs to the ATPase alpha/beta chains family.
ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL
Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
N-terminal domain of the delta subunit of the F1F0-ATP synthase
ATP SYNTHASE SUBUNIT DELTA, CHLOROPLASTIC
F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.
F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains.
Belongs to the ATPase delta chain family.
F0F1 ATP synthase delta/epsilon subunit, N-terminal
ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL
Epsilon subunit of F1F0-ATP synthase N-terminal domain
Produces ATP from ADP in the presence of a proton gradient across the membrane.
F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c.
Belongs to the ATPase epsilon chain family.
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
ATP synthase, gamma subunit, helix hairpin domain
Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Belongs to the ATPase gamma chain family.
ATP SYNTHASE LIPID-BINDING PROTEIN, MITOCHONDRIAL
Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.
Reversibly protonated during proton transport
SOLUBLE LYTIC MUREIN TRANSGLYCOSYLASE-RELATED
Putative outer membrane protein assembly factor BamD
Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE
7,8-diamino-pelargonic acid aminotransferase
Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only aminotransferase known to utilize SAM as an amino donor.
Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. BioA subfamily.
Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAM
Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine.
Belongs to the radical SAM superfamily. Biotin synthase family.
ATP-dependent dethiobiotin synthetase BioD
Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
Belongs to the dethiobiotin synthetase family.
CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE
Putative 8-amino-7-oxononanoate synthase
Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.
Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. BioF subfamily.
Catalyzes the transformation of pimelate into pimeloyl-CoA with concomitant hydrolysis of ATP to AMP.
Crystal structure of myo-inositol-1(or 4)-monophosphatase (aq_1983) from Aquifex aeolicus VF5.
Fructose-1,6-Bisphosphatase, subunit A, domain 1
Phosphatase with broad specificity; it can dephosphorylate fructose 1,6-bisphosphate, and both D and L isomers of inositol-1-phosphate (I-1-P).
Belongs to the inositol monophosphatase superfamily. FBPase class 4 family.
Carbamoyl-phosphate synthase small subunit, N-terminal domain
CARBAMOYL-PHOSPHATE SYNTHASE ARGININE-SPECIFIC SMALL CHAIN
Carbamoyl phosphate synthetase, small subunit N-terminal domain
Carbamoyl-phosphate synthase small chain
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
Carbamoyl-phosphate synthase large chain, N-terminal section
Carbamoyl-phosphate synthetase ammonia chain
Binds 2 magnesium or manganese ions per subunit.
CarB is split into two genes in A.aeolicus (AQ_1172 and AQ_2101).
Carbamoyl-phosphate synthase large chain, C-terminal section
Crystal structure of uncharacterized conserved protein from Aquifex aeolicus.
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-316
CRISPR-associated endonuclease Cas1, C-terminal domain
CRISPR-associated endonuclease Cas1, N-terminal domain
CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Acts as a dsDNA endonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.
Homodimer, forms a heterotetramer with a Cas2 homodimer.
Belongs to the CRISPR-associated endonuclease Cas1 family.
X-RAY CRYSTALLOGRAPHY (3.31 ANGSTROMS) IN COMPLEXES WITH CTP; TRNA AND MAGNESIUM
tRNA nucleotidyltransferase involved in the synthesis of the tRNA CCA terminus. Adds the two cytidine residues to tRNA.
Reduces the CMP incorporation at position 74 of the tRNA, but does not affect the CMP incorporation at position 75.
Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel.
Heptamer of 7 subunits arranged in a ring. Interacts with the chaperonin GroEL.
TCP-1-like chaperonin intermediate domain
60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL
Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
Forms a cylinder of 14 subunits composed of two heptameric rings stacked back-to-back. Interacts with the co-chaperonin GroES.
Belongs to the chaperonin (HSP60) family.
2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain
Catalyzes the condensation of pyruvate and acetyl-coenzyme A to form (R)-citramalate.
Belongs to the alpha-IPM synthase/homocitrate synthase family.
NICOTINAMIDE-NUCLEOTIDE AMIDOHYDROLASE PNCC
Molybdenum cofactor biosynthesis proteins
Catalyzes both citrate generation and citrate cleavage. Part of a reversible tricarboxylic acid (TCA) cycle that can fix carbon dioxide autotrophically and may represent an ancestral mode of the conventional reductive TCA (rTCA) cycle. The direction is controlled by the available carbon source(s).
kcat is 0.931 sec(-1) with citrate as substrate. kcat is 1.34 sec(-1) with CoA as substrate. kcat is 250 sec(-1) with acetyl-CoA as substrate.
1.11 umol/min/mg enzyme toward citrate for the reverse reaction
1.60 umol/min/mg enzyme toward CoA for the reverse reaction
298 umol/min/mg enzyme toward acetyl-CoA for the forward reaction
Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity).
Homohexamer. The oligomerization is ATP-dependent (By similarity).
The Clp repeat (R) domain probably functions as a substrate-discriminating domain, recruiting aggregated proteins to the ClpB hexamer and/or stabilizing bound proteins. The NBD2 domain is responsible for oligomerization, whereas the NBD1 domain stabilizes the hexamer probably in an ATP-dependent manner. The movement of the coiled-coil domain is essential for ClpB ability to rescue proteins from an aggregated state, probably by pulling apart large aggregated proteins, which are bound between the coiled-coils motifs of adjacent ClpB subunits in the functional hexamer (By similarity).
ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT
Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Fourteen ClpP subunits assemble into 2 heptameric rings which stack back to back to give a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes.
ClpX chaperone, C4-type zinc finger domain
ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL
ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED
Glucocorticoid receptor-like (DNA-binding domain)
ATP-dependent Clp protease ATP-binding subunit ClpX
ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.
Component of the ClpX-ClpP complex. Forms a hexameric ring that, in the presence of ATP, binds to fourteen ClpP subunits assembled into a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes.
Bifunctional chorismate mutase/prephenate dehydratase
Chorismate mutase-prephenate dehydratase
Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate.
Essential for prephenate dehydratase activity
Pantetheine-phosphate adenylyltransferase
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
BIFUNCTIONAL COENZYME A SYNTHASE-RELATED
Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
A monovalent cation. Ammonium or potassium.
Belongs to the type III pantothenate kinase 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.
Belongs to the peptide transporter carbon starvation (CstA) (TC 2.A.114) family.
RIBOSOMAL PROTEIN L25/GLN-TRNA SYNTHETASE, ANTI-CODON-BINDING DOMAIN-CONTAINING PROTEIN
Not known. A homolog of ribosomal protein bL25, it is missing the N-terminal domain which binds 5S rRNA. In vitro does not bind 5S rRNA.
Binds 1 heme c group covalently per subunit.
lambda repressor-like DNA-binding domains
Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.
Tryptophan synthase beta subunit-like PLP-dependent enzymes
Belongs to the cysteine synthase/cystathionine beta-synthase family.
Probable inorganic carbon transporter subunit DabA
Part of an energy-coupled inorganic carbon pump.
Belongs to the inorganic carbon transporter (TC 9.A.2) DabA family.
L-GLUTAMINE--4-(METHYLSULFANYL)-2-OXOBUTANOATE AMINOTRANSFERASE
Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate.
Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. LL-diaminopimelate aminotransferase subfamily.
4-HYDROXY-TETRAHYDRODIPICOLINATE SYNTHASE
Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB.
4-HYDROXY-TETRAHYDRODIPICOLINATE REDUCTASE 1, CHLOROPLASTIC-RELATED
4-hydroxy-tetrahydrodipicolinate reductase
Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction.
DIAMINOPIMELATE EPIMERASE, CHLOROPLASTIC
Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
Belongs to the diaminopimelate epimerase family.
Could be important to modulate the pK values of the two catalytic cysteine residues
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.
Southeast collaboratory for structural genomics (SECSG)
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.
Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate.
METHYLTETRAHYDROFOLATE:HOMOCYSTEINE METHYLTRANSFERASE RELATED
Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Belongs to the uroporphyrinogen decarboxylase family.
Belongs to the D-alanine--D-alanine ligase family.
Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (By similarity).
Belongs to the polypeptide deformylase family.
Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.
Schiff-base intermediate with acetaldehyde
GTPase that plays an essential role in the late steps of ribosome biogenesis.
Associates with the 50S ribosomal subunit.
Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. EngA (Der) GTPase family.
Aspartate-beta-semialdehyde dehydrogenase
Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate.
Belongs to the aspartate-semialdehyde dehydrogenase family.
Belongs to the archaeal-type DHQ synthase family.
BIFUNCTIONAL IPC TRANSFERASE AND DIPP SYNTHASE
1L-myo-inositol-1-phosphate cytidylyltransferase
CDP-L-myo-inositol myo-inositolphosphotransferase
Di-myo-inositol-1,3'-phosphate-1'-phosphate synthase
Involved in biosynthesis of di-myo-inositol phosphate (DIP), a widespread organic solute in microorganisms adapted to hot environments. Catalyzes the condensation of CTP and L-myo-inositol-1-phosphate into CDP-L-myo-inositol, as well as the biosynthesis of di-myo-inositol-1,3'-phosphate-1'-phosphate (DIPP) from CDP-L-myo-inositol and L-myo-inositol-1-phosphate.
In the N-terminal section; belongs to the MobA family.
In the C-terminal section; belongs to the CDP-alcohol phosphatidyltransferase class-I family.
ALPHA/BETA-HYDROLASES SUPERFAMILY PROTEIN
Belongs to the dienelactone hydrolase family.
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 76-399
CHROMOSOMAL REPLICATION INITIATOR PROTEIN DNAA
Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids (By similarity).
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-405 IN COMPLEX WITH ZINC
DNA primase, catalytic core, N-terminal domain
RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
Contains an N-terminal zinc-binding domain, a central core domain that contains the primase activity, and a C-terminal DnaB-binding domain.
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
By stress conditions e.g. heat shock (By similarity).
Belongs to the heat shock protein 70 family.
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.
5' to 3' exonuclease, C-terminal subdomain
CHROMOSOME TRANSMISSION FIDELITY FACTOR 18
Polydeoxyribonucleotide synthase [NAD(+)]
DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
Manganese or magnesium. Has higher activity with manganese.
Belongs to the NAD-dependent DNA ligase family. LigA subfamily.
Belongs to the DNA polymerase type-A family.
Bacterial DNA polymerase III alpha subunit, thumb domain
DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain is the DNA polymerase (By similarity).
DNA polymerase III contains a core (composed of alpha, epsilon and theta chains) that associates with a tau subunit. This core dimerizes to form the PolIII' complex. PolIII' associates with the gamma complex (composed of gamma, delta, delta', psi and chi chains) and with the beta chain to form the complete DNA polymerase III complex (By similarity).
Belongs to the DNA polymerase type-C family. DnaE subfamily.
DNA polymerase III beta sliding clamp subunit
Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP-independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of replication as well as for processivity of DNA replication.
Forms a ring-shaped head-to-tail homodimer around DNA which binds and tethers DNA polymerases and other proteins to the DNA. The DNA replisome complex has a single clamp-loading complex (3 tau and 1 each of delta, delta', psi and chi subunits) which binds 3 Pol III cores (1 core on the leading strand and 2 on the lagging strand) each with a beta sliding clamp dimer. Additional proteins in the replisome are other copies of gamma, psi and chi, Ssb, DNA helicase and RNA primase.
Belongs to the beta sliding clamp family.
DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'-5' exonuclease (By similarity).
Binds 2 divalent metal cations. Magnesium or manganese.
Crystal structure of D-Tyr-tRNA(tyr) deacylase from Aquifex aeolicus.
An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. 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 and helps enforce protein L-homochirality.
A Gly-cisPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of L-amino acids.
Gly-cisPro motif, important for rejection of L-amino acids
TRNA-DIHYDROURIDINE(47) SYNTHASE [NAD(P)(+)]-LIKE
Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines.
DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDOHYDROLASE
This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
1-DEOXY-D-XYLULOSE 5-PHOSPHATE REDUCTOISOMERASE
1-DEOXY-D-XYLULOSE 5-PHOSPHATE REDUCTOISOMERASE, CHLOROPLASTIC
1-deoxy-D-xylulose-5-phosphate reductoisomerase, C-terminal domain
1-deoxyxylulose-5-phosphate reductoisomerase
2-C-methyl-D-erythritol 4-phosphate synthase
Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
1-D-DEOXYXYLULOSE 5-PHOSPHATE SYNTHASE-RELATED
1-DEOXY-D-XYLULOSE-5-PHOSPHATE SYNTHASE, CHLOROPLASTIC
Thiamin diphosphate-binding fold (THDP-binding)
Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
Binds 1 thiamine pyrophosphate per subunit.
Belongs to the transketolase family. DXPS subfamily.
Elongation Factor G (Translational Gtpase), domain 3
RIBOSOME-RELEASING FACTOR 2, MITOCHONDRIAL
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity).
Belongs to the 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.
ELONGATION FACTOR P (EF-P) FAMILY PROTEIN
Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase (By similarity).
Belongs to the elongation factor P family.
Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
DNA helicase RuvA subunit, C-terminal domain
Elongation factor Ts, dimerisation domain
Elongation factor Ts (EF-Ts), dimerisation domain
Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome (By similarity).
Involved in Mg(2+) ion dislocation from EF-Tu
Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
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.
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.
Necessary for normal cell division and for the maintenance of normal septation.
Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. EngB GTPase family.
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
The covalent binding to the substrate causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein.
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.
ELONGATION FACTOR P--(R)-BETA-LYSINE LIGASE
Elongation factor P--(R)-beta-lysine ligase homolog
Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN TERNARY COMPLEX WITH A GTP ANALOG AND RNA
Prokaryotic type KH domain (KH-domain type II)
An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism (By similarity). The GTPase is stimulated about 6-fold in the presence of a 12 nucleotide 16S rRNA C-terminal fragment. Mutations in the rRNA sequence obviate stimulation. RNA-binding depends on GTP-binding by the GTPase domain. May function as a checkpoint for assembly of the 30S ribosomal subunit.
Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Era GTPase family.
5'-3' exonuclease acting preferentially on double-stranded DNA.
Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB (By similarity).
The accessory proteins ExbB and ExbD seem to form a complex with TonB.
EXBD MEMBRANE COMPONENT OF PMF-DRIVEN MACROMOLECULE IMPORT SYSTEM
Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates.
SEDOHEPTULOSE-1,7-BISPHOSPHATASE, CHLOROPLASTIC
D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1
Crystal structure of aq_1716 from Aquifex aeolicus VF5.
3-OXOACYL-(ACYL-CARRIER-PROTEIN) REDUCTASE
3-oxoacyl-[acyl-carrier-protein] reductase FabG
3-ketoacyl-acyl carrier protein reductase
Beta-Ketoacyl-acyl carrier protein reductase
Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis.
Belongs to the short-chain dehydrogenases/reductases (SDR) family.
