STRINGSTRING
purK purK A7J50_5806 A7J50_5806 atpC atpC atpD atpD atpG atpG atpA atpA atpH atpH atpF atpF atpE atpE atpB atpB A7J50_4009 A7J50_4009 A7J50_4072 A7J50_4072 A7J50_4075 A7J50_4075 A7J50_4117 A7J50_4117 cobB-2 cobB-2 purM purM A7J50_4182 A7J50_4182 ligA ligA A7J50_4320 A7J50_4320 A7J50_4323 A7J50_4323 A7J50_4334 A7J50_4334 A7J50_4336 A7J50_4336 A7J50_4430 A7J50_4430 alaS alaS acsA acsA A7J50_4545 A7J50_4545 A7J50_4552 A7J50_4552 A7J50_4599 A7J50_4599 A7J50_4600 A7J50_4600 queC queC aspS aspS proS proS purT purT purL purL guaA guaA hisS hisS queC-2 queC-2 gluQ gluQ panC panC acsA-2 acsA-2 carB carB leuS leuS mpl mpl A7J50_5172 A7J50_5172 glyS glyS glyQ glyQ A7J50_0123 A7J50_0123 gshA gshA rimK rimK A7J50_0334 A7J50_0334 argS argS purA purA A7J50_0527 A7J50_0527 nadE nadE pncB pncB purD purD A7J50_0599 A7J50_0599 A7J50_0600 A7J50_0600 ddl ddl A7J50_0744 A7J50_0744 ileS ileS trpS trpS gatB gatB gatA gatA gatC gatC A7J50_0923 A7J50_0923 murE murE murF murF murD murD murC murC ddl-2 ddl-2 valS valS A7J50_1079 A7J50_1079 argG argG metG metG A7J50_5717 A7J50_5717 lysS lysS A7J50_1306 A7J50_1306 birA birA tyrS tyrS bioD bioD A7J50_5368 A7J50_5368 ligB ligB A7J50_5469 A7J50_5469 A7J50_5470 A7J50_5470 gshB gshB A7J50_5581 A7J50_5581 A7J50_5583 A7J50_5583 accA accA tilS tilS pyrG pyrG A7J50_1449 A7J50_1449 A7J50_1569 A7J50_1569 A7J50_1570 A7J50_1570 purC purC A7J50_1637 A7J50_1637 A7J50_1932 A7J50_1932 sucC sucC sucD sucD A7J50_1978 A7J50_1978 A7J50_2002 A7J50_2002 A7J50_2085 A7J50_2085 A7J50_2166 A7J50_2166 A7J50_2390 A7J50_2390 A7J50_2435 A7J50_2435 A7J50_2449 A7J50_2449 A7J50_2582 A7J50_2582 A7J50_2605 A7J50_2605 A7J50_2741 A7J50_2741 A7J50_2806 A7J50_2806 A7J50_2832 A7J50_2832 A7J50_2979 A7J50_2979 A7J50_3126 A7J50_3126 A7J50_3160 A7J50_3160 A7J50_3213 A7J50_3213 A7J50_3272 A7J50_3272 A7J50_3330 A7J50_3330 serS serS A7J50_3514 A7J50_3514 cysS cysS glnS glnS A7J50_3549 A7J50_3549 A7J50_3551 A7J50_3551 A7J50_3553 A7J50_3553 A7J50_3689 A7J50_3689 pheT pheT pheS pheS thrS thrS A7J50_3867 A7J50_3867 accD accD gltX gltX A7J50_3909 A7J50_3909 A7J50_3918 A7J50_3918 A7J50_5615 A7J50_5615 A7J50_3998 A7J50_3998
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
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a 3D structure is known or predicted
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purKN5-carboxyaminoimidazole ribonucleotide synthase; Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR). (361 aa)
A7J50_5806Biotin carboxylase; Pfam:pfam02786 Carbamoyl-phosphate synthase L chain, ATP binding domain. (471 aa)
atpCATP synthase F0F1 subunit epsilon; Produces ATP from ADP in the presence of a proton gradient across the membrane. (138 aa)
atpDATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. (459 aa)
atpGATP synthase gamma chain; 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. (286 aa)
atpAATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. (514 aa)
atpHF0F1 ATP synthase subunit delta; 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. (178 aa)
atpFF0F1 ATP synthase subunit B; Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0); Belongs to the ATPase B chain family. (156 aa)
atpEATP synthase subunit c; 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. (85 aa)
atpBF0F1 ATP synthase subunit A; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. Belongs to the ATPase A chain family. (289 aa)
A7J50_4009Long-chain acyl-CoA synthetase; Pfam:pfam00501 AMP-binding enzyme. (608 aa)
A7J50_4072methylcrotonoyl-CoA carboxylase; Pfam:pfam01039 Carboxyl transferase domain. (538 aa)
A7J50_40753-methylcrotonyl-CoA carboxylase subunit alpha; Pfam:pfam02786 Carbamoyl-phosphate synthase L chain, ATP binding domain. (640 aa)
A7J50_4117Pfam:pfam00006 ATP synthase alpha/beta family, nucleotide-binding domain. (452 aa)
cobB-2Cobyrinic acid A,C-diamide synthase; Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of hydrogenobyrinate, using either L- glutamine or ammonia as the nitrogen source; Belongs to the CobB/CbiA family. (467 aa)
