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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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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[Homology]
Score
ydfNPutative oxidoreductase; Putative nitroreductase that may contribute to the degradation of aromatic compounds. (206 aa)    
Predicted Functional Partners:
ydfO
Putative dioxygenase; Putative ring-cleavage dioxygenase that may contribute to the degradation of aromatic compounds.
  
  
 0.991
yodE
Putative lyase/dioxygenase; Putative ring-cleavage dioxygenase that may contribute to the degradation of aromatic compounds.
  
  
 0.914
yvaB
NADH:dichloroindophenol oxidoreductase; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity. Confers resistance to catechol, 2- methylhydroquinone (2-MHQ), and diamide. Probably could also reduce benzoquinones produce by the auto-oxidation of catechol and 2- methylhydroquinone.
   
  
 0.914
mhqA
Putative hydroquinone-specific extradiol dioxygenase; Putative ring-cleavage dioxygenase that may contribute to the degradation of aromatic compounds.
  
  
 0.885
mhqR
Transcriptional regulator (MarR family); Negatively regulates mhqA, mhqED, mhqNOP, and azoR2 which may contribute to the degradation of aromatic compounds.
     
 0.790
rtbJ
Antitoxin of ribonuclease RttI; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity. Confers resistance to catechol, 2- methylhydroquinone (2-MHQ), and diamide. Probably could also reduce benzoquinones produce by the auto-oxidation of catechol and 2- methylhydroquinone.
      
 0.763
catE
Catechol-2,3-dioxygenase subunit; Involved in the meta cleavage of catechol to 2-hydroxymuconic semialdehyde. Essential for growth and viability in the presence of catechol and probably involved in the detoxification of catechol.
     
 0.721
ydzF
Putative transcriptional regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator.
     
 0.716
ydeP
Putative transcriptional regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator.
     
 0.713
ytcD
Putative transcriptional regulator (MarD family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator.
     
 0.695
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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