STRINGSTRING
AFA71122.1 AFA71122.1 AFA71141.1 AFA71141.1 AFA71157.1 AFA71157.1 accC accC AFA71162.1 AFA71162.1 hypF hypF AFA71222.1 AFA71222.1 AFA71302.1 AFA71302.1 acsA1 acsA1 lig lig lysS1 lysS1 serS serS AFA71488.1 AFA71488.1 pccB pccB AFA71586.1 AFA71586.1 AFA71727.1 AFA71727.1 AFA71736.1 AFA71736.1 acsA2 acsA2 AFA71883.1 AFA71883.1 AFA71907.1 AFA71907.1 AFA71941.1 AFA71941.1 AFA71944.1 AFA71944.1 AFA71963.1 AFA71963.1 cysS cysS AFA72087.1 AFA72087.1 AFA72121.1 AFA72121.1 AFA72190.1 AFA72190.1 AFA72215.1 AFA72215.1 AFA72254.1 AFA72254.1 AFA72255.1 AFA72255.1 AFA72259.1 AFA72259.1 AFA72260.1 AFA72260.1 AFA72307.1 AFA72307.1 metG metG asnB1 asnB1 AFA72485.1 AFA72485.1 AFA72609.1 AFA72609.1 guaA guaA trpS trpS pyc pyc AFA72772.1 AFA72772.1 AFA72778.1 AFA72778.1 AFA72779.1 AFA72779.1 birA birA purK purK AFA72790.1 AFA72790.1 argS argS atpB atpB atpE atpE atpF atpF atpFH atpFH atpA atpA atpG atpG atpD atpD atpC atpC pncB pncB AFA72931.1 AFA72931.1 valS valS folC folC cobB cobB proS proS AFA73112.1 AFA73112.1 thrS thrS hisS hisS aspS aspS AFA73254.1 AFA73254.1 alaS alaS AFA73277.1 AFA73277.1 carA carA carB carB coaBC coaBC AFA73321.1 AFA73321.1 AFA73355.1 AFA73355.1 AFA73369.1 AFA73369.1 AFA73387.1 AFA73387.1 mshC mshC pafA pafA cobN cobN lcfB1 lcfB1 menE menE AFA73562.1 AFA73562.1 AFA73575.1 AFA73575.1 pyrG pyrG tyrS tyrS argG argG pheT pheT pheS pheS AFA73719.1 AFA73719.1 bioD bioD ileS ileS murC murC murD murD murF1 murF1 murE murE lcfB2 lcfB2 asnB2 asnB2 glnA1 glnA1 glnA2 glnA2 accD6 accD6 lcfB3 lcfB3 glyQS glyQS AFA73977.1 AFA73977.1 gltX1 gltX1 gatB gatB gatA gatA gatC gatC ligA ligA ligD ligD cofE cofE lcfB4 lcfB4 purA1 purA1 AFA74266.1 AFA74266.1 AFA74352.1 AFA74352.1 AFA74360.1 AFA74360.1 mOCS3 mOCS3 AFA74397.1 AFA74397.1 AFA74486.1 AFA74486.1 AFA74600.1 AFA74600.1 AFA74632.1 AFA74632.1 AFA74702.1 AFA74702.1 AFA74703.1 AFA74703.1 AFA74709.1 AFA74709.1 AFA74820.1 AFA74820.1 AFA74842.1 AFA74842.1 sucD sucD sucC sucC glnN glnN AFA74912.1 AFA74912.1 AFA74967.1 AFA74967.1 AFA75017.1 AFA75017.1 AFA75041.1 AFA75041.1 nadE nadE purM purM purL purL AFA75149.1 AFA75149.1 AFA75154.1 AFA75154.1 paaF paaF AFA75187.1 AFA75187.1 purQ purQ purS purS purC purC purD purD AFA75272.1 AFA75272.1 AFA75276.1 AFA75276.1 AFA75291.1 AFA75291.1 AFA75292.1 AFA75292.1 AFA75293.1 AFA75293.1 AFA75294.1 AFA75294.1 AFA75301.1 AFA75301.1 AFA75315.1 AFA75315.1 AFA75316.1 AFA75316.1 AFA75324.1 AFA75324.1 lysS2 lysS2 panC panC tilS tilS purT purT purA2 purA2 AFA75697.1 AFA75697.1 AFA75698.1 AFA75698.1 AFA75710.1 AFA75710.1 AFA75719.1 AFA75719.1 AFA75720.1 AFA75720.1 gltX2 gltX2 murF2 murF2 ddl ddl AFA75890.1 AFA75890.1 AFA75923.1 AFA75923.1 AFA75924.1 AFA75924.1 AFA75927.1 AFA75927.1 AFA75940.1 AFA75940.1 leuS leuS
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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AFA71122.1Glutamate--ammonia ligase; Belongs to the glutamine synthetase family. (448 aa)
AFA71141.1Putative fatty-acid--CoA ligase. (513 aa)
AFA71157.1Putative long-chain-fatty-acid-CoA ligase. (499 aa)
accCBiotin carboxylase AccC. (457 aa)
AFA71162.1Putative carboxyltransferase. (499 aa)
hypFCarbamoyltransferase HypF. (788 aa)
AFA71222.1Putative medium-chain-fatty-acid--CoA ligase. (539 aa)
AFA71302.1Putative CoA ligase. (523 aa)
