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trpD protein (Synechocystis sp. PCC6803) - STRING interaction network
"trpD" - Anthranilate phosphoribosyltransferase in Synechocystis sp. PCC6803
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second shell of interactors
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filled nodes:
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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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trpDAnthranilate 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)    
Predicted Functional Partners:
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)
 
  0.999
trpG
Anthranilate synthase component II (196 aa)
  0.999
trpE2
Anthranilate synthase component I (485 aa)
 
  0.999
trpF
5’-phosphoribosyl anthranilate isomerase (218 aa)
 
 
  0.999
trpA
Tryptophan synthase subunit alpha; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3- phosphate (264 aa)
 
  0.996
trpC
Indole-3-glycerol phosphate synthase (295 aa)
 
 
  0.996
trpB
Tryptophan synthase beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine (412 aa)
 
  0.992
aroC
Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system (362 aa)
   
 
  0.928
sll1634
Hypothetical protein (349 aa)
   
     
  0.909
tyrA
Prephenate dehydrogenase (279 aa)
   
   
  0.866
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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