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| | proS | prolyl-tRNA synthetase; 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 dea [...] (567 aa) |
| | ABD30386.1 | Glutamine synthetase, type I. (446 aa) |
| | asnS | asparaginyl-tRNA synthetase,putative. (430 aa) |
| | birA | BirA bifunctional protein, putative; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a repressor; Belongs to the biotin--protein ligase family. (323 aa) |
| | ABD30701.1 | acetyl-CoA carboxylase, biotin carboxylase; This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. (451 aa) |
| | glyQS | glycyl-tRNA synthetase; Catalyzes the attachment of glycine to tRNA(Gly). Belongs to the class-II aminoacyl-tRNA synthetase family. (463 aa) |
| | purK | Phosphoribosylaminoimidazole carboxylase, ATPase subunit; Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR). (374 aa) |
| | ABD30783.1 | acetyl-CoA carboxylase, biotin carboxylase, putative. (453 aa) |
| | alaS | alanyl-tRNA synthetase; 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. (876 aa) |
| | aspS | aspartyl-tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. (588 aa) |
| | lysS | lysyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family. (495 aa) |
| | tilS | Conserved hypothetical protein; 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. (431 aa) |
| | metG | methionyl-tRNA synthetase, putative; 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 2B subfamily. (657 aa) |
| | guaA | GMP synthase, putative; Catalyzes the synthesis of GMP from XMP. (513 aa) |
| | ABD29477.1 | Conserved hypothetical protein. (340 aa) |
| | sbnF | Conserved hypothetical protein; Catalyzes the condensation of L-2,3-diaminopropionic acid (L- Dap) and citryl-diaminoethane to form L-2,3-diaminopropionyl-citryl- diaminoethane, the third step in staphyloferrin B biosynthesis. (616 aa) |
| | sbnE | Conserved hypothetical protein; Catalyzes the synthesis of citryl-L-2,3-diaminopropionic acid from L-2,3-diaminopropionic acid (L-Dap) and citrate, the first step in staphyloferrin B biosynthesis. (578 aa) |
| | sbnC | Conserved hypothetical protein; Catalyzes the condensation of L-2,3-diaminopropionyl-citryl- diaminoethane and 2-oxoglutarate to form staphyloferrin B, the fourth and last step in staphyloferrin B biosynthesis. (584 aa) |
| | hisS | histidyl-tRNA synthetase. (420 aa) |
| | ABD30835.1 | Folylpolyglutamate synthase/dihydrofolate synthase, putative; Belongs to the folylpolyglutamate synthase family. (423 aa) |
| | valS | valyl-tRNA synthetase; 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; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily. (876 aa) |
| | purA | Adenylosuccinate synthetase; 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. (427 aa) |
| | thrS | threonyl-tRNA synthetase; 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). (645 aa) |
| | tyrS | tyrosyl-tRNA synthetase; 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 1 subfamily. (420 aa) |
| | fhs | Formate-tetrahydrofolate ligase, putative; Belongs to the formate--tetrahydrofolate ligase family. (555 aa) |
| | murC | UDP-N-acetylmuramate--alanine ligase; Cell wall formation; Belongs to the MurCDEF family. (437 aa) |
| | ABD30924.1 | Conserved hypothetical protein; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (198 aa) |
| | leuS | leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (805 aa) |
| | menE | O-succinylbenzoic acid--coa ligase, putative; Converts 2-succinylbenzoate (OSB) to 2-succinylbenzoyl-CoA (OSB-CoA); Belongs to the ATP-dependent AMP-binding enzyme family. MenE subfamily. (492 aa) |
| | gatB | glutamyl-tRNA(Gln) amidotransferase, B subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily. (475 aa) |
| | gatA | glutamyl-tRNA(Gln) amidotransferase, A subunit; 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). (485 aa) |
| | gatC | glutamyl-tRNA(Gln) amidotransferase, C subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family. (100 aa) |
| | ligA | DNA ligase, NAD-dependent; 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. (667 aa) |
| | nadE | NAD+ synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. (273 aa) |
| | ABD31181.1 | Nicotinate phosphoribosyltransferase, putative; Catalyzes the first step in the biosynthesis of NAD from nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D- ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate. Belongs to the NAPRTase family. (480 aa) |
| | murF | UDP-N-acetylmuramoylalanyl-D-glutamyl-2, 6-diaminopimelate--D-alanyl-D-alanyl ligase; Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein; Belongs to the MurCDEF family. MurF subfamily. (452 aa) |
| | ddl | D-alanine--D-alanine ligase; Cell wall formation. (356 aa) |
| | pyrG | CTP synthase; 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. (536 aa) |