acsA1Acetyl-coenzyme A synthetase AcsA. (531 aa)
ligDNA ligase Lig. (511 aa)
lysS1lysyl-tRNA synthetase LysS; Belongs to the class-II aminoacyl-tRNA synthetase family. (1133 aa)
serSseryl-tRNA synthetase SerS; 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). (418 aa)
AFA71488.1Putative long-chain-fatty-acid--AMP ligase. (640 aa)
pccBpropionyl-CoA carboxylase beta chain PccB. (515 aa)
AFA71586.1Putative ATP-dependent DNA ligase. (812 aa)
AFA71727.1Hypothetical protein. (387 aa)
AFA71736.1Condensation domain-containing protein. (488 aa)
acsA2Acetyl-coenzyme A synthetase AcsA; 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)
AFA71883.1Carboxylate-amine ligase; ATP-dependent carboxylate-amine ligase which exhibits weak glutamate--cysteine ligase activity; Belongs to the glutamate--cysteine ligase type 2 family. YbdK subfamily. (376 aa)
AFA71907.1Hypothetical protein. (158 aa)
AFA71941.1Putative long-chain-fatty-acid--CoA ligase. (555 aa)
AFA71944.1Putative long-chain-fatty-acid--CoA ligase. (584 aa)
AFA71963.1Putative fatty-acid--CoA ligase. (509 aa)
cysScysteinyl-tRNA synthetase CysS; Belongs to the class-I aminoacyl-tRNA synthetase family. (464 aa)
AFA72087.1Putative 4-coumarate--CoA ligase. (534 aa)
AFA72121.1Putative acyl-CoA ligase. (566 aa)
AFA72190.1Putative o-succinylbenzoate--CoA ligase. (275 aa)
AFA72215.1Putative UBA/THIF-type NAD/FAD binding protein. (383 aa)
AFA72254.1Putative acetyl/propionyl CoA carboxylase, beta subunit. (536 aa)
AFA72255.1Putative acetyl/propionyl CoA carboxylase, alpha subunit. (701 aa)
AFA72259.1Putative fatty-acid--CoA ligase. (561 aa)
AFA72260.1acetoacetyl-CoA synthetase. (667 aa)
AFA72307.15-formyltetrahydrofolate cyclo-ligase; Belongs to the 5-formyltetrahydrofolate cyclo-ligase family. (194 aa)
metGmethionyl-tRNA synthetase MetG; 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. (534 aa)
asnB1Asparagine synthetase; Glutamine-hydrolysing. (613 aa)
AFA72485.1Putative biotin carboxylase. (1089 aa)
AFA72609.1Putative fatty-acid--CoA ligase. (505 aa)
guaAGMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP. (528 aa)
trpStryptophanyl-tRNA synthetase TrpS; Catalyzes the attachment of tryptophan to tRNA(Trp). Belongs to the class-I aminoacyl-tRNA synthetase family. (346 aa)
pycPyruvate carboxylase Pyc; 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. (1129 aa)
AFA72772.1Putative acetyl-/propionyl-CoA carboxylase alpha chain. (597 aa)
AFA72778.1Hypothetical protein. (81 aa)
AFA72779.1propionyl-CoA carboxylase beta chain. (542 aa)
birAbiotin-[acetyl-CoA-carboxylase] ligase BirA. (275 aa)
purKPhosphoribosylaminoimidazole carboxylase, ATPase subunit PurK; Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR). (397 aa)
AFA72790.1Hypothetical protein. (237 aa)
argSarginyl-tRNA synthetase ArgS. (550 aa)
atpBATP synthase subunit a; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. (252 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. (87 aa)
atpFATP 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. (170 aa)
atpFHATP synthase subunit b-delta; Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). 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; Belongs to the ATPase delta chain family. (449 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. Belongs to the ATPase alpha/beta chains family. (542 aa)