Crystal structure of 3-oxoacyl-[acyl-carrier-protein] synthase III from Aquifex aeolicus VF5.
3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE
3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE III, CHLOROPLASTIC
Beta-ketoacyl-[acyl-carrier-protein] synthase III
3-oxoacyl-[acyl-carrier-protein] synthase 3
3-oxoacyl-[acyl-carrier-protein] synthase III
Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH.
Belongs to the thiolase-like superfamily. FabH family.
Crystal structure of enoyl-[acyl-carrier-protein] reductase (NADH) from Aquifex aeolicus VF5.
ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH], CHLOROPLASTIC
Enoyl-[acyl-carrier-protein] reductase [NADH] FabI
Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity).
Belongs to the short-chain dehydrogenases/reductases (SDR) family. FabI subfamily.
(3R)-HYDROXYMYRISTOYL-[ACYL-CARRIER-PROTEIN] DEHYDRATASE
3-HYDROXYACYL-[ACYL-CARRIER-PROTEIN] DEHYDRATASE
Thioesterase/thiol ester dehydrase-isomerase
3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ
Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Belongs to the thioester dehydratase family. FabZ subfamily.
Necessary for formate dehydrogenase activity.
Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Belongs to the 2Fe2S plant-type ferredoxin family.
Belongs to the 2Fe2S Shethna-type ferredoxin family.
NA(+)-TRANSLOCATING NADH-QUINONE REDUCTASE SUBUNIT
May be involved in the assembly of iron-sulfur clusters (Isc-Fd).
Optimum temperature is 106 degrees Celsius at pH 7. Highly thermostable.
Belongs to the adrenodoxin/putidaredoxin family.
f41 fragment of flagellin, N-terminal domain
Flagellar export chaperone, C-terminal domain
Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.
Belongs to the bacterial flagellin family.
Low-potential electron donor to a number of redox enzymes.
FLAGELLA BASAL BODY P-RING FORMATION PROTEIN FLGA
Involved in the assembly process of the P-ring formation. It may associate with FlgF on the rod constituting a structure essential for the P-ring assembly or may act as a modulator protein for the P-ring assembly (By similarity).
Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body (By similarity).
The basal body constitutes a major portion of the flagellar organelle and consists of a number of rings mounted on a central rod. In Gram-negative bacteria, at least four rings, L, P, S and M are present, whereas Gram-positive bacteria lack the L and P rings. The rod consists of about 26 subunits of FlgG in the distal portion, and FlgB, FlgC and FlgF build up the proximal portion of the rod with about 6 subunits each. Rod assembly occurs by export via the flagellum-specific pathway of its constituent proteins and by their incorporation into the rod structure in the probable order of FlgB, FlgC, FlgF and FlgG. Another protein, FliE, also assembles onto the stable rod structure (By similarity).
Belongs to the flagella basal body rod proteins family.
The basal body constitutes a major portion of the flagellar organelle and consists of four rings (L,P,S, and M) mounted on a central rod. The rod consists of about 26 subunits of FlgG in the distal portion, and FlgB, FlgC and FlgF are thought to build up the proximal portion of the rod with about 6 subunits each (By similarity).
Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
The basal body constitutes a major portion of the flagellar organelle and consists of four rings (L,P,S, and M) mounted on a central rod.
FLAGELLAR P-RING PERIPLASMIC PROTEIN FLGI
FLAGELLAR BIOSYNTHESIS PROTEIN FLHA-RELATED
FLAGELLAR EXPORT PROTEIN, MEMBRANE FLHA SUBUNIT-RELATED
Required for formation of the rod structure of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin (By similarity).
Belongs to the FHIPEP (flagella/HR/invasion proteins export pore) family.
Required for formation of the rod structure in the basal body of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin (By similarity).
Belongs to the type III secretion exporter family.
Flagellar FlhF biosynthesis protein, N domain
SIGNAL RECOGNITION PARTICLE RECEPTOR SUBUNIT ALPHA
Necessary for flagellar biosynthesis. May be involved in translocation of the flagellum (By similarity).
Required for the morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end (By similarity).
FLAGELLAR HOOK-BASAL BODY COMPLEX PROTEIN FLIE
The M ring may be actively involved in energy transduction.
The basal body constitutes a major portion of the flagellar organelle and consists of five rings (E,L,P,S, and M) mounted on a central rod. The M ring is integral to the inner membrane of the cell and may be connected to the flagellar rod via the S ring. The S (supramembrane ring) lies just distal to the M ring. The L and P rings lie in the outer membrane and the periplasmic space, respectively (By similarity).
FliG is one of 2 proteins (FliG, FliN) that might form the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity).
Probable catalytic subunit of a protein translocase for flagellum-specific export, or a proton translocase involved in local circuits at the flagellum.
Controls the rotational direction of flagella during chemotaxis.
FliM is one of 2 proteins (FliG, FliN) that might form a switch complex that is proposed to be located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation (Potential).
Plays a role in the flagellum-specific transport system.
Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Na(+) is not transported, but it plays an essential structural role and its presence is essential for fluoride channel function.
Belongs to the fluoride channel Fluc/FEX (TC 1.A.43) family.
METHIONYL-TRNA FORMYLTRANSFERASE, MITOCHONDRIAL
Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
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.
Ferredoxin oxidoreductase 1 subunit ForD
Ferredoxin oxidoreductase 1 subunit delta
Heterotetramer of one alpha, one beta, one delta and one gamma chain.
Ferredoxin oxidoreductase 2 subunit ForD
Ferredoxin oxidoreductase 2 subunit delta
X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) OF 405-634
the mitochondrial inner membrane i-aaa protease complex (mimp) family
ATP-DEPENDENT ZINC METALLOPROTEASE YME1L1
Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
The isolated protease domain (residues 405-634) forms a stable hexamer.
In the central section; belongs to the AAA ATPase family.
In the C-terminal section; belongs to the peptidase M41 family.
Signal recognition particle SRP54, nucleotide-binding domain
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.
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-331 IN COMPLEX WITH GDP
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1-331
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.
Structural study of Project ID aq_1065 from Aquifex aeolicus VF5.
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH NAD
GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE
GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 2
NAD-dependent glyceraldehyde-3-phosphate dehydrogenase
Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG.
Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT A
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln) (By similarity).
Belongs to the amidase family. GatA subfamily.
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).
GLUTAMYL-TRNA GLN AMIDOTRANSFERASE SUBUNIT B MITOCHONDRIAL AND PROKARYOTIC PET112-RELATED
GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT B, MITOCHONDRIAL
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln) (By similarity).
Belongs to the GatB/GatE family. GatB subfamily.
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Glu-tRNAGln amidotransferase C subunit, N-terminal domain
GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT C, MITOCHONDRIAL
Glutamyl-tRNA(Gln) amidotransferase subunit C
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C
Tetrahydrobiopterin biosynthesis enzymes-like
Toroid-shaped homodecamer, composed of two pentamers of five dimers.
Belongs to the GTP cyclohydrolase I family.
GLYCINE CLEAVAGE SYSTEM H PROTEIN, MITOCHONDRIAL
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.
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.
Aminomethyltransferase beta-barrel domains
Aminomethyltransferase beta-barrel domain
The glycine cleavage system catalyzes the degradation of glycine.
GRANULE-BOUND STARCH SYNTHASE 1, CHLOROPLASTIC/AMYLOPLASTIC
STARCH SYNTHASE 1, CHLOROPLASTIC/AMYLOPLASTIC
UDP-Glycosyltransferase/glycogen phosphorylase
Synthesizes alpha-1,4-glucan chains using ADP-glucose.
Belongs to the glycosyltransferase 1 family. Bacterial/plant glycogen synthase subfamily.
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.
Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
GLUCOSAMINE--FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE, ISOMERIZING
GLUTAMINE--FRUCTOSE-6-PHOSPHATE TRANSAMINASE (ISOMERIZING)
N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Glutamine--fructose-6-phosphate aminotransferase [isomerizing]
L-glutamine--D-fructose-6-phosphate amidotransferase
Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
UDP-N-acetylglucosamine pyrophosphorylase
N-acetylglucosamine-1-phosphate uridyltransferase
Glucosamine-1-phosphate N-acetyltransferase
Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family.
In the C-terminal section; belongs to the transferase hexapeptide repeat family.
Glutamine synthetase/guanido kinase, catalytic domain
Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia.
The activity of this enzyme could be controlled by adenylation under conditions of abundant glutamine.
Oligomer of 12 subunits arranged in the form of two hexagons.
Belongs to the glutamine synthetase family.
NITROGEN REGULATORY PROTEIN P-II HOMOLOG
In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP. P-II-UMP allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme. Conversely, in nitrogen excess P-II is deuridylated and promotes the adenylation of GS. P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is uridylylated to P-II-UMP, these events are reversed (By similarity).
Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
Inhibited by fructose 1,6-bisphosphate (FBP).
SERINE HYDROXYMETHYLTRANSFERASE, MITOCHONDRIAL
Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
Plays an important role in substrate specificity
THF-DEPENDENT SERINE HYDROXYMETHYLTRANSFERASE ACTIVITY
Its primary function is to catalyze the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of L-threonine, L-allo-threonine, L-threo-beta-phenylserine and L-erythro-beta-phenylserine. This second activity is likely to be physiological in H.thermophilus, which is an organism that lacks the ortholog gene for the 'real' threonine aldolase characterized in mesophilic bacteria (LtaE), yeast and plants.
kcat is 18.7 sec(-1) for the L-serine hydroxymethyltransferase reaction, 2.3 sec(-1) for the L-threonine cleavage, and 18.0 sec(-1) for the L-allo-threonine cleavage, at 70 degrees Celsius. In the THF-independent aldolase reaction, the rate constants for the erythro form substrates and for the substrates with beta-phenyl groups are larger than those for the threo form substrates and for the substrates with beta-methyl groups, respectively.
0.28 mM for L-serine (at pH 7.5 and 70 degrees Celsius)
0.78 mM for glycine (at pH 7.5 and 70 degrees Celsius)
7.64 mM for L-threonine (at pH 7.5 and 70 degrees Celsius)
0.92 mM for L-allo-threonine (at pH 7.5 and 70 degrees Celsius)
0.59 mM for L-allo-threonine (at pH 7.5 and 75 degrees Celsius)
4.98 mM for DL-threo-beta-phenylserine (at pH 7.5 and 75 degrees Celsius)
2.63 mM for DL-erythro-beta-phenylserine (at pH 7.5 and 75 degrees Celsius)
Optimum pH is 7.4 for the THF-independent L-allothreonine aldolase activity. More than 95% of full activity remains at pH 8.4, although the activities are reduced to about 90% at pH 6.9 and about 75% at pH 5.9.
Highly thermostable. Retains almost complete THF-independent L-allo-threonine aldolase activity after being incubated at 75 degrees Celsius for 10 minutes, and retains about 77% residual activity after being treated at 87 degrees Celsius for the same time.
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.
Required for morphogenesis under gluconeogenic growth conditions.
Belongs to the gluconeogenesis factor family.
GLYCEROL-3-PHOSPHATE DEHYDROGENASE [NAD(+)] 2, CHLOROPLASTIC
6-phosphogluconate dehydrogenase C-terminal domain-like
Glycerol-3-phosphate dehydrogenase [NAD(P)+]
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase
Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
Involved in the biosynthesis of 6-O-methylglucose lipopolysaccarides (MGLPs). Catalyzes the transfer of a glucose (Glc) moiety from uridine diphosphate (UDP-Glc) to the position 2 of 3-phospho-D-glycerate (3-PGA) to form glucosyl-3-phosphoglycerate (GPG). GpgS is most active with UDP-glucose, followed by GDP-glucose, ADP-glucose, and to a lesser extent, TDP-glucose. 3-PGA is the only acceptor for these glucosyl donors.
Requires divalent cations for activity in the following order of efficiency: Mn(2+), Co(2+), Mg(2+) and Ni(2+) ions.
0.09 mM for 3-PGA (at 70 degrees Celsius)
0.25 mM for 3-PGA (at 85 degrees Celsius)
0.3 mM for 3-PGA (at 90 degrees Celsius)
1.47 mM for UDP-glucose (at 70 degrees Celsius)
1.55 mM for UDP-glucose (at 85 degrees Celsius)
1.58 mM for UDP-glucose (at 90 degrees Celsius)
51.5 umol/min/mg enzyme with 3-PGA as substrate (at 70 degrees Celsius)
110 umol/min/mg enzyme with 3-PGA as substrate (at 85 degrees Celsius)
128 umol/min/mg enzyme with 3-PGA as substrate (at 90 degrees Celsius)
66 umol/min/mg enzyme with UDP-glucose as substrate (at 70 degrees Celsius)
98 umol/min/mg enzyme with UDP-glucose as substrate (at 85 degrees Celsius)
106 umol/min/mg enzyme with UDP-glucose as substrate (at 90 degrees Celsius)
Optimum temperature is 90 degrees Celsius. GpgS is inactive at 40 degrees Celsius, but the activity increases dramatically above 50 degrees Celsius. At 100 degrees Celsius, GpgS retains 33% of the total activity.
Belongs to the glycosyltransferase 2 family.
X-ray crystal structure of a phosphoglycolate phosphatase from Aquifex aeolicus.
New York structural genomix research consortium (NYSGXRC)
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-213 IN COMPLEX WITH SUBSTRATE ANALOGS
PHOSPHATASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_7G00760)-RELATED
Specifically catalyzes the dephosphorylation of 2-phosphoglycolate.
Belongs to the HAD-like hydrolase superfamily. CbbY/CbbZ/Gph/YieH family.
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.
PYRIDOXAL PHOSPHATE PHOSPHATASE YBHA-RELATED
Glucosyl-3-phosphoglycerate/mannosyl-3-phosphoglycerate phosphatase
Involved in the biosynthesis of glucosylglycerate. Catalyzes the dephosphorylation of glucosyl-3-phosphoglycerate (GPG) and mannosyl-3-phosphoglycerate (MPG) to glucosylglycerate (GG) and mannosylglycerate (MG), respectively.
Divalent metal cations. Can use Mg(2+), Co(2+) and, to a lesser extent, Mn(2+) ions.
97 umol/min/mg enzyme with GPG as substrate (at 70 degrees Celsius)
288 umol/min/mg enzyme with GPG as substrate (at 90 degrees Celsius)
294 umol/min/mg enzyme with GPG as substrate (at 85 degrees Celsius)
17.9 umol/min/mg enzyme with MPG as substrate (at 90 degrees Celsius)
15.75 umol/min/mg enzyme with MPG as substrate (at 70 degrees Celsius)
19.6 umol/min/mg enzyme with MPG as substrate (at 85 degrees Celsius)
Optimum temperature is 85 degrees Celsius.
Belongs to the HAD-like hydrolase superfamily. MPGP family.
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 synthetase C-terminal dimerisation domain
Catalyzes the synthesis of GMP from XMP.
