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glyA glyA ilvA ilvA trpB trpB trpF trpF trpA trpA trpC trpC trpE trpE trpG trpG trpE2 trpE2 sll1634 sll1634 trpD trpD
"trpA" - Tryptophan synthase subunit alpha in Synechocystis sp. PCC6803
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experimentally determined
Predicted Interactions
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gene fusions
gene co-occurrence
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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 (264 aa)    
Predicted Functional Partners:
trpB
Tryptophan synthase beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine (412 aa)
  0.999
trpC
Indole-3-glycerol phosphate synthase (295 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) (348 aa)
 
  0.996
trpF
5’-phosphoribosyl anthranilate isomerase (218 aa)
 
 
  0.992
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 concentr [...] (508 aa)
 
 
  0.989
trpE2
Anthranilate synthase component I (485 aa)
 
 
  0.986
trpG
Anthranilate synthase component II (196 aa)
 
 
  0.974
sll1634
Hypothetical protein (349 aa)
 
 
  0.965
ilvA
L-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 (508 aa)
   
 
  0.934
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 (427 aa)
     
 
  0.928
Your Current Organism:
Synechocystis sp. PCC6803
NCBI taxonomy Id: 1148
Other names: Aphanocapsa sp. (strain N-1), Aphanocapsa sp. N-1, S. sp. PCC 6803, Synechocystis, Synechocystis PCC6803, Synechocystis sp. (ATCC 27184), Synechocystis sp. (PCC 6803), Synechocystis sp. (strain PCC 6803), Synechocystis sp. ATCC 27184, Synechocystis sp. PCC 6803, Synechocystis sp. PCC 6803 A, Synechocystis sp. PCC 6803 B, Synechocystis sp. PCC6803
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