purMPhosphoribosylformylglycinamidine cyclo-ligase; Pfam:pfam02769 AIR synthase related protein, C-terminal domain. (352 aa)
A7J50_4182Siderophore synthetase; Pfam:pfam04183 IucA / IucC family. (641 aa)
ligADNA ligase (NAD(+)) LigA; 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; Belongs to the NAD-dependent DNA ligase family. LigA subfamily. (788 aa)
A7J50_4320Sulfurylase; Pfam:pfam00899 ThiF family. (620 aa)
A7J50_4323threonyl-tRNA synthetase; Pfam:pfam07973 Threonyl and Alanyl tRNA synthetase second additional domain. (242 aa)
A7J50_4334Hypothetical protein; Pfam:pfam05618 Putative ATP-dependant zinc protease. (181 aa)
A7J50_4336Alpha-L-glutamate ligase; Pfam:pfam14397 Sugar-transfer associated ATP-grasp. (328 aa)
A7J50_4430Hypothetical protein; Pfam:pfam04174 A circularly permuted ATPgrasp. (469 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. (872 aa)
acsAacetyl-CoA 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. (651 aa)
A7J50_4545Hypothetical protein. (242 aa)
A7J50_4552Hypothetical protein; Pfam:pfam00117 Glutamine amidotransferase class-I. (235 aa)
A7J50_4599Long-chain fatty acid--CoA ligase; Pfam:pfam00501 AMP-binding enzyme. (563 aa)
A7J50_4600Long-chain fatty acid--CoA ligase; Pfam:pfam00501 AMP-binding enzyme. (562 aa)
queC7-cyano-7-deazaguanine synthase; Catalyzes the ATP-dependent conversion of 7-carboxy-7- deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)). Belongs to the QueC family. (225 aa)
aspSAspartate--tRNA(Asp/Asn) ligase; 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. (591 aa)
proSProline--tRNA ligase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). 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 deacy [...] (571 aa)
purTPhosphoribosylglycinamide formyltransferase 2; Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate; Belongs to the PurK/PurT family. (393 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. (1298 aa)
guaAGMP synthase; Catalyzes the synthesis of GMP from XMP. (525 aa)
hisSPfam:pfam00587 tRNA synthetase class II core domain (G, H, P, S and T). (429 aa)
queC-2Queuosine 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. (232 aa)
gluQglutamyl-Q tRNA(Asp) ligase; 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. (295 aa)
panCPantoate--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)
acsA-2acetyl-CoA 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. (645 aa)
carBPfam:pfam02786 Carbamoyl-phosphate synthase L chain, ATP binding domain; Belongs to the CarB family. (1073 aa)
leuSleucine--tRNA ligase; Pfam:pfam13603 Leucyl-tRNA synthetase, Domain 2; Belongs to the class-I aminoacyl-tRNA synthetase family. (868 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. (449 aa)
A7J50_5172Pfam:pfam03738 Glutathionylspermidine synthase preATP-grasp. (385 aa)
glySPfam:pfam02092 Glycyl-tRNA synthetase beta subunit. (684 aa)
glyQPfam:pfam02091 Glycyl-tRNA synthetase alpha subunit. (317 aa)
A7J50_0123Pfam:pfam11583 P-aminobenzoate N-oxygenase AurF. (315 aa)
gshAPfam:pfam04262 Glutamate-cysteine ligase; Belongs to the glutamate--cysteine ligase type 1 family. Type 1 subfamily. (527 aa)
rimKalpha-L-glutamate ligase; Pfam:pfam08443 RimK-like ATP-grasp domain; Belongs to the RimK family. (301 aa)
A7J50_0334Pfam:pfam00120 Glutamine synthetase, catalytic domain. (468 aa)
argSPfam:pfam00750 tRNA synthetases class I (R). (578 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. (429 aa)
A7J50_0527Hypothetical protein; Pfam:pfam04174 A circularly permuted ATPgrasp. (828 aa)
nadENAD synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source; Belongs to the NAD synthetase family. (275 aa)
pncBNicotinate phosphoribosyltransferase; Catalyzes the synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP; Belongs to the NAPRTase family. (404 aa)
purDPhosphoribosylamine--glycine ligase; Pfam:pfam01071 Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Belongs to the GARS family. (430 aa)
