STRINGSTRING
hisC hisC hisH hisH hisA hisA hisF hisF hisI hisI wcaB wcaB yfbQ yfbQ usg usg aroC aroC cysZ cysZ cysK cysK cysM cysM dapE dapE dapA dapA glyA glyA pheA pheA tyrA tyrA aroF aroF cysI cysI cysJ cysJ argA argA lysA lysA lysR lysR ygeX ygeX ygfK ygfK serA serA argG argG gltB gltB gltD gltD argR argR aroE aroE argD argD aroB aroB aroK aroK asd asd cysE cysE ilvN ilvN ilvB ilvB asnA asnA ilvL ilvL ilvG ilvG ilvM ilvM ilvE ilvE ilvD ilvD ilvA ilvA ilvC ilvC dapF dapF metR metR metE metE glnA glnA metJ metJ metL metL metF metF argE argE ivbL ivbL leuL leuL serB serB yjgM yjgM argI argI yjgF yjgF alr alr lysC lysC metH metH metA metA argH argH argB argB argC argC thrA thrA thrB thrB thrC thrC dapB dapB carA carA carB carB folA folA leuD leuD leuC leuC leuB leuB leuA leuA ilvI ilvI ilvH ilvH panD panD pfs pfs dapD dapD proB proB proA proA proC proC aroL aroL aroM aroM folD folD asnB asnB aroG aroG ybiB ybiB serS serS serC serC aroA aroA putA putA trpA trpA trpB trpB trpC trpC trpD trpD trpE trpE cysB cysB puuA puuA ydiB ydiB aroD aroD aroH aroH astC astC selD selD hisG hisG hisD hisD hisB hisB
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.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
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
Others
textmining
co-expression
protein homology
Your Input:
hisCHistidinol-phosphate aminotransferase; Function experimentally demonstrated in the studied species; enzyme. (356 aa)
hisHImidazole glycerol phosphate synthase, glutamine amidotransferase subunit with HisF; Function experimentally demonstrated in the studied species; enzyme. (196 aa)
hisAN-(5'-phospho-L-ribosyl-formimino)-5-amino-1- (5'-phosphoribosyl)-4-imidazolecarboxamide isomerase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the HisA/HisF family. (245 aa)
hisFImidazole glycerol phosphate synthase, catalytic subunit with HisH; Function experimentally demonstrated in the studied species; enzyme; Belongs to the HisA/HisF family. (258 aa)
hisIFused phosphoribosyl-AMP cyclohydrolase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the PRA-PH family. (202 aa)
wcaBPutative acyl transferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (162 aa)
yfbQPutative aminotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (405 aa)
usgPutative semialdehyde dehydrogenase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (337 aa)
aroCChorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. (361 aa)
cysZPutative inner membrane protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative transporter. (253 aa)
cysKCysteine synthase A, O-acetylserine sulfhydrolase A subunit; Function experimentally demonstrated in the studied species; enzyme; Belongs to the cysteine synthase/cystathionine beta- synthase family. (323 aa)
cysMCysteine synthase B (O-acetylserine sulfhydrolase B); Function experimentally demonstrated in the studied species; enzyme. (303 aa)
dapEN-succinyl-diaminopimelate deacylase; Function experimentally demonstrated in the studied species; enzyme. (375 aa)
dapADihydrodipicolinate synthase; Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). (292 aa)
glyASerine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. (417 aa)
pheAFused chorismate mutase P; Function experimentally demonstrated in the studied species; enzyme. (386 aa)
tyrAFused chorismate mutase T; Function experimentally demonstrated in the studied species; enzyme. (373 aa)
aroF3-deoxy-D-arabino-heptulosonate-7-phosphate synthase, tyrosine-repressible; Function experimentally demonstrated in the studied species; enzyme. (356 aa)
cysISulfite reductase, beta subunit, NAD(P)-binding, heme-binding; Function experimentally demonstrated in the studied species; enzyme. (570 aa)
cysJSulfite reductase, alpha subunit, flavoprotein; Function experimentally demonstrated in the studied species; enzyme. (599 aa)
argAFused acetylglutamate kinase homolog (inactive); Function experimentally demonstrated in the studied species; enzyme; Belongs to the acetyltransferase family. ArgA subfamily. (443 aa)
lysADiaminopimelate decarboxylase, PLP-binding; Function experimentally demonstrated in the studied species; enzyme. (420 aa)