Glutamyl-tRNA reductase, N-terminal domain
Glutamyl tRNA-reductase catalytic, N-terminal 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.
Glutamyl tRNA-reductase dimerization domain
Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity).
Porphobilinogen deaminase, C-terminal domain
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.
Catalyzes the ferrous insertion into protoporphyrin IX.
OXYGEN-INDEPENDENT COPROPORPHYRINOGEN III OXIDASE
Involved in the heme biosynthesis. Catalyzes the anaerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen III to yield the vinyl groups in protoporphyrinogen IX.
Belongs to the anaerobic coproporphyrinogen-III oxidase family.
Oxygen-binding protein. May be involved in a storage mechanism or for delivery to oxygen-requiring enzymes. The oxygen-binding site contains two iron atoms.
RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs.
HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE
Purine salvage pathway enzyme that catalyzes the transfer of the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to the N9 position of the 6-oxopurines hypoxanthine and guanine to form the corresponding ribonucleotides IMP (inosine 5'-monophosphate) and GMP (guanosine 5'-monophosphate), with the release of PPi.
Belongs to the purine/pyrimidine phosphoribosyltransferase family.
ATP PHOSPHORIBOSYLTRANSFERASE ATP-PRTASE
Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity (By similarity).
Heteromultimer composed of HisG and HisZ subunits.
Lacks the C-terminal regulatory region which is replaced by HisZ.
Belongs to the ATP phosphoribosyltransferase family. Short subfamily.
Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
HISTIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN
HISTIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN HIS7
Histidine biosynthesis bifunctional protein HisIE
In the N-terminal section; belongs to the PRA-CH family.
In the C-terminal section; belongs to the PRA-PH family.
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase
1-(5-PHOSPHORIBOSYL)-5-[(5-PHOSPHORIBOSYLAMINO)METHYLIDENEAMINO] IMIDAZOLE-4-CARBOXAMIDE ISOMERASE
Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase
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 (By similarity).
IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE HISHF
IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISF/H IGP SYNTHASE SUBUNIT HISF/H
Imidazole glycerol phosphate synthase subunit HisF
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit (By similarity).
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.
IMIDAZOLEGLYCEROL-PHOSPHATE DEHYDRATASE HIS7
Belongs to the imidazoleglycerol-phosphate dehydratase family.
Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.
HISTIDINOL-PHOSPHATE AMINOTRANSFERASE-RELATED
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.
HISTIDINE--TRNA LIGASE, MITOCHONDRIAL-RELATED
ATP phosphoribosyltransferase regulatory subunit
Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine (By similarity).
This function is generally fulfilled by the C-terminal part of HisG, which is missing in some bacteria such as this one.
Belongs to the class-II aminoacyl-tRNA synthetase family. HisZ subfamily.
7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase HPPK
2-AMINO-4-HYDROXY-6-HYDROXYMETHYLDIHYDROPTERIDINE PYROPHOSPHOKINASE
6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, HPPK
6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase
Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step in folate biosynthesis pathway.
Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
Under oxidizing conditions two disulfide bonds are formed involving the reactive cysteines. Under reducing conditions zinc is bound to the reactive cysteines and the protein is inactive.
ATP-DEPENDENT PROTEASE ATPASE SUBUNIT HSLU
ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
A double ring-shaped homohexamer of HslV is capped on each side by a ring-shaped HslU homohexamer. The assembly of the HslU/HslV complex is dependent on binding of ATP.
Belongs to the ClpX chaperone family. HslU subfamily.
Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
Allosterically activated by HslU binding.
Belongs to the peptidase T1B family. HslV subfamily.
Metalloproteases ('zincins'), catalytic domain
Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase.
Isocitrate/Isopropylmalate dehydrogenase-like
Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Belongs to the isocitrate and isopropylmalate dehydrogenases family.
TRANSLATION INITIATION FACTOR IF-1, CHLOROPLASTIC
One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex.
Component of the 30S ribosomal translation pre-initiation complex which assembles on the 30S ribosome in the order IF-2 and IF-3, IF-1 and N-formylmethionyl-tRNA(fMet); mRNA recruitment can occur at any time during PIC assembly.
Translation initiation factor IF- 2, domain 3
TRANSLATION INITIATION FACTOR IF-2, MITOCHONDRIAL
TRANSLATION INITIATION FACTOR IF-2-RELATED
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex (By similarity).
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. IF-2 subfamily.
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
Translation initiation factor 3 (IF-3), C-terminal domain
Translation initiation factor 3 (IF-3), N-terminal domain
TRANSLATION INITIATION FACTOR IF-3, MITOCHONDRIAL
Translation initiation factor IF3, C-terminal domain
Translation initiation factor IF3, N-terminal domain
IF-3 binds to the 30S ribosomal subunit and shifts the equilibrum between 70S ribosomes and their 50S and 30S subunits in favor of the free subunits, thus enhancing the availability of 30S subunits on which protein synthesis initiation begins.
KETOL-ACID REDUCTOISOMERASE, MITOCHONDRIAL
Alpha-keto-beta-hydroxylacyl reductoisomerase
Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
Belongs to the ketol-acid reductoisomerase family.
Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH or NADH to yield (R)-2,3-dihydroxy-isovalerate.
kcat is 0.12 sec(-1) for isomerase activity with NADPH (at pH 7 with S2AL as substrate). kcat is 0.12 sec(-1) for isomerase activity with NADH (at pH 7 with S2AL as substrate).
39 uM for NADH (at pH 7 with S2AL as substrate)
46 uM for NADPH (at pH 7 with S2AL as substrate)
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.
D-amino Acid Aminotransferase, subunit A, domain 2
BRANCHED-CHAIN-AMINO-ACID AMINOTRANSFERASE-RELATED
D-aminoacid aminotransferase-like PLP-dependent enzymes
Probable branched-chain-amino-acid aminotransferase
Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.
ACETOLACTATE SYNTHASE SMALL SUBUNIT 2, CHLOROPLASTIC
Acetohydroxy-acid synthase small subunit
Belongs to the acetolactate synthase small subunit family.
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
Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
Molecular cloning, expression, and characterization of inorganic pyrophosphatase from Aquifex pyrophilus.
MUTAGENESIS OF ASP-38; 140-GLU--THR-157 AND 130-GLU--THR-157
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (2FE-2S)
IRON-SULFUR CLUSTER ASSEMBLY ENZYME NIFU HOMOLOG
Iron-sulfur cluster assembly scaffold protein IscU
A scaffold on which IscS assembles Fe-S clusters. Subsequently gives the nascent cluster to other proteins. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters (Probable).
Homotrimer upon overexpression in E.coli and in crystal structure. The trimer binds Fe-S clusters, upon exposure to air it loses the clusters and concomitantly dissociates into monomers and dimers.
Stabilizes 2Fe-2S cluster binding, prolongs its half-life in air.
Belongs to the FPP/GGPP synthase family.
2-C-METHYL-D-ERYTHRITOL 4-PHOSPHATE CYTIDYLYLTRANSFERASE, CHLOROPLASTIC
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
4-diphosphocytidyl-2C-methyl-D-erythritol synthase
Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Belongs to the IspD/TarI cytidylyltransferase family. IspD subfamily.
Positions MEP for the nucleophilic attack
4-DIPHOSPHOCYTIDYL-2-C-METHYL-D-ERYTHRITOL KINASE, CHLOROPLASTIC
4-diphosphocytidyl-2-C-methyl-D-erythritol kinase
4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase
Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Belongs to the GHMP kinase family. IspE subfamily.
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
2-C-METHYL-D-ERYTHRITOL 2,4-CYCLODIPHOSPHATE SYNTHASE, CHLOROPLASTIC
Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP).
Binds 1 divalent metal cation per subunit.
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (4FE-4S)
4-HYDROXY-3-METHYLBUT-2-EN-1-YL DIPHOSPHATE SYNTHASE
4-HYDROXY-3-METHYLBUT-2-EN-1-YL DIPHOSPHATE SYNTHASE (FERREDOXIN), CHLOROPLASTIC
Nitrite and sulphite reductase 4Fe-4S domain-like
4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin)
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase
Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (3FE-4S)
4-hydroxy-3-methylbut-2-enyl diphosphate reductase, catalytic domain
4-HYDROXY-3-METHYLBUT-2-ENYL DIPHOSPHATE REDUCTASE
Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
Was shown to bind 1 [3Fe-4S] cluster per subunit (PubMed:19035630). However, it likely initially contains a [4Fe-4S] cluster which easily degrades into a [3Fe-4S] form in the presence of oxygen (By similarity).
590 uM for 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate
Optimum temperature is 60 degrees Celsius.
DEHYDRODOLICHYL DIPHOSPHATE SYNTHASE FAMILY MEMBER
Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
RdgB/HAM1 family non-canonical purine NTP pyrophosphatase
INOSINE TRIPHOSPHATE PYROPHOSPHATASE/HAM1 PROTEIN
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.
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH BI-SUBSTRATE ANALOG AP5A
Microbial and mitochondrial ADK, insert 'zinc finger' domain
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. Some bacteria have evolved a zinc-coordinating structure that stabilizes the LID domain.
HYDROPEROXIDASE I, BIFUNCTIONAL CATALASE-PEROXIDASE
Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.
Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme.
Belongs to the peroxidase family. Peroxidase/catalase subfamily.
Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-244)
Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-95)
CYTIDYLATE KINASE/PANTOATE-BETA-ALANINE LIGASE
Belongs to the cytidylate kinase family. Type 1 subfamily.
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 periplasmic 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
Metal cation-transporting ATPase, ATP-binding domain N
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.
{[(2,2-Dihydroxy-Ethyl)-(2,3,4,5-Tetrahydroxy-6-Phosphonooxy-Hexyl)-Amino]-Methyl}-Phosphonic Acid
2-DEHYDRO-3-DEOXYPHOSPHOOCTONATE ALDOLASE 1-RELATED
PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE
2-dehydro-3-deoxyphosphooctonate aldolase
3-deoxy-D-manno-octulosonic acid 8-phosphate synthase
Phospho-2-dehydro-3-deoxyoctonate aldolase
3-DEOXY-MANNO-OCTULOSONATE CYTIDYLYLTRANSFERASE
3-DEOXY-MANNO-OCTULOSONATE CYTIDYLYLTRANSFERASE, MITOCHONDRIAL
CMP-2-keto-3-deoxyoctulosonic acid synthase
Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH CMP
MUTAGENESIS OF GLY-30; GLU-31; GLU-98; LYS-162; ARG-212 AND GLU-276
3-Deoxy-D-manno-octulosonic-acid transferase, N-terminal domain
3-DEOXY-D-MANNO-OCTULOSONIC ACID TRANSFERASE, MITOCHONDRIAL-RELATED
3-deoxy-D-manno-octulosonic acid transferase
Lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase
Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of a single 3-deoxy-D-manno-octulosonate (Kdo) residue from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A. Is strictly monofunctional, i.e. is capable of adding only a single Kdo residue to the acceptor lipid.
Highly thermostable. Does not lose activity after 16 hours at 70 or 80 degrees Celsius, but incubation of the enzyme at 90 and 99 degrees Celsius for 1 hour results in gradual loss of activity.
Can form homodimer, homotrimer and homotetramer.
Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 30 subfamily.
Nearly complete loss of catalytic activity.
Belongs to the KhpA RNA-binding protein family.
HOMOSERINE/4-DIPHOSPHOCYTIDYL-2-C-METHYL-D-ERYTHRITOL KINASE
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
RIBOSE-PHOSPHATE PYROPHOSPHOKINASE 5, CHLOROPLASTIC
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 I subfamily.
Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Belongs to the thymidylate kinase family.
Crystal structures of GTP-binding protein lepA from Aquifex aeolicus.
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH GTP
TRANSLATION FACTOR GUF1 HOMOLOG, CHLOROPLASTIC
Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. LepA subfamily.
2-ISOPROPYLMALATE SYNTHASE 1, CHLOROPLASTIC-RELATED
Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily.
Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate (By similarity).
Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 1 subfamily.
3-ISOPROPYLMALATE DEHYDRATASE LARGE SUBUNIT 2
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.
3-ISOPROPYLMALATE DEHYDRATASE SMALL SUBUNIT 1-RELATED
3-ISOPROPYLMALATE DEHYDRATASE SMALL SUBUNIT 2-RELATED-RELATED
3-isopropylmalate dehydratase small subunit
Belongs to the LeuD family. LeuD type 2 subfamily.
PHOSPHATIDYLGLYCEROL--PROLIPOPROTEIN DIACYLGLYCERYL TRANSFERASE
PROLIPOPROTEIN DIACYLGLYCERYL TRANSFERASE
Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
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
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.
Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Belongs to the CN hydrolase family. Apolipoprotein N-acyltransferase subfamily.
ABC TRANSPORTER ATP-BINDING PROTEIN MG467-RELATED
LIPOPROTEIN-RELEASING SYSTEM ATP-BINDING PROTEIN LOLD
Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner.
The complex is composed of two ATP-binding proteins (LolD) and two transmembrane proteins (LolC and LolE).
Belongs to the ABC transporter superfamily. Lipoprotein translocase (TC 3.A.1.125) family.
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. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
Homohexamer. Organized in a ring with a central cavity.
Udp N-acetylglucosamine O-acyltransferase, C-terminal domain
ACYL-[ACYL-CARRIER-PROTEIN]--UDP-N-ACETYLGLUCOSAMINE O-ACYLTRANSFERASE
ACYL-[ACYL-CARRIER-PROTEIN]--UDP-N-ACETYLGLUCOSAMINE O-ACYLTRANSFERASE, MITOCHONDRIAL-RELATED
Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Belongs to the transferase hexapeptide repeat family. LpxA subfamily.
LIPID-A-DISACCHARIDE SYNTHASE, MITOCHONDRIAL-RELATED
Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
MUTAGENESIS OF HIS-19; GLU-73; HIS-74; GLU-95; ASP-100; GLU-222; HIS-226; ASP-234 AND HIS-253
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-271 IN COMPLEX WITH ZINC
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 2-271 IN COMPLEX WITH ZINC
UDP-3-O-ACYL-N-ACETYLGLUCOSAMINE DEACETYLASE 1, MITOCHONDRIAL-RELATED
UDP-3-O-acyl-N-acetylglucosamine deacetylase
UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase
Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis.
20-fold decrease in activity. 2-fold decrease in zinc content.
10-fold decrease in activity. 3.6-fold decrease in zinc content.
Almost loss of activity. 10-fold decrease in zinc content.
720-fold decrease in activity. 16.6-fold decrease in zinc content.
Almost loss of activity. 1.5-fold decrease in zinc content.
Loss of activity. 4.3-fold decrease in zinc content.
UDP-3-O-ACYLGLUCOSAMINE N-ACYLTRANSFERASE
UDP-3-O-ACYLGLUCOSAMINE N-ACYLTRANSFERASE 1, MITOCHONDRIAL-RELATED
Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Belongs to the transferase hexapeptide repeat family. LpxD subfamily.