| | bioW | 6-carboxyhexanoate--CoA ligase, putative; Catalyzes the transformation of pimelate into pimeloyl-CoA with concomitant hydrolysis of ATP to AMP. (230 aa) |
| | bioD | Dethiobiotin synthase, putative; Catalyzes a mechanistically unusual reaction, the ATP- dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8- diaminopelargonic acid (DAPA) to form an ureido ring. (228 aa) |
| | panC | Pantoate--beta-alanine ligase; Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. Belongs to the pantothenate synthetase family. (283 aa) |
| | gltX | glutamyl-tRNA synthetase; 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. (484 aa) |
| | cysS | cysteinyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (466 aa) |
| | serS | seryl-tRNA synthetase; Catalyzes the attachment of serine to tRNA(Ser). Is also probably 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). (428 aa) |
| | argS | arginyl-tRNA synthetase. (553 aa) |
| | queC | Conserved hypothetical protein; Catalyzes the ATP-dependent conversion of 7-carboxy-7- deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)). (222 aa) |
| | dltA | D-alanine-activating enzyme; Catalyzes the first step in the D-alanylation of lipoteichoic acid (LTA), the activation of D-alanine and its transfer onto the D- alanyl carrier protein (Dcp) DltC. In an ATP-dependent two-step reaction, forms a high energy D-alanyl-AMP intermediate, followed by transfer of the D-alanyl residue as a thiol ester to the phosphopantheinyl prosthetic group of the Dcp. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall. Belongs to the ATP-dependent AMP [...] (485 aa) |
| | argG | Argininosuccinate synthase; Belongs to the argininosuccinate synthase family. Type 1 subfamily. (401 aa) |
| | trpS | tryptophanyl-tRNA synthetase; Catalyzes the attachment of tryptophan to tRNA(Trp). Belongs to the class-I aminoacyl-tRNA synthetase family. (329 aa) |
| | murE | UDP-N-acetylmuramoylalanyl-D-glutamate--2, 6-diaminopimelate ligase; Catalyzes the addition of L-lysine to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. Cannot use diaminopimelate as substrate. Seems to have a role in beta-lactam antibiotic resistance. (493 aa) |
| | ABD30088.1 | Lipoyltransferase and lipoate-protein ligase, putative. (328 aa) |
| | purC | Phosphoribosylaminoimidazole-succinocarboxamide synthase; Belongs to the SAICAR synthetase family. (234 aa) |
| | purS | Phosphoribosylformylglycinamidine synthase, PurS protein; 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 [...] (87 aa) |
| | purQ | Phosphoribosylformylglycinamidine synthase I; 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 i [...] (223 aa) |
| | purL | Phosphoribosylformylglycinamidine synthase 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 [...] (729 aa) |
| | purM | Phosphoribosylformylglycinamidine cyclo-ligase. (342 aa) |
| | purD | Phosphoribosylamine-glycine ligase; Belongs to the GARS family. (415 aa) |
| | ABD30181.1 | Pyruvate carboxylase; Catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second. (1150 aa) |
| | tmcAL | Conserved hypothetical protein; Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac- AMP) and then transfers the acetyl group to tRNA to form ac(4)C34. (379 aa) |
| | pheS | phenylalanyl-tRNA synthetase, alpha subunit; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. (352 aa) |
| | pheT | phenylalanyl-tRNA synthetase, beta subunit; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (800 aa) |
| | bshC | Conserved hypothetical protein; Involved in bacillithiol (BSH) biosynthesis. May catalyze the last step of the pathway, the addition of cysteine to glucosamine malate (GlcN-Mal) to generate BSH. (400 aa) |
| | murD | UDP-N-acetylmuramoylalanine--D-glutamate ligase; Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). Belongs to the MurCDEF family. (449 aa) |
| | ileS | isoleucyl-tRNA synthetase; 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). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily. (917 aa) |
| | carA | Carbamoyl-phosphate synthase, small subunit; Belongs to the CarA family. (366 aa) |
| | carB | Carbamoyl-phosphate synthase, large subunit. (1057 aa) |
| | ABD30285.1 | Phosphopantothenoylcysteine decarboxylase/phosphopantothenate--cysteine ligase; Catalyzes two steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4- phosphopantothenoylcysteine, in the latter compound is decarboxylated to form 4'-phosphopantotheine; In the C-terminal section; belongs to the PPC synthetase family. (399 aa) |
| | sucC | succinyl-CoA synthetase, beta subunit, putative; 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. (388 aa) |
| | sucD | succinyl-CoA synthetase, alpha subunit, putative; 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. (302 aa) |
