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pyrG pyrG Sps_01755 Sps_01755 Sps_02082 Sps_02082 Sps_02084 Sps_02084 proS proS tilS tilS ileS ileS Sps_02460 Sps_02460 tyrS tyrS Sps_02560 Sps_02560 Sps_03302 Sps_03302 Sps_03333 Sps_03333 Sps_01173 Sps_01173 aspS aspS queC queC thrS thrS serS serS Sps_00876 Sps_00876 purA purA asnS asnS acsA acsA purM purM Sps_00480 Sps_00480 nadE nadE birA birA Sps_00296 Sps_00296 Sps_00224 Sps_00224 kbl kbl glyQ glyQ glyS glyS Sps_00043 Sps_00043 murD murD murF murF murE murE murC murC Sps_03358 Sps_03358 ligA ligA Sps_03625 Sps_03625 gltX gltX purL purL guaA guaA purD purD Sps_03033 Sps_03033 gshB gshB rimK rimK Sps_02818 Sps_02818 hisS hisS gshA gshA alaS alaS Sps_01703 Sps_01703 Sps_04165 Sps_04165 carB carB carA carA leuS leuS lipB lipB valS valS cobQ cobQ Sps_04856 Sps_04856 Sps_04869 Sps_04869 lysS lysS Sps_04977 Sps_04977 gluQ gluQ panC panC mpl mpl purA-2 purA-2 ddl ddl Sps_01289 Sps_01289 Sps_01295 Sps_01295 Sps_01298 Sps_01298 purC purC pheT pheT pheS pheS Sps_01379 Sps_01379 metG metG Sps_01550 Sps_01550 bioD bioD sucD sucD Sps_05252 Sps_05252 fhs fhs argS argS trpS trpS argG argG Sps_05608 Sps_05608 Sps_01770 Sps_01770 cysS cysS glnS glnS sucC sucC Sps_01975 Sps_01975 Sps_02077 Sps_02077
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pyrGCTP 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. (545 aa)
Sps_01755Folylpolyglutamate synthase/dihydrofolate synthase; 'PFAM: Mur ligase family, glutamate ligase domain; Mur ligase middle domain'; TIGRFAM: folylpolyglutamate synthase/dihydrofolate synthase; Belongs to the folylpolyglutamate synthase family. (423 aa)
Sps_02082acetyl-CoA carboxylase, carboxyltransferase component (subunits alpha and beta); PFAM: Carboxyl transferase domain. (535 aa)
Sps_020843-methylcrotonoyl-CoA carboxylase, alpha subunit; 'PFAM: Carbamoyl-phosphate synthase L chain, ATP binding domain; Biotin carboxylase C-terminal domain; Carbamoyl-phosphate synthase L chain, N-terminal domain; Biotin-requiring enzyme'; 'TIGRFAM: acetyl-CoA carboxylase, biotin carboxylase subunit'. (701 aa)
proSprolyl-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 [...] (569 aa)
tilStRNA(Ile)-lysidine synthetase; 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. Belongs to the tRNA(Ile)-lysidine synthase family. (467 aa)
ileSIsoleucyl-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. (924 aa)
Sps_02460PFAM: CobD/Cbib protein. (327 aa)
tyrStyrosyl-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 2 subfamily. (398 aa)
Sps_02560'PFAM: Glutamine synthetase, catalytic domain'. (449 aa)
Sps_03302Phosphopantothenoylcysteine 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. (413 aa)
Sps_03333acyl-CoA synthetase/AMP-acid ligase; PFAM: AMP-binding enzyme. (454 aa)
Sps_01173alpha-L-glutamate ligase-related protein; PFAM: Sugar-transfer associated ATP-grasp; TIGRFAM: alpha-L-glutamate ligase-related protein. (320 aa)
aspSaspartyl-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. (595 aa)
queCpreQ(0) biosynthesis protein QueC; Catalyzes the ATP-dependent conversion of 7-carboxy-7- deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)). Belongs to the QueC family. (229 aa)
thrSthreonyl-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). (642 aa)
serSseryl-tRNA synthetase; 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). (428 aa)
Sps_00876acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; PFAM: AMP-binding enzyme; AMP-binding enzyme C-terminal domain. (579 aa)
purAAdenylosuccinate 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. (418 aa)
asnS'PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain'; TIGRFAM: asparaginyl-tRNA synthetase. (466 aa)
acsAAcetyl-coenzyme A synthetase; Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA; Belongs to the ATP-dependent AMP-binding enzyme family. (650 aa)
purMPhosphoribosylformylglycinamidine cyclo-ligase; 'PFAM: AIR synthase related protein, N-terminal domain; AIR synthase related protein, C-terminal domain'; TIGRFAM: phosphoribosylaminoimidazole synthetase. (345 aa)
Sps_00480Asparagine synthase, glutamine-hydrolyzing; PFAM: Glutamine amidotransferase domain; Asparagine synthase; TIGRFAM: asparagine synthase (glutamine-hydrolyzing). (558 aa)
nadENH(3)-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source; Belongs to the NAD synthetase family. (276 aa)
birAbirA, biotin-(acetyl-CoA-carboxylase) ligase; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon. (320 aa)
