STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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Neighborhood
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Co-expression
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[Homology]
Score
KEZ49715.1Dihydropteroate synthase; Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8- dihydropteroate (H2Pte), the immediate precursor of folate derivatives. (285 aa)    
Predicted Functional Partners:
KEZ49716.1
Dihydroneopterin aldolase; Catalyzes the conversion of 7,8-dihydroneopterin to 6- hydroxymethyl-7,8-dihydropterin.
 
 
 0.999
KEZ49717.1
2-amino-4-hydroxy-6- hydroxymethyldihydropteridine pyrophosphokinase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.999
folE
GTP cyclohydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.998
KEZ51874.1
Folylpolyglutamate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the folylpolyglutamate synthase family.
 
 0.998
KEZ49714.1
4-amino-4-deoxychorismate lyase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.996
trpE-2
Aminobenzoate synthetase; 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 concentrations of [...]
 
 
 0.956
KEZ49713.1
Anthranilate synthase component II; TrpG; with TrpE catalyzes the formation of anthranilate and glutamate from chorismate and glutamine; TrpG provides the glutamine amidotransferase activity; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.943
KEZ49718.1
XRE family transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
    0.889
ilvE
Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.
  
 
 0.871
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 [...]
 
 
 0.846
Your Current Organism:
Bacillus indicus
NCBI taxonomy Id: 246786
Other names: B. indicus, Bacillus cibi, Bacillus cibi Yoon et al. 2005, Bacillus indicus Suresh et al. 2004 emend. Stropko et al. 2014, Bacillus sp. KU12, Bacillus sp. KU14, DSM 15820, DSM 16189 [[Bacillus cibi]], JCM 12168, KCTC 3880 [[Bacillus cibi]], LMG 22858, LMG:22858, MTCC 4374, strain JG-30 [[Bacillus cibi]], strain Sd/3
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