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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
glcFGlycolate oxidase iron-sulfur subunit; Component of a complex that catalyzes the oxidation of glycolate to glyoxylate. Is also able to oxidize D-lactate ((R)- lactate). Does not link directly to O(2), and 2,6-dichloroindophenol (DCIP) and phenazine methosulfate (PMS) can act as artificial electron acceptors in vitro, but the physiological molecule that functions as primary electron acceptor during glycolate oxidation is unknown. (444 aa)    
Predicted Functional Partners:
glcD
Glycolate oxidase subunit; Component of a complex that catalyzes the oxidation of glycolate to glyoxylate. Is also able to oxidize D-lactate ((R)- lactate). Does not link directly to O(2), and 2,6-dichloroindophenol (DCIP) and phenazine methosulfate (PMS) can act as artificial electron acceptors in vitro, but the physiological molecule that functions as primary electron acceptor during glycolate oxidation is unknown. Belongs to the FAD-binding oxidoreductase/transferase type 4 family.
 
 0.999
yobM
Putative phage protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type h: extrachromosomal origin.
   
  
 0.921
yjnA
Putative integral inner membrane protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pm: putative membrane component.
      
 0.919
lutB
Component of an iron-sulfur oxidase; Is essential for L-lactate degradation and allows cells to grow with lactate as the sole carbon source. Has probably a role as an electron transporter during oxidation of L-lactate. May also allow cells to utilize an alternative carbon source during biofilm formation, since it contributes to the formation of architecturally complex communities when lactate is present.
 
 
 0.919
yvcT
Putative 2-hydroxyacid dehydrogenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.
    
 0.911
kdgA
2-keto-3-deoxygluconate-6-phosphate aldolase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme.
   
 
 0.904
katA
Vegetative catalase 1; Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide.
     
  0.900
katX
Major catalase in spores; Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide; Belongs to the catalase family.
     
  0.900
katE
Catalase 2; Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide. Involved in sporulation.
    
  0.900
lutC
Component of an iron-sulfur oxidase; Is essential for L-lactate degradation and allows cells to grow with lactate as the sole carbon source. May also allow cells to utilize an alternative carbon source during biofilm formation, since it contributes to the formation of architecturally complex communities when lactate is present.
 
 
 0.864
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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