Sps_002962-succinylbenzoyl-CoA synthetase; PFAM: AMP-binding enzyme; AMP-binding enzyme C-terminal domain; TIGRFAM: O-succinylbenzoate-CoA ligase. (494 aa)
Sps_00224acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; PFAM: AMP-binding enzyme. (582 aa)
kbl2-amino-3-ketobutyrate coenzyme A ligase; Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA. (397 aa)
glyQPFAM: Glycyl-tRNA synthetase alpha subunit; 'TIGRFAM: glycyl-tRNA synthetase, tetrameric type, alpha subunit'. (287 aa)
glySPFAM: Glycyl-tRNA synthetase beta subunit; DALR anticodon binding domain; 'TIGRFAM: glycyl-tRNA synthetase, tetrameric type, beta subunit'. (689 aa)
Sps_00043Biotin-dependent carboxylase-like protein; PFAM: Allophanate hydrolase subunit 2; TIGRFAM: biotin-dependent carboxylase uncharacterized domain. (309 aa)
murDUDP-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)
murFUDP-N-acetylmuramoyl-tripeptide--D-alanyl-D- alanine 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. (455 aa)
murEUDP-N-acetylmuramoylalanyl-D-glutamate--2, 6-diaminopimelate ligase; Catalyzes the addition of an amino acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. (492 aa)
murCUDP-N-acetylmuramate--L-alanine ligase; Cell wall formation; Belongs to the MurCDEF family. (489 aa)
Sps_03358'PFAM: Glutamine synthetase, catalytic domain; Glutamine synthetase, beta-Grasp domain'; 'TIGRFAM: glutamine synthetase, type I'. (469 aa)
ligADNA 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. (682 aa)
Sps_03625Lipid A core-O-antigen ligase-like enyme; PFAM: O-antigen ligase like membrane protein. (451 aa)
gltXglutamyl-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). (469 aa)
purLPhosphoribosylformylglycinamidine synthase; Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. (1293 aa)
guaAGMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP. (525 aa)
purDPhosphoribosylamine--glycine ligase; 'PFAM: Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide synthetase, C domain'; TIGRFAM: phosphoribosylamine--glycine ligase; Belongs to the GARS family. (430 aa)
Sps_03033acetyl-CoA carboxylase, biotin carboxylase subunit; 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. (454 aa)
gshB'PFAM: Prokaryotic glutathione synthetase, N-terminal domain; Prokaryotic glutathione synthetase, ATP-grasp domain'; 'TIGRFAM: glutathione synthetase, prokaryotic'; Belongs to the prokaryotic GSH synthase family. (317 aa)
rimKSSU ribosomal protein S6P modification protein; PFAM: RimK-like ATP-grasp domain; Putative ATP-dependant zinc protease; 'TIGRFAM: alpha-L-glutamate ligase, RimK family'; Belongs to the RimK family. (464 aa)
Sps_02818Hypothetical protein; PFAM: tRNA synthetases class I (W and Y); TIGRFAM: tryptophanyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (257 aa)
hisSPFAM: Anticodon binding domain; Histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase. (424 aa)
gshAPFAM: Glutamate-cysteine ligase; TIGRFAM: glutamate--cysteine ligase; Belongs to the glutamate--cysteine ligase type 1 family. Type 1 subfamily. (535 aa)
alaSalanyl-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. (874 aa)
Sps_01703acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; PFAM: AMP-binding enzyme; AMP-binding enzyme C-terminal domain. (576 aa)
Sps_04165'PFAM: Anticodon binding domain; tRNA synthetase class II core domain (G, H, P, S and T)'; TIGRFAM: threonyl-tRNA synthetase. (392 aa)
carB'PFAM: Carbamoyl-phosphate synthase L chain, ATP binding domain; MGS-like domain; Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate synthase L chain, N-terminal domain'; 'TIGRFAM: carbamoyl-phosphate synthase, large subunit'; Belongs to the CarB family. (1072 aa)
carA'PFAM: Carbamoyl-phosphate synthase small chain, CPSase domain; Glutamine amidotransferase class-I'; 'TIGRFAM: carbamoyl-phosphate synthase, small subunit'; Belongs to the CarA family. (381 aa)
leuS'PFAM: Leucyl-tRNA synthetase, Domain 2; tRNA synthetases class I (I, L, M and V); Anticodon-binding domain of tRNA'; 'TIGRFAM: leucyl-tRNA synthetase, eubacterial and mitochondrial family'; Belongs to the class-I aminoacyl-tRNA synthetase family. (863 aa)
lipBLipoate-protein ligase B; 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. (217 aa)
valSvalyl-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. (973 aa)
cobQAdenosylcobyric acid synthase (glutamine-hydrolysing); Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. Belongs to the CobB/CobQ family. CobQ subfamily. (539 aa)
Sps_04856PFAM: 5-formyltetrahydrofolate cyclo-ligase family; 'TIGRFAM: 5,10-methenyltetrahydrofolate synthetase'. (207 aa)