A7J50_0599acetyl-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. (453 aa)
A7J50_0600acetyl-CoA carboxylase biotin carboxyl carrier protein; 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. (152 aa)
ddlD-alanine--D-alanine ligase; Cell wall formation; Belongs to the D-alanine--D-alanine ligase family. (364 aa)
A7J50_0744Molybdopterin biosynthesis protein MoeB; Pfam:pfam00899 ThiF family. (251 aa)
ileSisoleucine--tRNA ligase; 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. (943 aa)
trpSTryptophan--tRNA ligase; Catalyzes the attachment of tryptophan to tRNA(Trp). Belongs to the class-I aminoacyl-tRNA synthetase family. (455 aa)
gatBglutamyl-tRNA amidotransferase; 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. (481 aa)
gatAglutamyl-tRNA amidotransferase; 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). (483 aa)
gatCAspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C; 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. (95 aa)
A7J50_0923Long-chain-fatty-acid--CoA ligase; Pfam:pfam00501 AMP-binding enzyme. (560 aa)
murEUDP-N-acetylmuramoylalanyl-D-glutamate--2, 6-diaminopimelate ligase; 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. Belongs to the MurCDEF family. MurE subfamily. (487 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. (456 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. (448 aa)
murCUDP-N-acetylmuramate--alanine ligase; Cell wall formation; Belongs to the MurCDEF family. (481 aa)
ddl-2D-alanine--D-alanine ligase; Cell wall formation; Belongs to the D-alanine--D-alanine ligase family. (318 aa)
valSValine--tRNA ligase; 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. (948 aa)
A7J50_1079Hypothetical protein; Pfam:pfam01425 Amidase; Belongs to the amidase family. (443 aa)
argGPfam:pfam00764 Arginosuccinate synthase; Belongs to the argininosuccinate synthase family. Type 1 subfamily. (405 aa)
metGMethionine--tRNA ligase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. (683 aa)
A7J50_5717Bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; 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. (402 aa)
lysSPfam:pfam00152 tRNA synthetases class II (D, K and N); Belongs to the class-II aminoacyl-tRNA synthetase family. (500 aa)
A7J50_1306Thiamine biosynthesis protein ThiF; Pfam:pfam00899 ThiF family. (271 aa)
birABiotin--protein 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. (319 aa)
tyrSTyrosine--tRNA ligase; 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. (399 aa)
bioDATP-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) to form an ureido ring. (226 aa)
A7J50_5368Hypothetical protein; Pfam:pfam05618 Putative ATP-dependant zinc protease. (171 aa)
ligBNAD-dependent DNA ligase LigB; 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. Belongs to the NAD-dependent DNA ligase family. LigB subfamily. (554 aa)
A7J50_5469Pfam:pfam06833 Malonate decarboxylase gamma subunit (MdcE). (256 aa)
A7J50_5470Malonate decarboxylase subunit beta; Pfam:pfam01039 Carboxyl transferase domain. (280 aa)
gshBPfam:pfam02955 Prokaryotic glutathione synthetase, ATP-grasp domain; Belongs to the prokaryotic GSH synthase family. (317 aa)
A7J50_5581Pfam:pfam00120 Glutamine synthetase, catalytic domain. (452 aa)
A7J50_5583Pfam:pfam00120 Glutamine synthetase, catalytic domain. (458 aa)
accAacetyl-CoA carboxylase 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. (315 aa)
tilStRNA(Ile)-lysidine synthase; 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. (439 aa)
pyrGCTP synthetase; 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. (543 aa)
A7J50_1449Pfam:pfam01068 ATP dependent DNA ligase domain. (544 aa)
A7J50_1569Allophanate hydrolase; Pfam:pfam01425 Amidase. (590 aa)
A7J50_1570Urea carboxylase; Pfam:pfam02626 Allophanate hydrolase subunit 2. (1230 aa)
purCPhosphoribosylaminoimidazole-succinocarboxamide synthase; Pfam:pfam01259 SAICAR synthetase. (237 aa)
