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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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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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Swol_0359KEGG: sde:Sde_0754 indole-3-glycerol-phosphate synthase. (260 aa)    
Predicted Functional Partners:
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).
  
 0.999
trpF
KEGG: gme:Gmet_2492 N-(5'phosphoribosyl)anthranilate isomerase (PRAI); Belongs to the TrpF family.
 
 0.999
trpB
Tryptophan synthase, beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine.
 
 0.999
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
Swol_0364
Anthranilate synthase, component I / anthranilate synthase, component II; KEGG: ana:all0414 anthranilate synthase.
 
 0.999
trpB-2
Tryptophan synthase, beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine.
  
 
 0.928
aroE
Shikimate dehydrogenase; Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
 
 
 0.774
hisI
KEGG: chy:CHY_1091 bifunctional phosphoribosyl-AMP cyclohydrolase/phosphoribosyl-ATP pyrophosphatase protein; In the N-terminal section; belongs to the PRA-CH family.
  
  
 0.631
pheA
Prephenate dehydratase; KEGG: aae:aq_951 chorismate mutase/prephenate dehydratase.
 
  
 0.596
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.
 
  
 0.591
Your Current Organism:
Syntrophomonas wolfei Goettingen
NCBI taxonomy Id: 335541
Other names: S. wolfei subsp. wolfei str. Goettingen G311, Syntrophomonas wolfei str. Goettingen, Syntrophomonas wolfei subsp. wolfei Goettingen, Syntrophomonas wolfei subsp. wolfei str. Goettingen, Syntrophomonas wolfei subsp. wolfei str. Goettingen G311, Syntrophomonas wolfei subsp. wolfei str. Gottingen, Syntrophomonas wolfei subsp. wolfei strain Goettingen
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