atpGATP synthase gamma chain AtpG; 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. (315 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; Belongs to the ATPase alpha/beta chains family. (482 aa)
atpCATP synthase epsilon chain AtpC; Produces ATP from ADP in the presence of a proton gradient across the membrane. (126 aa)
pncBNicotinate phosphoribosyltransferase PncB; 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. (432 aa)
AFA72931.1Putative long-chain-fatty-acid--CoA ligase. (594 aa)
valSvalyl-tRNA synthetase ValS; 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. (881 aa)
folCDihydrofolate synthase / folylpolyglutamate synthase FolC. (545 aa)
cobBCobyrinic acid a,c-diamide synthase CobB; 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. (522 aa)
proSprolyl-tRNA synthetase ProS; 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 involve [...] (580 aa)
AFA73112.1AMP-binding domain-containing protein. (1164 aa)
thrSthreonyl-tRNA synthetase ThrS; Belongs to the class-II aminoacyl-tRNA synthetase family. (689 aa)
hisShistidyl-tRNA synthetase HisS. (421 aa)
aspSaspartyl-tRNA synthetase AspS; 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. (612 aa)
AFA73254.1Hypothetical protein. (918 aa)
alaSalanyl-tRNA synthetase AlaS; 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. (901 aa)
AFA73277.1Hypothetical protein. (206 aa)
carACarbamoyl-phosphate synthase small chain CarA; Belongs to the CarA family. (389 aa)
carBCarbamoyl-phosphate synthase large chain CarB; Belongs to the CarB family. (1116 aa)
coaBCCoenzyme A biosynthesis bifunctional protein CoaBC; 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. (432 aa)
AFA73321.1Hypothetical protein. (129 aa)
AFA73355.1Putative fatty-acid--CoA ligase. (515 aa)
AFA73369.1Von Willebrand factor type A domain-containing protein. (325 aa)
AFA73387.1Putative 2,3-dihydroxybenzoate-AMP ligase. (525 aa)
mshCL-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase MshC; Catalyzes the ATP-dependent condensation of GlcN-Ins and L- cysteine to form L-Cys-GlcN-Ins; Belongs to the class-I aminoacyl-tRNA synthetase family. MshC subfamily. (413 aa)
pafAPup--protein ligase PafA; Catalyzes the covalent attachment of the prokaryotic ubiquitin-like protein modifier Pup to the proteasomal substrate proteins, thereby targeting them for proteasomal degradation. This tagging system is termed pupylation. The ligation reaction involves the side-chain carboxylate of the C-terminal glutamate of Pup and the side- chain amino group of a substrate lysine. (452 aa)
cobNAerobic cobaltochelatase subunit CobN. (1218 aa)
lcfB1long-chain-fatty-acid--CoA ligase LcfB. (490 aa)
menE2-succinylbenzoate--CoA ligase MenE. (534 aa)
AFA73562.1AMP-dependent synthetase and ligase. (480 aa)
AFA73575.1AMP-dependent synthetase and ligase. (511 aa)
pyrGCTP synthase PyrG; 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. (561 aa)
tyrStyrosyl-tRNA synthetase TyrS; 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. (433 aa)
argGArgininosuccinate synthase ArgG; Belongs to the argininosuccinate synthase family. Type 1 subfamily. (400 aa)
pheTphenylalanyl-tRNA synthetase beta chain PheT; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (823 aa)
