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AIL79179.1 protein (Acinetobacter baumannii) - STRING interaction network
"AIL79179.1" - Tryptophan synthase in Acinetobacter baumannii
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second shell of interactors
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some 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
Others
textmining
co-expression
protein homology
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[Homology]
Score
AIL79179.1Tryptophan synthase; Derived by automated computational analysis using gene prediction method- Protein Homology (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 (267 aa)
  0.999
AIL79180.1
N-(5’-phosphoribosyl)anthranilate isomerase; Derived by automated computational analysis using gene prediction method- Protein Homology (219 aa)
   
  0.998
AIL78672.1
Indole-3-glycerol phosphate synthase; Derived by automated computational analysis using gene prediction method- Protein Homology (268 aa)
 
  0.998
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) (351 aa)
   
  0.947
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 (417 aa)
     
 
  0.913
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 (513 aa)
     
  0.913
ilvA2
L-threonine dehydratase catabolic TdcB; Derived by automated computational analysis using gene prediction method- Protein Homology (411 aa)
     
  0.913
AIL77784.1
L-serine ammonia-lyase; Derived by automated computational analysis using gene prediction method- Protein Homology (459 aa)
     
 
  0.907
serB
Phosphoserine phosphatase SerB; Derived by automated computational analysis using gene prediction method- Protein Homology (407 aa)
   
 
    0.902
thrH
Phosphoserine phosphatase/homoserine phosphotransferase bifunctional protein; Derived by automated computational analysis using gene prediction method- Protein Homology (205 aa)
   
 
    0.901
Your Current Organism:
Acinetobacter baumannii
NCBI taxonomy Id: 470
Other names: A. baumannii, ATCC 19606, Acinetobacter baumannii, Acinetobacter genomosp. 2, Acinetobacter genomospecies 2, Bacterium anitratum, CCUG 19096, CIP 70.34, DSM 30007, JCM 6841, NCCB 85021, NCTC 12156
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