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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
yodEPutative lyase/dioxygenase; Putative ring-cleavage dioxygenase that may contribute to the degradation of aromatic compounds. (303 aa)    
Predicted Functional Partners:
yodD
Putative hydrolase; Putative hydrolase that may contribute to the degradation of aromatic compounds.
  
 0.999
ydfN
Putative oxidoreductase; Putative nitroreductase that may contribute to the degradation of aromatic compounds.
  
  
 0.936
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.
   
  
 0.853
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.
 
  
 0.830
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.
   
  
 0.752
arxR
Transcriptional repressor; Negatively regulates yodC and azoR1 which may contribute to the degradation of aromatic compounds. Probably positively regulates the catechol-specific transcription of mhqNOP, mhqED, and mhqA.
   
  
 0.682
yodC
Putative oxidoreductase; Putative nitroreductase that may contribute to the degradation of aromatic compounds.
  
  
 0.532
yoyD
Putative exported protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pf: putative factor.
       0.505
yodF
Putative Na+/metabolite permease; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter; Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family.
  
    0.505
catD
Catechol-2,3-dioxygenase membrane subunit; Essential for growth and viability in the presence of catechol and probably involved in the detoxification of catechol.
     
 0.457
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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