TETRAACYLDISACCHARIDE 4'-KINASE, MITOCHONDRIAL-RELATED
Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
4-ALPHA-GLUCANOTRANSFERASE DPE1, CHLOROPLASTIC/AMYLOPLASTIC
Belongs to the disproportionating enzyme family.
Creatinase/methionine aminopeptidase superfamily
METHIONINE AMINOPEPTIDASE 1D, MITOCHONDRIAL
Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.
Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.
Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.
Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal
L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+))
Catalyzes the reversible oxidation of malate to oxaloacetate.
Belongs to the LDH/MDH superfamily. MDH type 3 family.
kcat is 871 sec(-1) with oxaloacetate as substrate.
1550 umol/min/mg enzyme toward oxaloacetate
GDP-mannose:di-myo-inositol-1,3'-phosphate beta-1,2-mannosyltransferase
Catalyzes the transfer of the mannosyl group from GDP-mannose to di-myo-inositol-1,3'-phosphate (DIP), producing mannosyl-di-myo-inositol phosphate (MDIP) (PubMed:19648237). Can also use MDIP as an acceptor of a second mannose residue, yielding di-mannosyl-di-myo-inositol phosphate (MMDIP) (By similarity).
5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE--HOMOCYSTEINE METHYLTRANSFERASE
Cobalamin-independent methionine synthase
Methionine synthase, vitamin-B12 independent isozyme
Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
Belongs to the vitamin-B12 independent methionine synthase family.
5,10-methylenetetrahydrofolate reductase
Catalyzes the NADH-dependent reduction of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate. Is required to provide the methyl group necessary for methionine synthetase to convert homocysteine to methionine; the methyl group is given by 5-methyltetrahydrofolate.
Belongs to the methylenetetrahydrofolate reductase family.
Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
ligand shared between two neighboring subunits
S-adenosylmethionine synthetase, C-terminal domain
Catalyzes the formation of S-adenosylmethionine from methionine and ATP.
Belongs to the AdoMet synthase 2 family.
Dimethylallyl diphosphate:tRNA dimethylallyltransferase
Isopentenyl-diphosphate:tRNA isopentenyltransferase
Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Methylthiotransferase, N-terminal domain
MiaB/RimO family radical SAM methylthiotransferase
CDK5 REGULATORY SUBUNIT-ASSOCIATED PROTEIN 1
MITOCHONDRIAL TRNA METHYLTHIOTRANSFERASE CDK5RAP1
tRNA-2-methylthio-N(6)-dimethylallyladenosine synthase
(Dimethylallyl)adenosine tRNA methylthiotransferase MiaB
Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Belongs to the methylthiotransferase family. MiaB subfamily.
Cell-division inhibitor MinC, C-terminal domain
Probable septum site-determining protein MinC
Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization (By similarity).
Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization.
Adenine nucleotide alpha hydrolases-like domains
MITOCHONDRIAL TRNA-SPECIFIC 2-THIOURIDYLASE 1
TRNA 5-METHYLAMINOMETHYL-2-THIOURIDYLATE -METHYLTRANSFERASE
Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
TRNA MODIFICATION GTPASE GTPBP3, MITOCHONDRIAL
Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Homodimer. Heterotetramer of two MnmE and two MnmG subunits.
Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. TrmE GTPase family.
Crystal structure of gidA from Aquifex aeolicus.
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH FAD
GidA associated domain, C-terminal subdomain
tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG/GidA
tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG
NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Homodimer. Heterotetramer of two MnmE and two MnmG subunits (By similarity).
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
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).
In the N-terminal section; belongs to the MoaC family.
Crystal structure of molybdopterin converting factor subunit 2 (aq_2181) from Aquifex aeolicus VF5.
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).
Probable molybdenum cofactor guanylyltransferase
Molybdopterin-guanine dinucleotide synthase
Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
MotA and MotB comprise the stator element of the flagellar motor complex. Required for rotation of the flagellar motor. Probable transmembrane proton channel (By similarity).
Each stator complex is composed of 4 MotA and 2 MotB subunits. 2 A subunits and 1 B subunit are thought to form a single ion channel, so that each stator complex contains two channels (By similarity).
MUTAGENESIS OF ASP-117; ASP-118; ASP-265; HIS-324; HIS-325 AND HIS-326
X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH MURAYMYCIN D2 INHIBITOR
MUTAGENESIS OF LYS-70; ASN-190; ASP-193; ASP-196; PHE-262 AND GLN-305
PHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE HOMOLOG
UDP-MurNAc-pentapeptide phosphotransferase
Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
Inhibited by natural nucleoside antibiotics including tunicamycin, capuramycin and muraymycin. Usually the cofactor magnesium is not required for antibiotic binding.
Belongs to the glycosyltransferase 4 family. MraY subfamily.
Loss of catalytic activity. Reduces binding to inhibitor.
THREONYLCARBAMOYLADENOSINE TRNA METHYLTHIOTRANSFERASE
Threonylcarbamoyladenosine tRNA methylthiotransferase MtaB
Catalyzes the methylthiolation of N6-threonylcarbamoyladenosine (t(6)A), leading to the formation of 2-methylthio-N6-threonylcarbamoyladenosine (ms(2)t(6)A) at position 37 in tRNAs that read codons beginning with adenine.
Belongs to the methylthiotransferase family. MtaB subfamily.
AMIDOHYDRO-REL DOMAIN-CONTAINING PROTEIN
Composite domain of metallo-dependent hydrolases
5-methylthioadenosine/S-adenosylhomocysteine deaminase
Catalyzes the deamination of 5-methylthioadenosine and S-adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L-homocysteine, respectively. Is also able to deaminate adenosine.
Belongs to the metallo-dependent hydrolases superfamily. MTA/SAH deaminase family.
translation initiation factor eif-2b, domain 1
S-methyl-5-thioribose-1-phosphate isomerase
Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Belongs to the eIF-2B alpha/beta/delta subunits family. MtnA subfamily.
Crystal structure of the L-fuculose-1-phosphate aldolase (aq_1979) from Aquifex aeolicus VF5.
Class II aldolase/adducin N-terminal domain
3-OXO-TETRONATE 4-PHOSPHATE DECARBOXYLASE-RELATED
Methylthioribulose-1-phosphate dehydratase
Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).
Belongs to the aldolase class II family. MtnB subfamily.
2,3-diketo-5-methylthio-1-phosphopentane phosphatase
Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Belongs to the HAD-like hydrolase superfamily. MasA/MtnC family.
1,2-DIHYDROXY-3-KETO-5-METHYLTHIOPENTENE DIOXYGENASE
Acireductone dioxygenase (Fe(2+)-requiring)
Acireductone dioxygenase (Ni(2+)-requiring)
Catalyzes 2 different reactions between oxygen and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway.
Belongs to the acireductone dioxygenase (ARD) family.
May play a role in metal incorporation in vivo
May play a role in transmitting local conformational changes
Crystal structure of UDP-N-acetylglucosamine 1-carboxyvinyltransferase from Aquifex aeolicus VF5.
X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) IN COMPLEX WITH UDP-N-ACETYLGLUCOSAMINE
X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG
FORMATION OF COVALENT REACTION INTERMEDIATE
UDP-N-ACETYLGLUCOSAMINE 1-CARBOXYVINYLTRANSFERASE
UDP-N-acetylglucosamine enolpyruvyl transferase
Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
Belongs to the EPSP synthase family. MurA subfamily.
2-(S-cysteinyl)pyruvic acid O-phosphothioketal
UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain
Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2
UDP-N-ACETYLENOLPYRUVOYLGLUCOSAMINE REDUCTASE
FAD-binding/transporter-associated domain-like
Uridine diphospho-N-Acetylenolpyruvylglucosamine reductase, MurB, C-terminal domain
UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE-RELATED
MurD-like peptide ligases, catalytic domain
MurD-like peptide ligases, peptide-binding domain
UDP-N-acetylmuramoyl-L-alanine synthetase
UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase
Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE MURE HOMOLOG, CHLOROPLASTIC
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase
UDP-N-acetylmuramyl-tripeptide synthetase
Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.
Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP.
Belongs to the MurCDEF family. MurE subfamily.
UDP-N-ACETYLGLUCOSAMINE--N-ACETYLMURAMYL-(PENTAPEPTIDE) PYROPHOSPHORYL-UNDECAPRENOL N-ACETYLGLUCOSAMINE TRANSFERASE 1
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase
Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase
Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Belongs to the glycosyltransferase 28 family. MurG subfamily.
Provides the (R)-glutamate required for cell wall biosynthesis.
Belongs to the aspartate/glutamate racemases family.
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH GLUTAMATE
Provides the (R)-glutamate required for cell wall biosynthesis. Converts L- or D-glutamate to D- or L-glutamate, respectively, but not other amino acids such as alanine, aspartate, and glutamine.
Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane.
Histidine kinase-like ATPase, C-terminal domain
MutL, C-terminal domain, dimerisation subdomain
DNA MISMATCH REPAIR PROTEIN MLH, PMS, MUTL
ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex (By similarity).
Belongs to the DNA mismatch repair MutL/HexB family.
Expression and characterization of MutL proteins from thermophilic eubacteria.
MutL, C-terminal domain, regulatory subdomain
This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex.
DNA MISMATCH REPAIR PROTEIN MUTS FAMILY MEMBER
DNA MISMATCH REPAIR PROTEIN MUTS, TYPE 2
Endonuclease that is involved in the suppression of homologous recombination and may therefore have a key role in the control of bacterial genetic diversity.
Belongs to the DNA mismatch repair MutS family. MutS2 subfamily.
DNA MISMATCH REPAIR PROTEIN MSH1, MITOCHONDRIAL
This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity (By similarity).
Belongs to the DNA mismatch repair MutS family.
Hyperthermophilic MutS proteins: isolation, characterization and enhancement of PCR specificity.
This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity.
Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
Belongs to the quinolinate synthase family. Type 2 subfamily.
Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal domain
Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain
Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal domain
Catalyzes the oxidation of L-aspartate to iminoaspartate, the first step in the de novo biosynthesis of NAD(+).
Belongs to the FAD-dependent oxidoreductase 2 family. NadB subfamily.
Important in orienting the L-aspartate substrate
nicotinate (nicotinamide) nucleotide adenylyltransferase
NICOTINATE-NUCLEOTIDE ADENYLYLTRANSFERASE-RELATED
Probable nicotinate-nucleotide adenylyltransferase
Nicotinate mononucleotide adenylyltransferase
Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
NH 3 /GLUTAMINE-DEPENDENT NAD + SYNTHETASE
Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source.
In the C-terminal section; belongs to the NAD synthetase family.
Proton acceptor; for glutaminase activity
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.
Nucleoside diphosphate kinase-like domain
NUCLEOSIDE DIPHOSPHATE KINASE DDB_G0292928-RELATED
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.
archaeoglobus fulgidus dsm 4304 superfamily
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.
Belongs to the transcriptional regulatory CopG/NikR family.
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH SUBSTRATE ANALOG
MUTAGENESIS OF HIS-93; TYR-95; ARG-218; ARG-219; HIS-226; HIS-261 AND TYR-263
Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain
Involved in heme d1 biosynthesis. Catalyzes the decarboxylation of siroheme into didecarboxysiroheme. Siroheme is probably decarboxylated to monodecarboxysiroheme, which is in turn decarboxylated to didecarboxysiroheme.
H.thermophilus possesses the fused nirDL gene but lacks the genes encoding NirG and NirH.
Loss of activity. Does not alter binding of the substrate analog Fe-URO III.
Almost loss of activity. Does not alter binding of the substrate analog Fe-URO III.
Does not affect didecarboxysiroheme production. Shows a reduced ability to bind the substrate analog Fe-URO III.
Does not affect didecarboxysiroheme production. Does not alter binding of the substrate analog Fe-URO III.
Does not affect didecarboxysiroheme production. Cannot bind the substrate analog Fe-URO III.
Loss of activity. Abolishes binding of the substrate analog Fe-URO III.
ATP-DEPENDENT (S)-NAD(P)H-HYDRATE DEHYDRATASE
ATP-DEPENDENT (S)-NAD(P)H-HYDRATE DEHYDRATASE FAMILY MEMBER
Bifunctional NAD(P)H-hydrate repair enzyme Nnr
ADP-dependent (S)-NAD(P)H-hydrate dehydratase
Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration (By similarity).
In the N-terminal section; belongs to the NnrE/AIBP family.
In the C-terminal section; belongs to the NnrD/CARKD family.
NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL
NAD-dependent protein deacetylase which modulates the activities of several proteins which are inactive in their acetylated form.
Belongs to the sirtuin family. Class III subfamily.
Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes.
BIFUNCTIONAL DTTP/UTP PYROPHOSPHATASE/METHYLTRANSFERASE PROTEIN-RELATED
Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Belongs to the Maf family. YhdE subfamily.
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH PHOSPHATE
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. Does not have kinase activity.
Optimum temperature is 70-80 degrees Celsius.
NADH:ubiquinone oxidoreductase, 30kDa subunit
NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 2, MITOCHONDRIAL
NADH-UBIQUINONE OXIDOREDUCTASE 49 KDA SUBUNIT
NADH-quinone oxidoreductase subunit C/D 1
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
NDH-1 is composed of 13 different subunits. Subunits NuoB, CD, E, F, and G constitute the peripheral sector of the complex (By similarity).
In the N-terminal section; belongs to the complex I 30 kDa subunit family.
In the C-terminal section; belongs to the complex I 49 kDa subunit family.
NADH-quinone oxidoreductase subunit C/D 2
NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 7, MITOCHONDRIAL
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity).
NDH-1 is composed of 14 different subunits. Subunits NuoB, C, D, E, F, and G constitute the peripheral sector of the complex.
Belongs to the complex I 20 kDa subunit family.
NDH-1 is composed of 13 different subunits. Subunits NuoB, CD, E, F, and G constitute the peripheral sector of the complex.
NADH DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN 2, MITOCHONDRIAL
NADH DEHYDROGENASE UBIQUINONE FLAVOPROTEIN 2, MITOCHONDRIAL
Belongs to the complex I 24 kDa subunit family.
NADH-ubiquinone oxidoreductase 51kDa subunit
NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain
Belongs to the complex I 51 kDa subunit family.
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone.
NDH-1 is composed of 14 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex.
Belongs to the complex I subunit 1 family.
NADH DEHYDROGENASE UBIQUINONE IRON-SULFUR PROTEIN 8, MITOCHONDRIAL
Belongs to the complex I 23 kDa subunit family.
NADH-UBIQUINONE OXIDOREDUCTASE SUBUNIT ND4L
Belongs to the complex I subunit 4L family.
Belongs to the complex I subunit 2 family.
