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trpB trpB trpA trpA trpC trpC trpD trpD trpG trpG trpE trpE glyA glyA ilvA ilvA ETA_16240 ETA_16240 pabB pabB serB serB
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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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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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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Score
trpBTryptophan synthase beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. (396 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
Anthranilate isomerase; silverDB:etchr01591; Belongs to the TrpC family.
 
 0.999
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).
 
  
 0.998
trpG
Putative Anthranilate synthase component II; silverDB:etchr01593.
 
  
 0.996
trpE
Anthranilate synthase component I; silverDB:etchr01594.
 
  
 0.996
glyA
Serine 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.
     
 0.930
ilvA
Threonine deaminase; 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.
  
 0.926
ETA_16240
L-serine dehydratase; silverDB:etchr01614.
  
 0.926
pabB
Para-aminobenzoate synthase component I; silverDB:etchr01517.
 
  
 0.924
serB
Phosphoserine phosphatase; silverDB:etchr00664.
   
 
 0.914
Your Current Organism:
Erwinia tasmaniensis
NCBI taxonomy Id: 465817
Other names: E. tasmaniensis Et1/99, Erwinia tasmaniensis Et1/99, Erwinia tasmaniensis str. Et1/99, Erwinia tasmaniensis strain Et1/99
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