lysRDNA-binding transcriptional dual regulator; Function experimentally demonstrated in the studied species; regulator. (311 aa)
ygeX2,3-diaminopropionate ammonia-lyase; Function experimentally demonstrated in the studied species; enzyme. (398 aa)
ygfKPutative oxidoreductase, Fe-S subunit; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative carrier. (1032 aa)
serAD-3-phosphoglycerate dehydrogenase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. (410 aa)
argGArgininosuccinate synthetase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the argininosuccinate synthase family. Type 2 subfamily. (447 aa)
gltBGlutamate synthase, large subunit; Function experimentally demonstrated in the studied species; enzyme. (1517 aa)
gltDGlutamate synthase, 4Fe-4S protein, small subunit; Function experimentally demonstrated in the studied species; carrier. (472 aa)
argRDNA-binding transcriptional dual regulator, L-arginine-binding; Regulates arginine biosynthesis genes. (156 aa)
aroEDehydroshikimate reductase, NAD(P)-binding; Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). (272 aa)
argDBifunctional acetylornithine aminotransferase and succinyldiaminopimelate aminotransferase; Involved in both the arginine and lysine biosynthetic pathways; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily. (406 aa)
aroB3-dehydroquinate synthase; Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). (362 aa)
aroKShikimate kinase I; Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate; Belongs to the shikimate kinase family. (173 aa)
asdAspartate-semialdehyde dehydrogenase, NAD(P)-binding; Catalyzes the NADPH-dependent formation of L-aspartate- semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl- 4-phosphate; Belongs to the aspartate-semialdehyde dehydrogenase family. (367 aa)
cysESerine acetyltransferase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the transferase hexapeptide repeat family. (273 aa)
ilvNAcetolactate synthase I, small subunit; Function experimentally demonstrated in the studied species; enzyme. (96 aa)
ilvBAcetolactate synthase I, large subunit; Function experimentally demonstrated in the studied species; enzyme. (562 aa)
asnAAsparagine synthetase A; Function experimentally demonstrated in the studied species; enzyme. (330 aa)
ilvLilvG operon leader peptide; Function experimentally demonstrated in the studied species; leader peptide. (32 aa)
ilvGAcetolactate synthase isozyme II large subunit; Function of strongly homologous gene; enzyme. (548 aa)
ilvMAcetolactate synthase II, small subunit; Function experimentally demonstrated in the studied species; enzyme. (87 aa)
ilvEBranched-chain amino-acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. (309 aa)
ilvDDihydroxyacid dehydratase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the IlvD/Edd family. (616 aa)
ilvAThreonine deaminase; Function experimentally demonstrated in the studied species; enzyme. (514 aa)
ilvCKetol-acid reductoisomerase, NAD(P)-binding; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. (491 aa)
dapFDiaminopimelate epimerase; Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- lysine and an essential component of the bacterial peptidoglycan. (274 aa)
metRDNA-binding transcriptional activator, homocysteine-binding; Function experimentally demonstrated in the studied species; regulator; Belongs to the LysR transcriptional regulatory family. (317 aa)
metE5-methyltetrahydropteroyltriglutamate- homocysteine S-methyltransferase; Catalyzes the transfer of a methyl group from 5- methyltetrahydrofolate to homocysteine resulting in methionine formation; Belongs to the vitamin-B12 independent methionine synthase family. (753 aa)
glnAGlutamine synthetase; Function experimentally demonstrated in the studied species; enzyme. (469 aa)
metJDNA-binding transcriptional repressor, S-adenosylmethionine-binding; This regulatory protein, when combined with SAM (S- adenosylmethionine) represses the expression of the methionine regulon and of enzymes involved in SAM synthesis; Belongs to the MetJ family. (105 aa)
metLFused aspartokinase II; Function experimentally demonstrated in the studied species; enzyme. (810 aa)