ANTITERMINATION NUSB DOMAIN-CONTAINING PROTEIN
N UTILIZATION SUBSTANCE PROTEIN B-RELATED
Transcription antitermination protein NusB
Involved in transcription antitermination. Required for transcription of ribosomal RNA (rRNA) genes. Binds specifically to the boxA antiterminator sequence of the ribosomal RNA (rrn) operons.
N-utilization substance G protein NusG, insert domain
RHO-INTERACTING TRANSCRIPTION TERMINATION FACTOR NUSG
TRANSCRIPTION TERMINATION/ANTITERMINATION PROTEIN NUSG
N-utilization substance G protein NusG, N-terminal domain
Participates in transcription elongation, termination and antitermination.
Monomer (PubMed:12198166). Homodimer (PubMed:12600194).
Contains an N-terminal RNP-like domain, a C-terminal element with a KOW sequence motif and a species-specific immunoglobulin-like fold.
DEVELOPMENTALLY REGULATED GTP-BINDING PROTEIN-RELATED
MITOCHONDRIAL RIBOSOME-ASSOCIATED GTPASE 2
Obg GTP-binding protein N-terminal domain
An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.
Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family.
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
Aspartate/ornithine carbamoyltransferase
ORNITHINE CARBAMOYLTRANSFERASE, MITOCHONDRIAL
ORNITHINE TRANSCARBAMYLASE, MITOCHONDRIAL
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.
CYTOCHROME C OXIDASE ASSEMBLY PROTEIN COX18, MITOCHONDRIAL
Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins.
Interacts with the Sec translocase complex via SecD. Specifically interacts with transmembrane segments of nascent integral membrane proteins during membrane integration.
Belongs to the OXA1/ALB3/YidC family. Type 1 subfamily.
Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
Belongs to the pyrroline-5-carboxylate reductase family.
3-METHYL-2-OXOBUTANOATE HYDROXYMETHYLTRANSFERASE
Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Pantoate-beta-alanine ligase, C-terminal domain
Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
The reaction proceeds by a bi uni uni bi ping pong mechanism.
Belongs to the pantothenate synthetase family.
Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
Binds 1 pyruvoyl group covalently per subunit.
Heterooctamer of four alpha and four beta subunits.
Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus.
Schiff-base intermediate with substrate; via pyruvic acid
Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
Belongs to the ketopantoate reductase family.
Biosynthetic peptidoglycan transglycosylase-like
BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED
In the N-terminal section; belongs to the glycosyltransferase 51 family.
In the C-terminal section; belongs to the transpeptidase family.
Helical; Signal-anchor for type II membrane protein
Proton donor; for transglycosylase activity
Acyl-ester intermediate; for transpeptidase activity
4-HYDROXYTHREONINE-4-PHOSPHATE DEHYDROGENASE
4-(phosphohydroxy)-L-threonine dehydrogenase
Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
The active site is located at the dimer interface.
Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Molecular chaperone capable of stabilizing a range of proteins.
Belongs to the prefoldin subunit alpha family.
ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE, MUSCLE TYPE
Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Allosterically activated by ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate.
Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Prokaryotic clade 'B1' sub-subfamily.
allosteric activator; ligand shared between dimeric partners
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.
CDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE 3-PHOSPHATIDYLTRANSFERASE
CDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE 3-PHOSPHATIDYLTRANSFERASE-RELATED
This protein catalyzes the committed step to the synthesis of the acidic phospholipids.
Belongs to the CDP-alcohol phosphatidyltransferase class-I family.
PHOSPHATE-SPECIFIC TRANSPORT SYSTEM ACCESSORY PROTEIN PHOU
Phosphate-specific transport system accessory protein PhoU homolog
Pst system accessory protein PhoU homolog
Plays a role in the regulation of phosphate uptake. In this role, it may bind, possibly as a chaperone, to PhoR, PhoB or a PhoR-PhoB complex to promote dephosphorylation of phospho-PhoB, or inhibit formation of the PhoR-PhoB transitory complex (Probable).
Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties (By similarity).
Belongs to the glycogen phosphorylase family.
Transcriptional coactivator/pterin dehydratase
PTERIN-4-ALPHA-CARBINOLAMINE DEHYDRATASE
Putative pterin-4-alpha-carbinolamine dehydratase
4-alpha-hydroxy-tetrahydropterin dehydratase
Belongs to the pterin-4-alpha-carbinolamine dehydratase family.
YggS family pyridoxal phosphate-dependent enzyme
PROLINE SYNTHETASE CO-TRANSCRIBED BACTERIAL HOMOLOG PROTEIN
Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis.
Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family.
FATTY ACID/PHOSPHOLIPID SYNTHESIS PROTEIN PLSX
Acyl-[acyl-carrier-protein]--phosphate acyltransferase
Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Homodimer. Probably interacts with PlsY.
Associated with the membrane possibly through PlsY.
glycerol-3-phosphate 1-O-acyltransferase PlsY
GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE-RELATED
Acyl-phosphate--glycerol-3-phosphate acyltransferase
Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Probable 6-oxopurine nucleoside phosphorylase
Purine nucleoside phosphorylase which is highly specific for 6-oxopurine nucleosides. Cleaves guanosine or inosine to respective bases and sugar-1-phosphate molecules. Involved in purine salvage.
Although this enzyme belongs to the family of MTA phosphorylases based on sequence homology, it has been shown that conserved amino acid substitutions in the substrate binding pocket convert the substrate specificity of this enzyme from 6-aminopurines to 6-oxopurines.
Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.
POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE
POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE 1, MITOCHONDRIAL
Eukaryotic type KH-domain (KH-domain type I)
Polynucleotide phosphorylase/guanosine pentaphosphate synthase (PNPase/GPSI), domain 3
Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Belongs to the polyribonucleotide nucleotidyltransferase family.
Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate.
The N-terminal domain contains the ATP/Pi binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site.
The reaction takes place in three steps, mediated by a phosphocarrier histidine residue located on the surface of the central domain. The two first partial reactions are catalyzed at an active site located on the N-terminal domain, and the third partial reaction is catalyzed at an active site located on the C-terminal domain. For catalytic turnover, the central domain swivels from the concave surface of the N-terminal domain to that of the C-terminal domain (By similarity).
Belongs to the PEP-utilizing enzyme family.
ELECTRON TRANSFER FLAVOPROTEIN BETA SUBUNIT LYSINE METHYLTRANSFERASE
S-adenosyl-L-methionine-dependent methyltransferases
Belongs to the methyltransferase superfamily. PrmA family.
MTRF1L RELEASE FACTOR GLUTAMINE METHYLTRANSFERASE
Release factor glutamine methyltransferase
Protein-glutamine N-methyltransferase PrmC
Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
Belongs to the protein N5-glutamine methyltransferase family. PrmC subfamily.
DELTA-1-PYRROLINE-5-CARBOXYLATE SYNTHASE
Glutamyl-gamma-semialdehyde dehydrogenase
Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.
Belongs to the gamma-glutamyl phosphate reductase family.
Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
Belongs to the glutamate 5-kinase family.
LACK OF PHOSPHOGLYCERATE MUTASE ACTIVITY
BROAD-SPECIFICITY PHOSPHATASE YOR283W-RELATED
Metal-independent phosphoserine phosphatase 1
Catalyzes the dephosphorylation of L-phosphoserine to serine and inorganic phosphate. Is poorly or not active toward D-phosphoserine, DL-phosphothreonine, 3-phosphoglycerate, para-nitrophenylphosphate, and fructose-6-phosphate. Does not display phosphoglycerate mutase activity.
Activity is not inhibited by EDTA in vitro, nor enhanced by the addition of Mg(2+).
Values are given for the homodimeric form of the protein.
Homodimer. Can also form a heterodimer with PspB.
Belongs to the histidine phosphatase superfamily. Metal-independent phosphoserine phosphatase family.
Metal-independent phosphoserine phosphatase 2
Part of a complex that catalyzes the dephosphorylation of L-phosphoserine to serine and inorganic phosphate. Is poorly or not active toward D-phosphoserine, DL-phosphothreonine, 3-phosphoglycerate, para-nitrophenylphosphate, and fructose-6-phosphate. Does not display phosphoglycerate mutase activity.
Heterodimer with PspA. The PspB subunit appears to have no or considerably lower PSP activity compared with that of PspA.
Phosphate import ATP-binding protein PstB
Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
The complex is composed of two ATP-binding proteins (PstB), two transmembrane proteins (PstC and PstA) and a solute-binding protein (PstS).
Belongs to the ABC transporter superfamily. Phosphate importer (TC 3.A.1.7) family.
The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Phosphoribosylglycinamide synthetase, C-terminal domain
PHOSPHORIBOSYLAMINE--GLYCINE LIGASE, CHLOROPLASTIC
Phosphoribosylaminoimidazole-succinocarboxamide synthase
Belongs to the SAICAR synthetase family.
Catalyzes two reactions in de novo purine nucleotide biosynthesis. Catalyzes the breakdown of 5-aminoimidazole- (N-succinylocarboxamide) ribotide (SAICAR or 2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate) to 5-aminoimidazole-4-carboxamide ribotide (AICAR or 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide) and fumarate, and of adenylosuccinate (ADS or N(6)-(1,2-dicarboxyethyl)-AMP) to adenosine monophosphate (AMP) and fumarate.
Homooligomer. Residues from neighboring subunits contribute catalytic and substrate-binding residues to each active site (By similarity).
Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.
BIFUNCTIONAL PURINE BIOSYNTHESIS PROTEIN ATIC
BIFUNCTIONAL PURINE BIOSYNTHESIS PROTEIN PURH
Phosphoribosylaminoimidazolecarboxamide formyltransferase
The IMP cyclohydrolase activity resides in the N-terminal region.
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.
PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE CATALYTIC SUBUNIT
N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE)
N5-carboxyaminoimidazole ribonucleotide mutase
5-(carboxyamino)imidazole ribonucleotide mutase
Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR).
Belongs to the AIR carboxylase family. Class I subfamily.
PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE
N5-carboxyaminoimidazole ribonucleotide synthase
5-(carboxyamino)imidazole ribonucleotide synthetase
Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR).
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.
CNF1/YfiH-like putative cysteine hydrolases
S-methyl-5'-thioadenosine phosphorylase aq_167
Purine nucleoside enzyme that catalyzes the phosphorolysis of adenosine and inosine nucleosides, yielding D-ribose 1-phosphate and the respective free bases, adenine and hypoxanthine. Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate. Also has adenosine deaminase activity.
Belongs to the purine nucleoside phosphorylase YfiH/LACC1 family.
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.
Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
X-RAY CRYSTALLOGRAPHY (1.61 ANGSTROMS) IN COMPLEX WITH ZINC
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH PYRB AND ZINC
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH PYRB; DIHYDROOROTIC ACID AND ZINC
Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Binds 1 Zn(2+) ion per subunit (PubMed:15381710, PubMed:15826652, PubMed:19128030, PubMed:24314009). Fully functional with a mononuclear metal center. Does not require a second metal for activity, although the conservation of the second metal-binding site during evolution leaves open the possibility that a second ion might bind in vivo (PubMed:24314009).
The monomer has very low activity by itself. Activated several thousandfold by formation of a complex with PyrB aspartate carbamoyltransferase (ATCase).
Monomer. Forms a 1:1 stoichiometric complex with PyrB. The complex exists as an equilibrium mixture of heterohexamers, composed of 3 PyrC and 3 PyrB subunits, and dodecamers. The complex has both DHOase and ATCase activities.
Belongs to the metallo-dependent hydrolases superfamily. DHOase family. Class I DHOase subfamily.
DIHYDROOROTATE DEHYDROGENASE (QUINONE), MITOCHONDRIAL-RELATED
Putative dihydroorotate dehydrogenase A (fumarate)
Catalyzes the conversion of dihydroorotate to orotate with fumarate as the electron acceptor.
Belongs to the dihydroorotate dehydrogenase family. Type 1 subfamily.
Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Belongs to the purine/pyrimidine phosphoribosyltransferase family. 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.
Allosterically activated by GTP. Inhibited by UTP.
Involved in allosteric activation by GTP
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
Dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit homolog
Dihydroorotate oxidase B, electron transfer subunit homolog
S-ADENOSYLMETHIONINE:TRNA RIBOSYLTRANSFERASE-ISOMERASE
Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
6-pyruvoyl tetrahydropterin synthase/QueD
6-carboxy-5,6,7,8-tetrahydropterin synthase
Catalyzes the conversion of 7,8-dihydroneopterin triphosphate (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) and acetaldehyde.
The active site is at the interface between 2 subunits. The proton acceptor Cys is on one subunit, and the charge relay system is on the other subunit (By similarity).
Belongs to the PTPS family. QueD subfamily.
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 S-adenosyl-L-methionine per subunit.
Belongs to the radical SAM superfamily. 7-carboxy-7-deazaguanine synthase family.
NADPH-DEPENDENT 7-CYANO-7-DEAZAGUANINE REDUCTASE
Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
Belongs to the GTP cyclohydrolase I family. QueF type 1 subfamily.
Probable DNA double-strand break repair Rad50 ATPase
Involved in DNA double-strand break repair (DSBR). The Rad50/Mre11 complex possesses single-strand endonuclease activity and ATP-dependent double-strand-specific 3'-5' exonuclease activity. Rad50 provides an ATP-dependent control of Mre11 by unwinding and/or repositioning DNA ends into the Mre11 active site (By similarity).
Homodimer. Forms a complex with Mre11 (By similarity).
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 (By similarity).
Belongs to the SMC family. RAD50 subfamily.
DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function.
Has a putative N-terminal zinc-finger, a middle region with homology to RecA with ATPase motifs including the RadA KNRFG motif, while the C-terminus is homologous to Lon protease.
Belongs to the RecA family. RadA subfamily.
MITOCHONDRIAL DNA REPAIR PROTEIN RECA HOMOLOG-RELATED
Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.
ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC
Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-DNA) (By similarity).
Belongs to the helicase family. RecG subfamily.
May be involved in recombinational repair of damaged DNA.
May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO.
Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
Methylated by PrmC. Methylation increases the termination efficiency of RF1 (By similarity).
Belongs to the prokaryotic/mitochondrial release factor family.
Methylated by PrmC. Methylation increases the termination efficiency of RF1.
Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA.
Methylated by PrmC. Methylation increases the termination efficiency of RF2 (By similarity).
Methylated by PrmC. Methylation increases the termination efficiency of RF2.
MUTAGENESIS OF ASP-138; ASP-142; ASP-144 AND ASP-160
RNA-free RNase P that catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus.
Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. It cleaves transiently a single DNA strand and remains covalently bound to the 5' DNA end through a tyrosine residue. May be involved in rewinding the DNA strands in the regions of the chromosome that have opened up to allow transcription or replication.
