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aroL aroL aroG aroG hisC hisC aroH aroH aroD aroD ydiB ydiB trpA trpA trpB trpB trpC trpC trpD trpD trpE trpE aspC aspC aroA aroA aroC aroC pheA pheA tyrA tyrA aroF aroF aroE aroE aroB aroB aroK aroK CAR20517.1 CAR20517.1 tyrB tyrB
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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
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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:
aroLShikimate kinase II; Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate. (174 aa)
aroG3-deoxy-D-arabino-heptulosonate-7-phosphate synthase, phenylalanine repressible; Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino- heptulosonate-7-phosphate (DAHP). (350 aa)
hisCHistidinol-phosphate aminotransferase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily. (356 aa)
aroH3-deoxy-D-arabino-heptulosonate-7-phosphate synthase, tryptophan repressible; Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino- heptulosonate-7-phosphate (DAHP). (348 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)
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)
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 TrpC family. (452 aa)
trpDFused glutamine amidotransferase (component II) of anthranilate synthase; Catalyzes the transfer of the phosphoribosyl group of 5- phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'- phosphoribosyl)-anthranilate (PRA). (531 aa)
trpEComponent I of anthranilate synthase; Function experimentally demonstrated in the studied species; enzyme. (520 aa)
aspCAspartate aminotransferase, PLP-dependent; Function experimentally demonstrated in the studied species; enzyme. (396 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)
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)
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; Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino- heptulosonate-7-phosphate (DAHP). (356 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)
aroB3-dehydroquinate synthase; Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ); Belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family. (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)
CAR20517.1Putative Shikimate dehydrogenase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (270 aa)
tyrBTyrosine aminotransferase, tyrosine-repressible, PLP-dependent; Function experimentally demonstrated in the studied species; enzyme. (397 aa)
Your Current Organism:
Escherichia coli IAI39
NCBI taxonomy Id: 585057
Other names: E. coli IAI39
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