metF5,10-methylenetetrahydrofolate reductase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the methylenetetrahydrofolate reductase family. (296 aa)
argEAcetylornithine deacetylase; Function experimentally demonstrated in the studied species; enzyme. (383 aa)
ivbLilvB operon leader peptide; Function experimentally demonstrated in the studied genus; leader peptide. (32 aa)
leuLLeu operon leader peptide; Function experimentally demonstrated in the studied genus; leader peptide. (28 aa)
serB3-phosphoserine phosphatase; Function experimentally demonstrated in the studied species; enzyme. (322 aa)
yjgMPutative acetyltransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (167 aa)
argIFragment of conserved hypothetical protein (part 3); Gene remnant. (334 aa)
yjgFKetoacid-binding protein; Function experimentally demonstrated in the studied species; putative enzyme. (128 aa)
alrAlanine racemase 1, PLP-binding, biosynthetic; Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids; Belongs to the alanine racemase family. (359 aa)
lysCAspartokinase III; Function experimentally demonstrated in the studied species; enzyme; Belongs to the aspartokinase family. (449 aa)
metHhomocysteine-N5-methyltetrahydrofolate transmethylase, B12-dependent; Function experimentally demonstrated in the studied species; enzyme. (1227 aa)
metAHomoserine transsuccinylase; Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine. (309 aa)
argHArgininosuccinate lyase; Function experimentally demonstrated in the studied species; enzyme. (457 aa)
argBAcetylglutamate kinase; Function experimentally demonstrated in the studied species; enzyme. (257 aa)
argCN-acetyl-gamma-glutamylphosphate reductase, NAD(P)-binding; Catalyzes the NADPH-dependent reduction of N-acetyl-5- glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde. Belongs to the NAGSA dehydrogenase family. Type 1 subfamily. (334 aa)
thrAFused aspartokinase I; Function experimentally demonstrated in the studied species; enzyme; Belongs to the aspartokinase family. (820 aa)
thrBHomoserine kinase; Function experimentally demonstrated in the studied species; enzyme. (310 aa)
thrCThreonine synthase; Function experimentally demonstrated in the studied species; enzyme. (428 aa)
dapBDihydrodipicolinate reductase; Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate; Belongs to the DapB family. (273 aa)
carACarbamoyl phosphate synthetase small subunit, glutamine amidotransferase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the CarA family. (382 aa)
carBCarbamoyl-phosphate synthase large subunit; Function experimentally demonstrated in the studied species; enzyme; Belongs to the CarB family. (1073 aa)
folADihydrofolate reductase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the dihydrofolate reductase family. (159 aa)
leuD3-isopropylmalate isomerase subunit; Function experimentally demonstrated in the studied species; enzyme. (201 aa)
leuC3-isopropylmalate isomerase subunit, dehydratase component; Function experimentally demonstrated in the studied species; enzyme. (466 aa)
leuB3-isopropylmalate dehydrogenase; Function experimentally demonstrated in the studied species; enzyme. (363 aa)
leuA2-isopropylmalate synthase; Function experimentally demonstrated in the studied species; enzyme. (523 aa)
ilvIAcetolactate synthase III, large subunit; Function experimentally demonstrated in the studied species; enzyme. (574 aa)
ilvHAcetolactate synthase III, thiamin-dependent, small subunit; Function experimentally demonstrated in the studied species; enzyme. (163 aa)
panDAspartate 1-decarboxylase; Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine; Belongs to the PanD family. (126 aa)
pfs5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'- methylthioribose and S-ribosylhomocysteine, respectively. Also cleaves 5'-deoxyadenosine, a toxic by-product of radical S-adenosylmethionine (SAM) enzymes, into 5-deoxyribose and adenine. Thus, is required for in vivo function of the radical SAM enzymes biotin synthase and lipoic acid synthase, that are inhibited by 5'-deoxyadenosine accumulatio [...] (232 aa)