Both the DNA unwinding and positive supercoiling activities require the cooperation of both domains. The cooperative action between the helicase-like and the topoisomerase domains is specific. The helicase-like domain probably does not directly unwind DNA but acts more likely by driving ATP-dependent conformational changes within the whole enzyme, functioning more like a protein motor. The 'latch' region of the N-terminal domain plays a regulatory role in the enzyme, repressing topoisomerase activity in the absence of ATP and therefore preventing the enzyme from acting as an ATP-independent relaxing enzyme; it also helps to coordinate nucleotide hydrolysis by the ATPase domain with the supercoiling activity of the topoisomerase domain.
This enzyme is the only unique feature of hyperthermophilic bacteria/archaea discovered so far. It appears to be essential for adaptation to life at high temperatures.
In the N-terminal section; belongs to the DEAD box helicase family. DDVD subfamily.
In the C-terminal section; belongs to the prokaryotic type I/III topoisomerase family.
Ile-198 is present instead of the conserved Val which is part of the DDVD box.
Facilitates transcription termination by a mechanism that involves Rho binding to the nascent RNA, activation of Rho's RNA-dependent ATPase activity, and release of the mRNA from the DNA template.
Homohexamer. The homohexamer assembles into an open ring structure.
2,5-DIAMINO-6-RIBOSYLAMINO-4(3H)-PYRIMIDINONE 5'-PHOSPHATE REDUCTASE
DIHYDROFOLATE REDUCTASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_8G06820)
2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one reductase
2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate synthase
Catalyzes an early step in riboflavin biosynthesis, the NADPH-dependent reduction of the ribose side chain of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate, yielding 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate.
3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE SYNTHASE
Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.
Binds 2 divalent metal cations per subunit. Magnesium or manganese.
In the N-terminal section; belongs to the DHBP synthase family.
In the C-terminal section; belongs to the GTP cyclohydrolase II family.
Proton acceptor; for GTP cyclohydrolase activity
Nucleophile; for GTP cyclohydrolase activity
Diaminohydroxyphosphoribosylaminopyrimidine deaminase
5-amino-6-(5-phosphoribosylamino)uracil reductase
Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-phosphate.
In the N-terminal section; belongs to the cytidine and deoxycytidylate deaminase family.
In the C-terminal section; belongs to the HTP reductase family.
An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
The PRC barrel domain binds ribosomal protein uS19.
30S ribosomal protein S12 methylthiotransferase RimO
RIBOSOMAL PROTEIN S12 METHYLTHIOTRANSFERASE RIMO
Ribosomal protein uS12 methylthiotransferase RimO
Ribosomal protein uS12 (aspartate-C(3))-methylthiotransferase
Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein uS12.
Belongs to the methylthiotransferase family. RimO subfamily.
Ribosome maturation factor RimP, C-terminal domain
Required for maturation of 30S ribosomal subunits.
RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN
RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT
R1 subunit of ribonucleotide reductase, N-terminal domain
Ribonucleoside-diphosphate reductase subunit alpha
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides (By similarity).
Under complex allosteric control mediated by deoxynucleoside triphosphates and ATP binding to separate specificity and activation sites on the alpha subunit. The type of nucleotide bound at the specificity site determines substrate preference. It seems probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP reduction and dTTP favors GDP reduction. Stimulated by ATP and inhibited by dATP binding to the activity site (By similarity).
Tetramer of two alpha and two beta subunits.
Belongs to the ribonucleoside diphosphate reductase large chain family.
allosteric effector that controls substrate specificity
RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SMALL CHAIN
RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SUBUNIT M2
Ribonucleoside-diphosphate reductase subunit beta
This protein undergoes a protein self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation.
Belongs to the ribonucleoside diphosphate reductase small chain family.
Ribonucleoside-diphosphate reductase subunit beta, 1st part
Ribonucleoside-diphosphate reductase subunit beta, 2nd part
Catalyzes the dismutation of two molecules of 6,7-dimethyl-8-ribityllumazine, resulting in the formation of riboflavin and 5-amino-6-(D-ribitylamino)uracil.
ligand shared between two trimeric partners
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF APOENZYME
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE ANALOG OR REACTION INTERMEDIATE ANALOG INHIBITORS AND PHOSPHATE
3-(7-hydroxy-8-ribityllumazine-6-yl) propionic acid
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.
10.0 uM for 5-amino-6-(D-ribitylamino)uracil (at 37 degrees Celsius and pH 7.0)
26 uM for 3,4-dihydroxy-2-butanone 4-phosphate (at 37 degrees Celsius and pH 7.0)
31 nmol/min/mg enzyme (at 37 degrees Celsius and pH 7.0)
425 nmol/min/mg enzyme (at 70 degrees Celsius and pH 7.0)
Extremely thermostable. Has a melting temperature of 119.9 degrees Celsius.
Forms an icosahedral capsid composed of 60 subunits, arranged as a dodecamer of pentamers.
39S RIBOSOMAL PROTEIN L10, MITOCHONDRIAL
Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.
Part of the ribosomal stalk of the 50S ribosomal subunit. The N-terminus interacts with L11 and the large rRNA to form the base of the stalk. The C-terminus forms an elongated spine to which L12 dimers bind in a sequential fashion forming a multimeric L10(L12)X complex (By similarity).
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.
One or more lysine residues are methylated.
Belongs to the universal ribosomal protein uL11 family.
39S RIBOSOMAL PROTEIN L13, MITOCHONDRIAL
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.
54S RIBOSOMAL PROTEIN L38, MITOCHONDRIAL
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 L19. In the 70S ribosome, L14 and L19 interact and together make contacts with the 16S rRNA in bridges B5 and B8.
Belongs to the universal ribosomal protein uL14 family.
39S RIBOSOMAL PROTEIN L15, MITOCHONDRIAL
Belongs to the universal ribosomal protein uL15 family.
39S RIBOSOMAL PROTEIN L16, MITOCHONDRIAL
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.
Belongs to the universal ribosomal protein uL16 family.
39S RIBOSOMAL PROTEIN L17, MITOCHONDRIAL
Part of the 50S ribosomal subunit. Contacts protein L32.
Belongs to the bacterial ribosomal protein bL17 family.
39S RIBOSOMAL PROTEIN L18, MITOCHONDRIAL
This is one of the proteins that bind and probably mediate the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.
Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S and 23S rRNAs.
Belongs to the universal ribosomal protein uL18 family.
39S RIBOSOMAL PROTEIN L19, MITOCHONDRIAL
This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site.
Belongs to the bacterial ribosomal protein bL19 family.
Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release.
Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.
Belongs to the universal ribosomal protein uL1 family.
Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release (By similarity).
50S RIBOSOMAL PROTEIN L20, CHLOROPLASTIC
Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit (By similarity).
Belongs to the bacterial ribosomal protein bL20 family.
Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit.
39S RIBOSOMAL PROTEIN L21, MITOCHONDRIAL
This protein binds to 23S rRNA in the presence of protein L20.
Part of the 50S ribosomal subunit. Contacts protein L20.
Belongs to the bacterial ribosomal protein bL21 family.
50S RIBOSOMAL PROTEIN L22, CHLOROPLASTIC
CHLOROPLAST 50S RIBOSOMAL PROTEIN L22-RELATED
This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. 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 (By similarity).
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
One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome.
Part of the 50S ribosomal subunit. Contacts protein L29, and trigger factor when it is bound to the ribosome.
Belongs to the universal ribosomal protein uL23 family.
39S RIBOSOMAL PROTEIN L24, MITOCHONDRIAL
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.
One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.
Belongs to the universal ribosomal protein uL24 family.
This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance.
Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA. Binds to the 5S rRNA independently of L5 and L18.
Belongs to the bacterial ribosomal protein bL25 family. CTC subfamily.
39S RIBOSOMAL PROTEIN L27, MITOCHONDRIAL
Belongs to the bacterial ribosomal protein bL27 family.
Belongs to the bacterial ribosomal protein bL28 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.
39S RIBOSOMAL PROTEIN L30, MITOCHONDRIAL
Belongs to the bacterial ribosomal protein bL31 family. Type A subfamily.
Belongs to the bacterial ribosomal protein bL32 family.
50S RIBOSOMAL PROTEIN L33, CHLOROPLASTIC
Belongs to the bacterial ribosomal protein bL33 family.
39S RIBOSOMAL PROTEIN L34, MITOCHONDRIAL
MITOCHONDRIAL RIBOSOMAL PROTEIN 34 FAMILY MEMBER
Belongs to the bacterial ribosomal protein bL34 family.
Belongs to the bacterial ribosomal protein bL35 family.
50S RIBOSOMAL PROTEIN L36, CHLOROPLASTIC
Belongs to the bacterial ribosomal protein bL36 family.
50S RIBOSOMAL PROTEIN L3-1, CHLOROPLASTIC
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 L19.
Belongs to the universal ribosomal protein uL3 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 one of the proteins that bind and probably mediate the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts 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; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA and the P site tRNA. Forms a bridge to the 30S subunit in the 70S ribosome.
Belongs to the universal ribosomal protein uL5 family.
This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.
Belongs to the universal ribosomal protein uL6 family.
39S RIBOSOMAL PROTEIN L12, MITOCHONDRIAL
Ribosomal protein L7/12, oligomerisation (N-terminal) domain
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
Homodimer. Part of the ribosomal stalk of the 50S ribosomal subunit. Forms a multimeric L10(L12)X complex, where L10 forms an elongated spine to which 2 to 4 L12 dimers bind in a sequential fashion. Binds GTP-bound translation factors.
Belongs to the bacterial ribosomal protein bL12 family.
Belongs to the bacterial ribosomal protein bL9 family.
Complete sequence of chromosome of Thermovibrio ammonificans HB-1.
Putative RNA ligase (PubMed:25324547). Is able to catalyze the adenylation reaction of ssDNA 3'-terminal phosphate (ssDNA 3'p) to 3'-adenylated DNA (ssDNA 3'pp5'A) (PubMed:25324547).
Probable dual-specificity RNA methyltransferase RlmN
23S rRNA (adenine(2503)-C(2))-methyltransferase
Ribosomal RNA large subunit methyltransferase N
tRNA (adenine(37)-C(2))-methyltransferase
Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.
Reaction proceeds by a ping-pong mechanism involving intermediate methylation of a conserved cysteine residue.
Belongs to the radical SAM superfamily. RlmN family.
ENDOLYTIC PEPTIDOGLYCAN TRANSGLYCOSYLASE RLPA
Probable endolytic peptidoglycan transglycosylase RlpA
Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides.
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-147 WITH AND WITHOUT MANGANESE
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-147 WITH MAGNESIUM
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-220 WITH DS-RNA
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH DS-RNA
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH PRODUCT
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH PRODUCT AND MAGNESIUM
Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Also processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Probably processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism.
Binds 2 Mg(2+) per subunit. Mn(2+) also supports catalytic activity.
Optimum temperature is 70-85 degrees Celsius.
Very low catalytic activity, binds RNA normally.
Loss of magnesium, alters ds-RNA binding, loss of activity.
Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism.
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.
Belongs to the RNase HII family. RnhC subfamily.
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF WILD-TYPE AND 3 MUTANT PROTEINS WITH SUBSTRATE
MUTAGENESIS OF ARG-86; THR-125 AND ARG-126
Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
Homohexameric ring arranged as a trimer of dimers (PubMed:12746447).
No processing of pre-tRNA-CCA-N(8), binds tRNA as well as wild-type.
Poor processing of pre-tRNA-CCA-N(8), removes a few nucleotides, binds tRNA better than wild-type.
Decreased processing of pre-tRNA-CCA-N(8), removes perhaps 4/8 nucleotides, binds tRNA slightly less well than wild-type.
Homohexameric ring arranged as a trimer of dimers.
3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs.
Belongs to the RNR ribonuclease family. RNase R subfamily.
F1F0 ATP synthase subunit B, membrane domain
Endoribonuclease that initiates mRNA decay.
Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.
Belongs to the ribulose-phosphate 3-epimerase family.
DNA-directed RNA polymerase, insert domain
C-terminal domain of RNA polymerase alpha subunit
Insert subdomain of RNA polymerase alpha subunit
DNA-directed RNA polymerase subunit alpha
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Homodimer. The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta' and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription.
The N-terminal domain is essential for RNAP assembly and basal transcription, whereas the C-terminal domain is involved in interaction with transcriptional regulators and with upstream promoter elements.
Belongs to the RNA polymerase alpha chain family.
DNA-directed RNA polymerase, beta subunit, external 1 domain
DNA-directed RNA polymerase, subunit 2, domain 6
RNA polymerase alpha subunit dimerisation domain
DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA
beta and beta-prime subunits of DNA dependent RNA-polymerase
The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta' and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription.
Belongs to the RNA polymerase beta chain family.
DNA-directed RNA polymerase subunit beta'
Belongs to the RNA polymerase beta' chain family.
DNA-DIRECTED RNA POLYMERASE SUBUNIT OMEGA
Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits (By similarity).
The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta' and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription (By similarity).
Belongs to the RNA polymerase subunit omega family.
Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another.
37S RIBOSOMAL PROTEIN S10, MITOCHONDRIAL
Involved in the binding of tRNA to the ribosomes.
Belongs to the universal ribosomal protein uS10 family.
28S RIBOSOMAL PROTEIN S11, MITOCHONDRIAL
40S RIBOSOMAL PROTEIN S14/30S RIBOSOMAL PROTEIN S11
Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome.
Part of the 30S ribosomal subunit. Interacts with proteins S7 and S18. Binds to IF-3.
Belongs to the universal ribosomal protein uS11 family.
28S RIBOSOMAL PROTEIN S12, MITOCHONDRIAL
With S4 and S5 plays an important role in translational accuracy.
Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.
Part of the 30S ribosomal subunit. Contacts proteins S8 and S17. May interact with IF1 in the 30S initiation complex.
Belongs to the universal ribosomal protein uS12 family.
30S RIBOSOMAL PROTEIN S13/40S RIBOSOMAL PROTEIN S18
37S RIBOSOMAL PROTEIN SWS2, MITOCHONDRIAL
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. Contacts the tRNAs in the A and P-sites.
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.
28S RIBOSOMAL PROTEIN S14, MITOCHONDRIAL
Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site.
Part of the 30S ribosomal subunit. Contacts proteins S3 and S10.
Belongs to the universal ribosomal protein uS14 family. Zinc-binding uS14 subfamily.
37S RIBOSOMAL PROTEIN S28, MITOCHONDRIAL
RIBOSOMAL PROTEIN S15, BACTERIAL AND ORGANELLAR
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it helps nucleate assembly of the platform of the 30S subunit by binding and bridging several RNA helices of the 16S rRNA.
Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.
Part of the 30S ribosomal subunit. Forms a bridge to the 50S subunit in the 70S ribosome, contacting the 23S rRNA.
Belongs to the universal ribosomal protein uS15 family.
28S RIBOSOMAL PROTEIN S16, MITOCHONDRIAL
Belongs to the bacterial ribosomal protein bS16 family.