A7J50_1637Pfam:pfam00120 Glutamine synthetase, catalytic domain. (456 aa)
A7J50_1932Glyoxylate carboligase; Pfam:pfam02776 Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Belongs to the TPP enzyme family. (591 aa)
sucCSuccinyl-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. (404 aa)
sucDSuccinyl-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. (293 aa)
A7J50_1978AMP-binding acetyl-CoA synthetase; Pfam:pfam00501 AMP-binding enzyme. (549 aa)
A7J50_2002alanyl-tRNA synthetase. (208 aa)
A7J50_2085Membrane protein; Pfam:pfam13425 O-antigen ligase like membrane protein. (477 aa)
A7J50_2166Pfam:pfam00120 Glutamine synthetase, catalytic domain. (448 aa)
A7J50_2390Putative acetoacetyl-coenzyme A synthetase; Pfam:pfam00501 AMP-binding enzyme. (652 aa)
A7J50_2435Cobaltochelatase subunit CobN; Pfam:pfam02514 CobN/Magnesium Chelatase. (1253 aa)
A7J50_2449Pfam:pfam00120 Glutamine synthetase, catalytic domain. (452 aa)
A7J50_2582Long-chain fatty acid--CoA ligase; Pfam:pfam00501 AMP-binding enzyme. (567 aa)
A7J50_2605Carboxylate--amine ligase; Pfam:pfam14401 RimK-like ATPgrasp N-terminal domain. (528 aa)
A7J50_2741Pfam:pfam13298 DNA polymerase Ligase (LigD). (824 aa)
A7J50_2806Hypothetical protein; Pfam:pfam04174 A circularly permuted ATPgrasp. (469 aa)
A7J50_2832Putative long-chain-fatty-acid-CoA ligase; Pfam:pfam00501 AMP-binding enzyme. (492 aa)
A7J50_2979Pfam:pfam00501 AMP-binding enzyme. (549 aa)
A7J50_3126Ester cyclase; Pfam:pfam07366 SnoaL-like polyketide cyclase. (130 aa)
A7J50_3160Amidase; Pfam:pfam01425 Amidase. (565 aa)
A7J50_3213Hypothetical protein; Pfam:pfam13519 von Willebrand factor type A domain. (362 aa)
A7J50_3272Pyoverdine non-ribosomal peptide synthetase; Pfam:pfam00501 AMP-binding enzyme. (3950 aa)
A7J50_3330AMP-dependent synthetase; Pfam:pfam00501 AMP-binding enzyme. (511 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). (426 aa)
A7J50_3514acyl-CoA synthetase. (303 aa)
cysSCysteine--tRNA ligase; Pfam:pfam01406 tRNA synthetases class I (C) catalytic domain; Belongs to the class-I aminoacyl-tRNA synthetase family. (462 aa)
glnSglutamate--tRNA ligase; Pfam:pfam00749 tRNA synthetases class I (E and Q), catalytic domain. (566 aa)
A7J50_3549AMP-binding domain protein; Pfam:pfam00501 AMP-binding enzyme. (542 aa)
A7J50_3551methylcrotonoyl-CoA carboxylase; Pfam:pfam01039 Carboxyl transferase domain. (535 aa)
A7J50_35533-methylcrotonyl-CoA carboxylase subunit alpha; Pfam:pfam02786 Carbamoyl-phosphate synthase L chain, ATP binding domain. (641 aa)
A7J50_3689Pfam:pfam10703 Molybdenum cofactor biosynthesis protein F. (273 aa)
pheTphenylalanyl-tRNA synthetase; Pfam:pfam03483 B3/4 domain; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (792 aa)
pheSPhenylalanine--tRNA ligase alpha subunit; Pfam:pfam01409 tRNA synthetases class II core domain (F); Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. (338 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). (640 aa)
A7J50_3867Folylpolyglutamate synthase; Pfam:pfam08245 Mur ligase middle domain; Belongs to the folylpolyglutamate synthase family. (435 aa)
accDacetyl-CoA carboxylase 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; Belongs to the AccD/PCCB family. (306 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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. (493 aa)
A7J50_3909Pfam:pfam09825 Biotin-protein ligase, N terminal. (246 aa)
A7J50_3918Pfam:pfam00587 tRNA synthetase class II core domain (G, H, P, S and T). (190 aa)
A7J50_5615Pfam:pfam01812 5-formyltetrahydrofolate cyclo-ligase family; Belongs to the 5-formyltetrahydrofolate cyclo-ligase family. (209 aa)
A7J50_3998Asparagine synthetase; Pfam:pfam13537 Glutamine amidotransferase domain. (590 aa)
Your Current Organism:
Pseudomonas antarctica
NCBI taxonomy Id: 219572
Other names: CCUG 49625, DSM 15318, LMG 22709, LMG:22709, MTCC 4992, Pseudomonas antarctica Reddy et al. 2004, strain CMS 35
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