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trpA protein (Pseudomonas oleovorans) - STRING interaction network
"trpA" - Tryptophan synthase alpha chain in Pseudomonas oleovorans
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second shell of interactors
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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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trpATryptophan 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 (269 aa)    
Predicted Functional Partners:
trpB
Tryptophan synthase beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine (403 aa)
  0.999
trpC
annotation not available (279 aa)
 
  0.999
JNHE01000022_gene2644
annotation not available (216 aa)
 
  0.997
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) (348 aa)
 
  0.994
JNHE01000002_gene2174
annotation not available (402 aa)
 
 
  0.990
trpE
Anthranilate synthase component 1; 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 concentr [...] (500 aa)
 
 
  0.987
JNHE01000026_gene3072
annotation not available (195 aa)
 
 
  0.975
JNHE01000004_gene1660
annotation not available (469 aa)
   
 
  0.917
JNHE01000042_gene3216
annotation not available (331 aa)
   
 
  0.871
ilvA
L-threonine dehydratase; 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 (504 aa)
     
 
  0.870
Your Current Organism:
Pseudomonas oleovorans
NCBI taxonomy Id: 301
Other names: ATCC 8062, CCUG 2087, CFBP 5589, CIP 59.11, IFO 13583, JCM 11598, LMG 2229, NBRC 13583, NCIMB 6576, NCTC 10692, NRRL B-778, P. oleovorans, Pseudomonas oleovorans, Pseudomonas sp. MGY01
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