37S RIBOSOMAL PROTEIN S17, MITOCHONDRIAL
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.
28S RIBOSOMAL PROTEIN S18C, MITOCHONDRIAL
Binds as a heterodimer with protein bS6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit.
Part of the 30S ribosomal subunit. Forms a tight heterodimer with protein bS6.
Belongs to the bacterial ribosomal protein bS18 family.
37S RIBOSOMAL PROTEIN S19, MITOCHONDRIAL
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
Belongs to the universal ribosomal protein uS19 family.
30S RIBOSOMAL PROTEIN S20, CHLOROPLASTIC
Belongs to the bacterial ribosomal protein bS20 family.
Belongs to the bacterial ribosomal protein bS21 family.
30S RIBOSOMAL PROTEIN S2 PROKARYOTIC AND ORGANELLAR
Belongs to the universal ribosomal protein uS2 family.
Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation.
Part of the 30S ribosomal subunit. Forms a tight complex with proteins S10 and S14.
Belongs to the universal ribosomal protein uS3 family.
37S RIBOSOMAL PROTEIN NAM9, MITOCHONDRIAL
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.
Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body.
Part of the 30S ribosomal subunit. Contacts proteins S4 and S8.
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.
Binds together with bS18 to 16S ribosomal RNA.
Belongs to the bacterial ribosomal protein bS6 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, probably blocks exit of the E-site tRNA.
Part of the 30S ribosomal subunit. Contacts proteins S9 and S11.
Belongs to the universal ribosomal protein uS7 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.
Part of the 30S ribosomal subunit. Contacts proteins S5 and S12.
Belongs to the universal ribosomal protein uS8 family.
Belongs to the universal ribosomal protein uS9 family.
Crystal structure of YjeQ from Aquifex aeolicus.
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH GDP AND ZINC IONS
ribosome small subunit-dependent GTPase A
SMALL RIBOSOMAL SUBUNIT BIOGENESIS GTPASE RSGA
SMALL RIBOSOMAL SUBUNIT BIOGENESIS GTPASE RSGA 1, MITOCHONDRIAL-RELATED
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S ribosomal subunit.
Monomer. Associates with 30S ribosomal subunit, binds 16S rRNA.
Belongs to the TRAFAC class YlqF/YawG GTPase family. RsgA subfamily.
X-RAY CRYSTALLOGRAPHY (1.44 ANGSTROMS) IN COMPLEXES WITH RNA AND S-ADENOSYL-L-HOMOCYSTEINE
Ribosomal RNA adenine dimethylase-like, domain 2
Ribosomal RNA small subunit methyltransferase A
16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase
S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase
Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family. RsmA subfamily.
16S RRNA (URACIL(1498)-N(3))-METHYLTRANSFERASE
RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE E
Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit (By similarity).
Belongs to the RNA methyltransferase RsmE family.
S-ADENOSYL-L-METHIONINE-DEPENDENT METHYLTRANSFERASES SUPERFAMILY PROTEIN
Ribosomal RNA small subunit methyltransferase G
16S rRNA 7-methylguanosine methyltransferase
Specifically methylates the N7 position of a guanine in 16S rRNA.
Belongs to the methyltransferase superfamily. RNA methyltransferase RsmG family.
Putative methyltransferase TM0872, insert domain
16S rRNA (cytosine(1402)-N(4))-methyltransferase RsmH
12S RRNA N4-METHYLCYTIDINE METHYLTRANSFERASE
Ribosomal RNA small subunit methyltransferase H
rRNA (cytosine-N(4)-)-methyltransferase RsmH
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Belongs to the methyltransferase superfamily. RsmH family.
16S rRNA (cytidine(1402)-2'-O)-methyltransferase
RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE I
16S rRNA 2'-O-ribose C1402 methyltransferase
rRNA (cytidine-2'-O-)-methyltransferase RsmI
Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA.
Belongs to the methyltransferase superfamily. RsmI family.
RNA 3'-terminal phosphate cyclase domain
RNA 3'-terminal phosphate cyclase, insert domain
RNA 3'-terminal phosphate cyclase, RPTC, insert domain
Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing (By similarity).
Belongs to the RNA 3'-terminal cyclase family. Type 1 subfamily.
Crossover junction endodeoxyribonuclease RusA
Endonuclease that resolves Holliday junction intermediates made during homologous genetic recombination and DNA repair. Exhibits sequence and structure-selective cleavage of four-way DNA junctions, where it introduces symmetrical nicks in two strands of the same polarity at the 5' side of CC dinucleotides.
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.
ATP adenosine-5'-phosphosulfate 3'-phosphotransferase
In the N-terminal section; belongs to the sulfate adenylyltransferase family.
In the C-terminal section; belongs to the APS kinase family.
Belongs to the sulfate adenylyltransferase family.
Helical scaffold and wing domains of SecA
SECA INNER MEMBRANE COMPONENT OF SEC PROTEIN SECRETION SYSTEM
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Monomer and homodimer. Part of the essential Sec protein translocation apparatus which comprises SecA, SecYEG and auxiliary proteins SecDF. Other proteins may also be involved.
Multidrug efflux transporter AcrB transmembrane domain
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Forms a complex with SecF. Part of the essential Sec protein translocation apparatus which comprises SecA, SecYEG and auxiliary proteins SecDF. Other proteins may also be involved.
Belongs to the SecD/SecF family. SecD subfamily.
X-RAY CRYSTALLOGRAPHY (7.5 ANGSTROMS) OF SECYEG IN COMPLEX WITH B.SUBTILIS SECA
Essential subunit of the protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Component of the Sec protein translocase complex. Heterotrimer consisting of SecY, SecE and SecG subunits. The heterotrimers can form oligomers, although 1 heterotrimer is thought to be able to translocate proteins. Interacts with SecDF, and other proteins may be involved. The channel interacts with SecA via subunit SecY.
Forms a complex with SecD. Part of the essential Sec protein translocation apparatus which comprises SecA, SecYEG and auxiliary proteins SecDF. Other proteins may also be involved.
Belongs to the SecD/SecF family. SecF subfamily.
Subunit of the protein translocation channel SecYEG.
PREPROTEIN TRANSLOCASE SUBUNIT SCY2, CHLOROPLASTIC
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently (By similarity).
Component of the Sec protein translocase complex. Heterotrimer consisting of SecY, SecE and SecG subunits. The heterotrimers can form oligomers, although 1 heterotrimer is thought to be able to translocate proteins. Interacts with the ribosome. Interacts with SecDF, and other proteins may be involved. Interacts with SecA (By similarity).
Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
INACTIVE SELENIDE, WATER DIKINASE-LIKE PROTEIN-RELATED
Synthesizes selenophosphate from selenide and ATP.
Belongs to the selenophosphate synthase 1 family. Class I subfamily.
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.
Superoxide dismutase, copper/zinc binding domain
Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Belongs to the Cu-Zn superoxide dismutase family.
Iron/manganese superoxide dismutase, C-terminal domain
SUPEROXIDE DISMUTASE [MN], MITOCHONDRIAL
Fe,Mn superoxide dismutase (SOD), C-terminal domain
Fe,Mn superoxide dismutase (SOD), N-terminal domain
Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Belongs to the iron/manganese superoxide dismutase family.
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-213 IN COMPLEX WITH IRON
Highly thermostable. Retains about 70% of its activity after heating for 60 minutes at 100 degrees Celsius.
L-cysteine S-thiosulfotransferase subunit SoxA
Thiosulfate-oxidizing multienzyme system protein SoxA1
C-type diheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosulfate or other inorganic sulfur substrates. This leads to the liberation of two electrons, which may be transferred from the SoxAX complex to another cytochrome c that then channels them into the respiratory electron transport chain. Some electrons may be used for reductive CO(2) fixation.
Binds 2 heme c groups covalently per subunit.
Thiosulfate-oxidizing multienzyme system protein SoxA2
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.
Crystal structure of the adenosylmethionine decarboxylase (aq_254) from Aquifex aeolicus VF5.
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.
Proton acceptor; for processing activity
GUANOSINE-3',5'-BIS DIPHOSPHATE 3'-PYROPHOSPHOHYDROLASE
Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase
Penta-phosphate guanosine-3'-pyrophosphohydrolase
In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. This enzyme catalyzes the degradation of ppGpp into GDP. It may also be capable of catalyzing the synthesis of ppGpp (By similarity).
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH FAD AND UBIQUINONE ANALOG
Catalyzes the oxidation of hydrogen sulfide, with the help of a quinone. Consecutive reaction cycles lead to the accumulation of a polysulfide product on the active site Cys residues; these products are released when they exceed a critical length, typically as cyclooctasulfur.
Signal recognition particle, SRP54 subunit, M-domain
SIGNAL RECOGNITION PARTICLE 54 KDA PROTEIN, CHLOROPLASTIC
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.
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.
SINGLE-STRANDED DNA-BINDING PROTEIN, MITOCHONDRIAL
Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism.
Important for interaction with partner proteins
STRUCTURE BY ELECTRON MICROSCOPY (13.00 ANGSTROMS) OF 2-131
TMRNA-BINDING COMPONENT OF TRANS-TRANSLATION TAGGING COMPLEX
Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation.
The tmRNA-SmpB complex associates with stalled 70S ribosomes.
Although the Valle et al., electron microscopy paper indicates this protein came from T.thermophilus its sequence maps to A.aeolicus.
SUCCINATE--COA LIGASE [GDP-FORMING] SUBUNIT BETA, MITOCHONDRIAL
Succinate--CoA ligase [ADP-forming] subunit beta
Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Heterotetramer of two alpha and two beta subunits.
Belongs to the succinate/malate CoA ligase beta subunit family.
SUCCINATE--COA LIGASE [ADP/GDP-FORMING] SUBUNIT ALPHA, MITOCHONDRIAL
Succinate--CoA ligase [ADP-forming] subunit alpha
Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit.
Belongs to the succinate/malate CoA ligase alpha subunit family.
Survival protein SurE-like phosphatase/nucleotidase
Nucleoside 5'-monophosphate phosphohydrolase
Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Belongs to the SurE nucleotidase family.
X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 1-454 WITH SUBSTRATES OR WITH ATP
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 758-867
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. The Aquifex aeolicus domain can be used in vitro to replace the corresponding domain in E.coli.
Belongs to the class-II aminoacyl-tRNA synthetase family.
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.
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.
Non-discriminating aspartyl-tRNA synthetase
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Glutamate-tRNA synthetase, class I, anticodon-binding domain 1
GLUTAMATE--TRNA LIGASE, MITOCHONDRIAL-RELATED
An anticodon-binding domain of class I aminoacyl-tRNA synthetases
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 1 subfamily.
PHENYLALANINE--TRNA LIGASE, MITOCHONDRIAL
Phenylalanine--tRNA ligase alpha subunit
Phenylalanyl-tRNA synthetase alpha subunit
Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily.
Ferrodoxin-fold anticodon-binding domain
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 1 subfamily.
GLYCINE--TRNA LIGASE, CHLOROPLASTIC/MITOCHONDRIAL 2
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 1 subfamily.
Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile) (By similarity).
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)) (By similarity).
LYSINE--TRNA LIGASE, CHLOROPLASTIC/MITOCHONDRIAL
LEUCINE--TRNA LIGASE, MITOCHONDRIAL-RELATED
Seems to consist of an alpha chain and a beta chain.
Crystal structure of Aquifex aeolicus methionyl-tRNA synthetase complexed with tRNA(met).
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 2A subfamily.
MITOCHONDRIAL RIBOSOME PROTEIN L39/PROLYL-TRNA LIGASE FAMILY MEMBER
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). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS.
0.06 mM for proline (at 60 degrees Celsius)
0.05 mM for cysteine (at 60 degrees Celsius)
Consists of three domains: the N-terminal catalytic domain, the editing domain and the C-terminal anticodon-binding domain.
Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 1 subfamily.
YbaK/aminoacyl-tRNA synthetase-associated domain
Arginyl tRNA synthetase N-terminal domain
Arginyl-tRNA synthetase (ArgRS), N-terminal 'additional' domain
Serine-tRNA synthetase, tRNA binding domain
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). Also edits incorrectly charged L-seryl-tRNA(Thr).
Valyl-tRNA synthetase, C-terminal domain
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.
The C-terminal coiled-coil domain is crucial for aminoacylation activity.
Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily.
Catalyzes the attachment of tryptophan to tRNA(Trp).
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 2 subfamily.
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH ZINC
TRNA(ADENINE(34)) DEAMINASE, CHLOROPLASTIC
Catalyzes the deamination of adenosine to inosine at the wobble position 34 of tRNA(Arg2).
Belongs to the cytidine and deoxycytidylate deaminase family.
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Belongs to the transaldolase family. Type 3B subfamily.
SEC-INDEPENDENT PROTEIN TRANSLOCASE PROTEIN TATA
Sec-independent protein translocase protein TatA 1
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Sec-independent protein translocase protein TatA 2
SEC-INDEPENDENT PROTEIN TRANSLOCASE PROTEIN TATC
SEC-INDEPENDENT PROTEIN TRANSLOCASE PROTEIN TATC, CHLOROPLASTIC-RELATED
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes.
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. Although the primary sequence of this enzyme is similar to those of the 1-Cys Prx6 enzymes, its catalytic properties resemble those of the typical 2-Cys Prxs and C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by thioredoxin.
Belongs to the peroxiredoxin family. Prx6 subfamily.
Cysteine sulfenic acid (-SOH) intermediate
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Homodimer. Within each dimer, one monomer is responsible for RNA recognition and catalysis, while the other monomer binds to the replacement base PreQ1.
Belongs to the queuine tRNA-ribosyltransferase family.
RNA binding; important for wobble base 34 recognition
PHOSPHOMETHYLPYRIMIDINE SYNTHASE, CHLOROPLASTIC
Hydroxymethylpyrimidine phosphate synthase
Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction.
Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
HYDROXYMETHYLPYRIMIDINE/PHOSPHOMETHYLPYRIMIDINE KINASE THI20-RELATED
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase
Hydroxymethylpyrimidine phosphate kinase
Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.
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.
Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
Homotetramer. Forms heterodimers with either ThiH or ThiS.
X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEXES WITH ATP; ADP; TMP; TPP AND MAGNESIUM
Crystal structure of thiamine monophosphate kinase (ThiL) from Aquifex Aeolicus.
New York structural genomics research consortium (NYSGRC)
Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.
Reaction mechanism of ThiL seems to utilize a direct, inline transfer of the gamma-phosphate of ATP to TMP rather than a phosphorylated enzyme intermediate.
Belongs to the thiamine-monophosphate kinase family.
Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
Belongs to the 2H phosphoesterase superfamily. ThpR family.
Thymidylate synthase-complementing protein Thy1
Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor, and NADPH and FADH(2) as the reductant.
