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trpA protein (Gallibacterium anatis) - STRING interaction network
"trpA" - Tryptophan synthase subunit alpha in Gallibacterium anatis
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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trpATryptophan synthase subunit alpha; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3- phosphate (270 aa)    
Predicted Functional Partners:
trpB
Tryptophan synthase subunit beta; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine (398 aa)
  0.999
UMN179_00018
Phosphoribosylanthranilate isomerase (474 aa)
 
  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) (333 aa)
 
  0.997
UMN179_00021
Anthranilate synthase, aminase component (512 aa)
 
 
  0.993
UMN179_00020
Anthranilate synthase, amidotransferase component (193 aa)
 
 
  0.992
UMN179_00554
Putative anthranilate synthase component II (190 aa)
 
 
  0.979
UMN179_00555
Para-aminobenzoate synthase component I (331 aa)
 
 
  0.936
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 (420 aa)
     
 
  0.886
hisI
Pyrophosphatase protein (205 aa)
   
   
  0.886
ilvA
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 (516 aa)
   
 
  0.814
Your Current Organism:
Gallibacterium anatis
NCBI taxonomy Id: 1005058
Other names: G. anatis, G. anatis UMN179, Gallibacterium, Gallibacterium Christensen et al. 2003 emend. Bisgaard et al. 2009, Gallibacterium anatis, Gallibacterium anatis UMN179, Gallibacterium anatis str. UMN179, Gallibacterium anatis strain UMN179, Pasteurella anatis, Salpingitia sp. 10672/6, Salpingitia sp. 10672/9, Salpingitia sp. 12158, Salpingitia sp. 20558, Salpingitia sp. 36961/sv7, Salpingitia sp. BJ3453, Salpingitia sp. BK3387.2, Salpingitia sp. CCM 5995, Salpingitia sp. Gerl.220, Salpingitia sp. Gerl.3348/80, Salpingitia sp. Gerl.4224, Salpingitia sp. IPDH 697/78, avian Pasteurella haemolytica complex
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