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trpD protein (Pedobacter sp. BAL39) - STRING interaction network
"trpD" - Anthranilate phosphoribosyltransferase in Pedobacter sp. BAL39
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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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) (329 aa)    
Predicted Functional Partners:
PBAL39_12332
Anthranilate synthase component II (190 aa)
  0.998
PBAL39_12327
Anthranilate synthase component I (468 aa)
 
  0.996
PBAL39_06041
P-aminobenzoate synthetase, component I (444 aa)
 
  0.996
trpF
N-(5’-phosphoribosyl)anthranilate isomerase (224 aa)
 
 
  0.994
trpB
Tryptophan synthase beta chain ; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine (393 aa)
 
  0.983
trpA
Tryptophan synthase alpha chain ; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3- phosphate (255 aa)
 
  0.981
PBAL39_12342
Indole-3-glycerol phosphate synthase (132 aa)
 
  0.972
PBAL39_25035
Inosine-5’-monophosphate dehydrogenase (489 aa)
   
 
  0.857
aroC
5-enolpyruvylshikimate-3-phosphate phospholyase ; 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 (363 aa)
   
 
  0.795
PBAL39_14514
Prephenate dehydratase (278 aa)
 
 
  0.772
Your Current Organism:
Pedobacter sp. BAL39
NCBI taxonomy Id: 391596
Other names: P. sp. BAL39, Pedobacter BAL39, Pedobacter sp. BAL39
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