Binds 4 FAD per tetramer. Each FAD binding site is formed by three monomers.
Belongs to the thymidylate synthase ThyX family.
Involved in ionization of N3 of dUMP, leading to its activation
ligand shared between neighboring subunits
TRIGGER FACTOR CHAPERONE AND PEPTIDYL-PROLYL CIS/TRANS ISOMERASE
TRIGGER FACTOR-LIKE PROTEIN TIG, CHLOROPLASTIC
Triger factor/SurA peptide-binding domain-like
Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (By similarity).
About half TF is bound to the ribosome near the polypeptide exit tunnel while the other half is free in the cytoplasm.
Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
The N-terminus of this protein overlaps with a tRNA(Leu) encoded in another frame on the same strand.
Belongs to the FKBP-type PPIase family. Tig subfamily.
Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Belongs to the tRNA(Ile)-lysidine synthase family.
Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.
Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+).
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
X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 494-769
DNA gyrase/topoisomerase IV, subunit A, C-terminal
DNA GYRASE SUBUNIT A, CHLOROPLASTIC/MITOCHONDRIAL
A type II topoisomerase. Despite its similarity to DNA gyrase, this enzyme is not able to supercoil DNA, and instead acts like topoisomerase IV. Relaxes both positively and negatively supercoiled DNA in an ATP-dependent fashion, decatenates interlocked circles. This the first bacteria shown to not contain DNA gyrase, although it has 2 copies of a reverse gyrase that introduces positive supercoils. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner (PubMed:21076033).
Optimum temperature is 70 degrees Celsius, active between 37 and 90 degrees Celsius.
Heterotetramer, composed of two 'GyrA' and two 'GyrB' chains. In the heterotetramer, 'GyrA' contains the active site tyrosine that forms a transient covalent intermediate with the DNA, while 'GyrB' binds cofactors and catalyzes ATP hydrolysis (PubMed:21076033).
The C-terminal domain (CTD, residues 494-769) contains 6 tandemly repeated subdomains known as blades, each of which is composed of a 4-stranded antiparallel beta-sheet. The blades form a flat, toroidal beta-pinwheel fold, to which DNA probably binds. Unlike most CTDs, this organism is missing the canonical GyrA-box. The isolated CTD does not impart writhe, DNA wrapping necessary for supercoil introduction. The ability to supercoil DNA is recovered if the CTD is swapped with the CTD of T.maritima (residues 482-804).
Belongs to the type II topoisomerase GyrA/ParC subunit family.
A type II topoisomerase. Despite its similarity to DNA gyrase, this enzyme is not able to supercoil DNA, and instead acts like topoisomerase IV. Relaxes both positively and negatively supercoiled DNA in an ATP-dependent fashion, decatenates interlocked circles. If this subunit is reconstituted with GyrA from E.coli the hybrid enzyme supercoils relaxed plasmid DNA; if paired with E.coli ParC supercoiling is not restored. This the first bacteria shown to not contain DNA gyrase, although it has 2 copies of a reverse gyrase that introduces positive supercoils. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner (PubMed:21076033).
Binds two Mg(2+) per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn(2+) or Ca(2+).
Heterotetramer, composed of two GyrA and two GyrB chains. In the heterotetramer, 'GyrA' contains the active site tyrosine that forms a transient covalent intermediate with DNA, while 'GyrB' binds cofactors and catalyzes ATP hydrolysis (PubMed:21076033).
Belongs to the type II topoisomerase GyrB family.
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Belongs to the triosephosphate isomerase family.
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 atypical 2-Cys peroxiredoxin, C(R) is present in the same subunit to form an intramolecular disulfide. The disulfide is subsequently reduced by thioredoxin.
Belongs to the peroxiredoxin family. Tpx subfamily.
N2,N2-dimethylguanosine tRNA methyltransferase, C-terminal domain
N 2 ,N 2 -DIMETHYLGUANOSINE TRNA METHYLTRANSFERASE
TRNA (GUANINE(26)-N(2))-DIMETHYLTRANSFERASE
tRNA (guanine(26)-N(2)/guanine(27)-N(2))-dimethyltransferase
Dimethylates the guanine residues at position 26 and 27 of one or more 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 (guanosine(46)-N7)-methyltransferase TrmB
3-DEOXY-D-MANNO-OCTULOSONIC-ACID TRANSFERASE/TRNA GUANINE-N 7 - -METHYLTRANSFERASE
tRNA (guanine(46)-N(7))-methyltransferase
Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
The C-terminal region is probably involved in protein stability.
Belongs to the class I-like SAM-binding methyltransferase superfamily. TrmB family.
Specifically methylates guanosine-37 in various tRNAs.
Belongs to the RNA methyltransferase TrmD family.
METHYLENETETRAHYDROFOLATE--TRNA-(URACIL-5-)-METHYLTRANSFERASE TRMFO
Folate-dependent tRNA (uracil-5-)-methyltransferase
Folate-dependent tRNA(M-5-U54)-methyltransferase
Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
Belongs to the MnmG family. TrmFO subfamily.
SPOU_METHYLASE DOMAIN-CONTAINING PROTEIN
tRNA (guanosine(18)-2'-O)-methyltransferase
Catalyzes the 2'-O methylation of guanosine at position 18 in tRNA. Type II methylase, which methylates only a subset of tRNA species.
Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family.
TRYPTOPHAN SYNTHASE ALPHA CHAIN, CHLOROPLASTIC
The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Tetramer of two alpha and two beta chains.
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
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.
Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia (By similarity).
Heterotetramer consisting of two non-identical subunits: a beta subunit (TrpG) and a large alpha subunit (TrpE).
Belongs to the anthranilate synthase component I family.
N-(5'-PHOSPHORIBOSYL)ANTHRANILATE ISOMERASE
Pseudouridine synthase I, catalytic domain, C-terminal subdomain
Pseudouridine synthase I, catalytic domain, N-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.
Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Belongs to the pseudouridine synthase TruB family. Type 1 subfamily.
Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
Belongs to the pseudouridine synthase TruD family.
The active site is a redox-active disulfide bond.
Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family.
TRNA N6-ADENOSINE THREONYLCARBAMOYLTRANSFERASE
TRNA N6-ADENOSINE THREONYLCARBAMOYLTRANSFERASE, MITOCHONDRIAL-RELATED
t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaD
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
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 involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
TRNA THREONYLCARBAMOYLADENOSINE BIOSYNTHESIS PROTEIN TSAE
t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaE
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 involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaD and TsaB. TsaE seems to play an indirect role in the t(6)A biosynthesis pathway, possibly in regulating the core enzymatic function of TsaD (By similarity).
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.
Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Bacitracin is thought to be involved in the inhibition of peptidoglycan synthesis by sequestering undecaprenyl diphosphate, thereby reducing the pool of lipid carrier available.
Structure of aq2163 protein from Aquifex aeolicus.
URACIL PHOSPHORIBOSYLTRANSFERASE, CHLOROPLASTIC
Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP.
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate.
Forms a heterotetramer with UvrB during the search for lesions.
Belongs to the ABC transporter superfamily. UvrA family.
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
Forms a heterotetramer with UvrA during the search for lesions. Interacts with UvrC in an incision complex.
The beta-hairpin motif is involved in DNA binding.
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
Interacts with UvrB in an incision complex.
Toxic component of a type II toxin-antitoxin (TA) system. An RNase.
Belongs to the PINc/VapC protein family.
YebC/PmpR family DNA-binding transcriptional regulator
TRANSCRIPTIONAL REGULATORY PROTEIN YEBC-RELATED
Probable transcriptional regulatory protein PERMA_0079
TRANSMEMBRANE PROTEIN WITH METALLOPHOSPHOESTERASE DOMAIN
TRANSMEMBRANE PROTEIN WITH METALLOPHOSPHOESTERASE DOMAIN-RELATED
Uncharacterized metallophosphoesterase aq_1054
Belongs to the metallophosphoesterase superfamily.
In the C-terminal section; belongs to the protein sulfotransferase family.
predicted glycosyltransferase like domains
UNDECAPRENYL PHOSPHATE-ALPHA-4-AMINO-4-DEOXY-L-ARABINOSE ARABINOSYL TRANSFERASE
Belongs to the glycosyltransferase 39 family.
YbhB/YbcL family Raf kinase inhibitor-like protein
PEBP (PHOSPHATIDYLETHANOLAMINE-BINDING PROTEIN) FAMILY PROTEIN
Nucleoid-associated protein YbaB-like domain
Nucleoid-associated protein SYO3AOP1_1366
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
Uncharacterized protein aq_1391/aq_1640/aq_aa40
Belongs to the sulfur carrier protein TusA family.
PSEUDOURIDINE SYNTHASE FAMILY PROTEIN-RELATED
S4 RNA-BINDING DOMAIN-CONTAINING PROTEIN
Uncharacterized RNA pseudouridine synthase aq_1464
Belongs to the pseudouridine synthase RsuA family.
OUTER-MEMBRANE LIPOPROTEIN CARRIER PROTEIN
Prokaryotic lipoproteins and lipoprotein localization factors
Crystal structure of hypothetical protein (aq_1494) from Aquifex aeolicus.
4-HYDROXYBENZOYL-COA THIOESTERASE FAMILY MEMBER
NOVEL THIOESTERASE SUPERFAMILY DOMAIN AND SAPOSIN A-TYPE DOMAIN CONTAINING PROTEIN (0610012H03RIK)
Belongs to the 4-hydroxybenzoyl-CoA thioesterase family.
Uncharacterized phosphosugar isomerase aq_1546
Belongs to the SIS family. GutQ/KpsF subfamily.
Cytochrome c oxidase-like, subunit I domain
MFS general substrate transporter like domains
Probable transcriptional regulatory protein aq_1575
3-OCTAPRENYL-4-HYDROXYBENZOATE CARBOXY-LYASE-RELATED
DNA INTERNALIZATION/COMPETENCE PROTEIN COMEC/REC2
Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3
L-LYSINE 2,3-AMINOMUTASE AQ_1632-RELATED
Putative L-lysine 2,3-aminomutase aq_1632
Belongs to the radical SAM superfamily. KamA family.
Belongs to the glycosyltransferase 83 family.
MITOCHONDRIAL RNA PSEUDOURIDINE SYNTHASE
RIBOSOMAL LARGE SUBUNIT PSEUDOURIDINE SYNTHASE D
Uncharacterized RNA pseudouridine synthase aq_1758
Belongs to the pseudouridine synthase RluA family.
Belongs to the universal stress protein A family.
LATE ENDOSOMAL/LYSOSOMAL MP1 INTERACTING PROTEIN
To P.aeruginosa PA0043 and M.thermoautotrophicum MTH1451.
DOMAIN GTPASE-ACTIVATING PROTEIN, PUTATIVE-RELATED-RELATED
iron-sulfur cluster assembly accessory protein
IRON-SULFUR CLUSTER ASSEMBLY 2 HOMOLOG, MITOCHONDRIAL
Toxic component of a type II toxin-antitoxin (TA) system. An RNase (By similarity).
MEMBRANE METALLOPROTEASE ARASP2, CHLOROPLASTIC-RELATED
LIGAND BINDING DOMAIN PROTEIN, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G14370)-RELATED
CYCLIC DI-GMP PHOSPHODIESTERASE PA4108-RELATED
Uncharacterized globin-like protein aq_211
Ribonuclease Z/Hydroxyacylglutathione hydrolase-like
Belongs to the metallo-beta-lactamase superfamily. Glyoxalase II family.
RNA POLYMERASE-BINDING TRANSCRIPTION FACTOR DKSA-RELATED
DnaK suppressor protein DksA, alpha-hairpin domain
TRNA (URACIL(54)-C(5))-METHYLTRANSFERASE
Uncharacterized RNA methyltransferase aq_257
Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family.
HTH-TYPE TRANSCRIPTIONAL REGULATOR AQ_268-RELATED
WINGED HELIX-TURN-HELIX TRANSCRIPTIONAL REGULATOR, RRF2 FAMILY
Putative HTH-type transcriptional regulator aq_268
2-IMINOBUTANOATE/2-IMINOPROPANOATE DEAMINASE
2-IMINOBUTANOATE/2-IMINOPROPANOATE DEAMINASE RIDA
Putative L-lysine 2,3-aminomutase aq_454
INTERMEMBRANE PHOSPHOLIPID TRANSPORT SYSTEM BINDING PROTEIN MLAD
INTERMEMBRANE PHOSPHOLIPID TRANSPORT SYSTEM BINDING PROTEIN MLAD-RELATED
Probable transcriptional regulatory protein HY04AAS1_0501
Uncharacterized RNA pseudouridine synthase aq_554
Uncharacterized HTH-type transcriptional regulator aq_603
Outer membrane protein transport protein (OMPP1/FadL/TodX)
Probable transcriptional regulatory protein SYO3AOP1_0685
the short chain amide and urea porin (sap) family
Belongs to the autoinducer-2 exporter (AI-2E) (TC 2.A.86) family.
MECHANOSENSITIVE ION CHANNEL PROTEIN 2, CHLOROPLASTIC
Mechanosensitive channel protein MscS (YggB), C-terminal domain
Mechanosensitive channel protein MscS (YggB), transmembrane region
Uncharacterized MscS family protein aq_812
GANGLIOSIDE INDUCED DIFFERENTIATION ASSOCIATED PROTEIN 2-RELATED
SEC TRANSLOCON ACCESSORY COMPLEX SUBUNIT YAJC
The SecYEG-SecDF-YajC-YidC holo-translocon (HTL) protein secretase/insertase is a supercomplex required for protein secretion, insertion of proteins into membranes, and assembly of membrane protein complexes. While the SecYEG complex is essential for assembly of a number of proteins and complexes, the SecDF-YajC-YidC subcomplex facilitates these functions.
Part of the SecDF-YidC-YajC translocase complex. The SecDF-YidC-YajC translocase forms a supercomplex with SecYEG, called the holo-translocon (HTL).
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
Belongs to the endoribonuclease YbeY family.
HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN 1
membrane protein insertion efficiency factor YidD
MEMBRANE PROTEIN INSERTION EFFICIENCY FACTOR-RELATED
Putative membrane protein insertion efficiency factor
Could be involved in insertion of integral membrane proteins into the membrane.
POLYNUCLEOTIDYL TRANSFERASE, RIBONUCLEASE H-LIKE SUPERFAMILY PROTEIN
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
IS200/IS605 family accessory protein TnpB-like domain
Belongs to the 'phage' integrase family.
O-(3'-phospho-DNA)-tyrosine intermediate
JHP933, nucleotidyltransferase-like core domain
FIDO DOMAIN-CONTAINING PROTEIN DDB_G0283145
PROTEIN ADENYLYLTRANSFERASE AQ_AA38-RELATED
Probable protein adenylyltransferase aq_aa38
Probable adenylyltransferase that mediates the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins.