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trpB trpB trpA trpA trpC trpC trpC-2 trpC-2 trpF trpF Psyr_4581 Psyr_4581 trpE trpE trpD trpD Psyr_2080 Psyr_2080 ilvA ilvA ilvA-2 ilvA-2
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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trpBTryptophan synthase, beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. (409 aa)    
Predicted Functional Partners:
trpA
Tryptophan synthase, alpha chain; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family.
 0.999
trpC
Indole-3-glycerol phosphate synthase; Belongs to the TrpC family.
 
 0.999
trpC-2
Indole-3-glycerol phosphate synthase; Belongs to the TrpC family.
 
 0.999
trpF
Phosphoribosylanthranilate isomerase; Belongs to the TrpF family.
  
 0.996
Psyr_4581
Anthranilate synthase, component II.
 
  
 0.979
trpE
Anthranilate synthase, component I; Part of a heterotetrameric complex that catalyzes the two- step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concent [...]
 
  
 0.979
trpD
Anthranilate phosphoribosyltransferase; Catalyzes the transfer of the phosphoribosyl group of 5- phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'- phosphoribosyl)-anthranilate (PRA).
 
  
 0.972
Psyr_2080
Aminodeoxychorismate synthase, subunit I.
 
  
 0.938
ilvA
L-threonine ammonia-lyase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.
  
 0.931
ilvA-2
L-threonine ammonia-lyase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.
  
 0.931
Your Current Organism:
Pseudomonas syringae B728a
NCBI taxonomy Id: 205918
Other names: P. syringae pv. syringae B728a, Pseudomonas syringae pv. syringae B728a, Pseudomonas syringae pv. syringae str. B728a, Pseudomonas syringae pv. syringae strain B728a
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