pheSphenylalanyl-tRNA synthetase alpha chain PheS; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. (358 aa)
AFA73719.1AMP-binding enzyme. (610 aa)
bioDDethiobiotin 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. (248 aa)
ileSisoleucyl-tRNA synthetase IleS; 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 2 subfamily. (1089 aa)
murCUDP-N-acetylmuramate--L-alanine ligase MurC; Cell wall formation; Belongs to the MurCDEF family. (544 aa)
murDUDP-N-acetylmuramoylalanine--D-glutamate ligase MurD; Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). Belongs to the MurCDEF family. (540 aa)
murF1UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D- alanine ligase MurF. (198 aa)
murEUDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2, 6-diaminopimelate ligase MurE; 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. (497 aa)
lcfB2long-chain-fatty-acid--CoA ligase LcfB. (642 aa)
asnB2Asparagine synthetase. (638 aa)
glnA1Glutamine synthetase 1. (477 aa)
glnA2Glutamine synthetase 2. (450 aa)
accD6propionyl-CoA carboxylase beta chain 6. (483 aa)
lcfB3long-chain-fatty-acid--CoA ligase LcfB. (550 aa)
glyQSglycyl-tRNA synthetase; Catalyzes the attachment of glycine to tRNA(Gly). Belongs to the class-II aminoacyl-tRNA synthetase family. (466 aa)
AFA73977.1Hypothetical protein. (547 aa)
gltX1glutamyl-tRNA synthetase GltX; 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. (502 aa)
gatBaspartyl/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); Belongs to the GatB/GatE family. GatB subfamily. (502 aa)
gatAglutamyl-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). (497 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. (107 aa)
ligADNA ligase 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. (693 aa)
ligDDNA polymerase LigD. (318 aa)
cofEF420-0:gamma-glutamyl ligase CofE. (455 aa)
lcfB4long-chain-fatty-acid--CoA ligase LcfB. (589 aa)
purA1Adenylosuccinate synthetase PurA; 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. (466 aa)
AFA74266.1AMP-dependent synthetase and ligase. (611 aa)
AFA74352.1propionate-CoA ligase protein. (637 aa)
AFA74360.1Hypothetical protein. (330 aa)
mOCS3Adenylyltransferase and sulfurtransferase MOCS3. (384 aa)
AFA74397.1Biotinylated protein. (73 aa)
AFA74486.1Putative 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase; Belongs to the TPP enzyme family. (680 aa)
AFA74600.1Hypothetical protein. (112 aa)
AFA74632.1Asparagine synthase family amidotransferase. (600 aa)
AFA74702.1Putative acetyl/propionyl-CoA carboxylase alpha subunit. (712 aa)
AFA74703.1Putative acetyl/propionyl-CoA carboxylase beta subunit. (532 aa)
AFA74709.1Putative acyl-CoA synthetase. (531 aa)
AFA74820.1Putative long-chain-fatty-acid--CoA ligase. (533 aa)
AFA74842.1Putative carboxyl transferase. (644 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. (300 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. (387 aa)
glnNGlutamine synthetase, type 3. (723 aa)
AFA74912.1Von Willebrand factor type A domain-containing protein. (575 aa)
AFA74967.1Putative o-succinylbenzoate--CoA ligase. (576 aa)
AFA75017.1ThiF family protein. (334 aa)
AFA75041.1Putative long-chain-fatty-acid--CoA ligase. (560 aa)
nadENAD+ synthase NadE; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. (675 aa)
purMPhosphoribosylformylglycinamidine cyclo-ligase PurM. (373 aa)
purLPhosphoribosylformylglycinamidine synthase 2; 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 [...] (763 aa)
AFA75149.1Von Willebrand factor type A domain-containing protein. (322 aa)
AFA75154.1Putative fatty-acid--CoA ligase. (564 aa)
paaFphenylacetate-CoA ligase PaaF; Catalyzes the activation of phenylacetic acid (PA) to phenylacetyl-CoA (PA-CoA). (438 aa)
AFA75187.1Putative acyl--CoA ligase. (578 aa)
purQPhosphoribosylformylglycinamidine synthase 1; 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 [...] (227 aa)
purSPhosphoribosylformylglycinamidine synthase, PurS subunit PurS; 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 th [...] (79 aa)
purCPhosphoribosylaminoimidazole-succinocarboxamide synthase PurC; Belongs to the SAICAR synthetase family. (295 aa)
purDPhosphoribosylamine--glycine ligase PurD; Belongs to the GARS family. (417 aa)
AFA75272.1Putative fatty-acid--CoA ligase. (511 aa)
AFA75276.1Putative fatty-acid--CoA ligase. (486 aa)
AFA75291.1Putative glycosyltransferase. (266 aa)
AFA75292.1Condensation domain-containing protein. (448 aa)
AFA75293.1Condensation domain-containing protein. (483 aa)
AFA75294.1Condensation domain-containing protein. (492 aa)
AFA75301.1Putative fatty-acid--CoA ligase. (539 aa)
AFA75315.1Putative fatty-acid--CoA ligase. (531 aa)
AFA75316.1Putative fatty-acid--CoA ligase. (535 aa)
AFA75324.1Putative fatty-acid--CoA ligase. (515 aa)
lysS2lysyl-tRNA synthetase LysS; Belongs to the class-II aminoacyl-tRNA synthetase family. (511 aa)
panCPantothenate synthetase PanC; Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. Belongs to the pantothenate synthetase family. (306 aa)
tilStRNA(Ile)-lysidine synthase TilS; 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. (316 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. (546 aa)
purA2Adenylosuccinate synthetase PurA; 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. (428 aa)
AFA75697.1Putative UDP-N-acetylmuramyl tripeptide synthase; Mur ligase. (430 aa)
AFA75698.1CobB/CobQ domain-containing protein. (239 aa)
AFA75710.1AMP-binding domain-containing protein. (508 aa)
AFA75719.1DNA primase, small subunit. (358 aa)
AFA75720.1ATP-dependent DNA ligase. (356 aa)
gltX2glutamyl-tRNA synthetase GltX; Belongs to the class-I aminoacyl-tRNA synthetase family. (285 aa)
murF2UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D- alanine ligase MurF; 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. (439 aa)
ddlD-alanine-D-alanine ligase; Cell wall formation; Belongs to the D-alanine--D-alanine ligase family. (358 aa)
AFA75890.1Putative AMP-binding protein. (491 aa)
AFA75923.1Hypothetical protein. (473 aa)
AFA75924.1ThiF domain-containing protein. (349 aa)
AFA75927.1AMP-binding domain-containing protein. (473 aa)
AFA75940.1AMP-binding domain-containing protein. (549 aa)
leuSleucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (958 aa)
Your Current Organism:
Gordonia polyisoprenivorans
NCBI taxonomy Id: 1112204
Other names: G. polyisoprenivorans VH2, Gordonia polyisoprenivorans VH2, Gordonia polyisoprenivorans str. VH2, Gordonia polyisoprenivorans strain VH2
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