dapD2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the transferase hexapeptide repeat family. (274 aa)
proBGamma-glutamate kinase; Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate. (367 aa)
proAGamma-glutamylphosphate reductase; Function experimentally demonstrated in the studied species; enzyme. (417 aa)
proCPyrroline-5-carboxylate reductase, NAD(P)-binding; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline. (269 aa)
aroLShikimate kinase II; Function experimentally demonstrated in the studied species; enzyme. (174 aa)
aroMConserved hypothetical protein; Homologs of previously reported genes of unknown function; 3001025. (225 aa)
folD5,10-methylene-tetrahydrofolate dehydrogenase; Function experimentally demonstrated in the studied species; enzyme. (288 aa)
asnBAsparagine synthetase B; Function experimentally demonstrated in the studied species; enzyme. (554 aa)
aroG3-deoxy-D-arabino-heptulosonate-7-phosphate synthase, phenylalanine repressible; Function experimentally demonstrated in the studied species; enzyme. (350 aa)
ybiBPutative transferase/phosphorylase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (320 aa)
serSseryl-tRNA synthetase, also charges selenocysteinyl-tRNA with serine; Function experimentally demonstrated in the studied species; enzyme. (430 aa)
serC3-phosphoserine/phosphohydroxythreonine aminotransferase; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily. (362 aa)
aroA5-enolpyruvylshikimate-3-phosphate synthetase; Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. (427 aa)
putAFused DNA-binding transcriptional regulator; Function experimentally demonstrated in the studied species; enzyme. (1320 aa)
trpATryptophan synthase, alpha subunit; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. (268 aa)
trpBTryptophan synthase, beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. (397 aa)
trpCFused indole-3-glycerolphosphate synthetase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the TrpF family. (452 aa)
trpDFused glutamine amidotransferase (component II) of anthranilate synthase; Function experimentally demonstrated in the studied species; enzyme. (531 aa)
trpEComponent I of anthranilate synthase; Function experimentally demonstrated in the studied species; enzyme. (520 aa)
cysBDNA-binding transcriptional dual regulator, O-acetyl-L-serine-binding; Function experimentally demonstrated in the studied species; regulator. (324 aa)
puuAgamma-Glu-putrescine synthase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the glutamine synthetase family. (472 aa)
ydiBQuinate/shikimate 5-dehydrogenase, NAD(P)-binding; The actual biological function of YdiB remains unclear, nor is it known whether 3-dehydroshikimate or quinate represents the natural substrate. Catalyzes the reversible NAD-dependent reduction of both 3-dehydroshikimate (DHSA) and 3-dehydroquinate to yield shikimate (SA) and quinate, respectively. It can use both NAD or NADP for catalysis, however it has higher catalytic efficiency with NAD. (288 aa)
aroD3-dehydroquinate dehydratase; Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis- dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. Belongs to the type-I 3-dehydroquinase family. (252 aa)
aroH3-deoxy-D-arabino-heptulosonate-7-phosphate synthase, tryptophan repressible; Function experimentally demonstrated in the studied species; enzyme. (348 aa)
astCSuccinylornithine transaminase, PLP-dependent; Function experimentally demonstrated in the studied species; enzyme. (406 aa)
selDSelenophosphate synthase; Function experimentally demonstrated in the studied species; enzyme. (347 aa)
hisGATP phosphoribosyltransferase; Catalyzes the condensation of ATP and 5-phosphoribose 1- diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity. (299 aa)
hisDBifunctional histidinal dehydrogenase and histidinol dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine. (434 aa)
hisBFused histidinol-phosphatase; Function experimentally demonstrated in the studied species; enzyme. (355 aa)
Your Current Organism:
Escherichia coli IAI1
NCBI taxonomy Id: 585034
Other names: E. coli IAI1, Escherichia coli str. IAI1, Escherichia coli strain IAI1
Server load: low (12%) [HD]