Sps_04869acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; PFAM: AMP-binding enzyme; AMP-binding enzyme C-terminal domain. (534 aa)
lysS'PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain'; 'TIGRFAM: lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial'; Belongs to the class-II aminoacyl-tRNA synthetase family. (500 aa)
Sps_049772'-5' RNA ligase; Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'- phosphomonoester; Belongs to the 2H phosphoesterase superfamily. ThpR family. (202 aa)
gluQGlutamyl-queuosine tRNA(Asp) synthetase; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon; Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily. (290 aa)
panCPantothenate synthetase; Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. Belongs to the pantothenate synthetase family. (281 aa)
mplUDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl- meso-diaminopimelate ligase; Reutilizes the intact tripeptide L-alanyl-gamma-D-glutamyl- meso-diaminopimelate by linking it to UDP-N-acetylmuramate. Belongs to the MurCDEF family. Mpl subfamily. (475 aa)
purA-2Adenylosuccinate 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. (431 aa)
ddlD-alanine--D-alanine ligase; Cell wall formation; Belongs to the D-alanine--D-alanine ligase family. (336 aa)
Sps_01289acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; PFAM: AMP-binding enzyme; AMP-binding enzyme C-terminal domain. (557 aa)
Sps_01295GMP synthase family protein; PFAM: Glutamine amidotransferase class-I. (232 aa)
Sps_01298'PFAM: Glutamine synthetase, catalytic domain'. (459 aa)
purCPFAM: SAICAR synthetase; 'TIGRFAM: phosphoribosylaminoimidazole-succinocarboxamide synthase; phosphoribosylaminoimidazole-succinocarboxamide synthase, Vibrio type'. (368 aa)
pheTphenylalanyl-tRNA synthetase beta subunit; PFAM: tRNA synthetase B5 domain; Ferredoxin-fold anticodon binding domain; B3/4 domain; Putative tRNA binding domain; 'TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit, non-spirochete bacterial'; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (795 aa)
pheSphenylalanyl-tRNA synthetase, alpha subunit; 'PFAM: tRNA synthetases class II core domain (F); Aminoacyl tRNA synthetase class II, N-terminal domain'; 'TIGRFAM: phenylalanyl-tRNA synthetase, alpha subunit'; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. (327 aa)
Sps_01379PFAM: DNA ligase OB-like domain; ATP dependent DNA ligase domain. (285 aa)
metGmethionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. (694 aa)
Sps_01550Mg chelatase, cobalamin biosynthesis protein CobN; PFAM: CobN/Magnesium Chelatase. (1319 aa)
bioDDethiobiotin synthase; 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. (231 aa)
sucDsuccinyl-CoA synthetase (ADP-forming) alpha subunit; 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. (290 aa)
Sps_05252GMP synthase family protein; PFAM: Glutamine amidotransferase class-I. (238 aa)
fhsPFAM: Formate--tetrahydrofolate ligase; Belongs to the formate--tetrahydrofolate ligase family. (570 aa)
argSarginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase. (581 aa)
trpStryptophanyl-tRNA synthetase; Catalyzes the attachment of tryptophan to tRNA(Trp). Belongs to the class-I aminoacyl-tRNA synthetase family. (335 aa)
argGPFAM: Arginosuccinate synthase; TIGRFAM: argininosuccinate synthase; Belongs to the argininosuccinate synthase family. Type 1 subfamily. (407 aa)
Sps_05608AMP-forming long-chain acyl-CoA synthetase; PFAM: AMP-binding enzyme. (598 aa)
Sps_01770Peptide arylation enzyme; PFAM: AMP-binding enzyme; AMP-binding enzyme C-terminal domain; 'TIGRFAM: 2,3-dihydroxybenzoate-AMP ligase'. (552 aa)
cysSPFAM: tRNA synthetases class I (C) catalytic domain; DALR domain; TIGRFAM: cysteinyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (459 aa)
glnS'PFAM: tRNA synthetases class I (E and Q), catalytic domain; tRNA synthetases class I (E and Q), anti-codon binding domain'; TIGRFAM: glutaminyl-tRNA synthetase. (556 aa)
sucCsuccinyl-CoA synthetase (ADP-forming) beta subunit; 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)
Sps_01975acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; PFAM: AMP-binding enzyme. (587 aa)
Sps_02077propionyl-CoA synthetase; PFAM: AMP-binding enzyme; AMP-binding enzyme C-terminal domain. (654 aa)
Your Current Organism:
Shewanella psychrophila
NCBI taxonomy Id: 225848
Other names: CGMCC 1.6159, JCM 13876, S. psychrophila, Shewanella psychrophila Xiao et al. 2007 emend. Thorell et al. 2019, Shewanella sp. WP2, strain WP2
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