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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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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
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from curated databases
textmining
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experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
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[Homology]
Score
Daci_0037PFAM: NADH:flavin oxidoreductase/NADH oxidase; KEGG: ajs:Ajs_0022 NADH:flavin oxidoreductase/NADH oxidase. (372 aa)    
Predicted Functional Partners:
Daci_3021
PFAM: NADH:flavin oxidoreductase/NADH oxidase; KEGG: cvi:CV_2245 flavoprotein NADH-dependent oxidoreductase.
  
  
 
0.907
Daci_3889
PFAM: NADH:flavin oxidoreductase/NADH oxidase; KEGG: psb:Psyr_2934 NADH:flavin oxidoreductase/NADH oxidase.
  
  
 
0.905
Daci_0038
PFAM: NADPH-dependent FMN reductase; KEGG: azo:azo2988 probable chromate reductase.
       0.565
Daci_0039
PFAM: conserved hypothetical protein; KEGG: bja:blr3080 hypothetical protein.
       0.554
Daci_0840
PFAM: pyruvate ferredoxin/flavodoxin oxidoreductase; KEGG: aav:Aave_4646 pyruvate ferredoxin/flavodoxin oxidoreductase.
     
 0.433
Daci_0040
PFAM: Glyoxalase/bleomycin resistance protein/dioxygenase; KEGG: eli:ELI_06420 glyoxalase family protein.
     
 0.430
Daci_0889
PFAM: glutathione peroxidase; KEGG: ajs:Ajs_0173 glutathione peroxidase; Belongs to the glutathione peroxidase family.
     
 0.428
Daci_2033
Oxygen-independent coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family.
      
 0.405
Daci_5174
NADH-quinone oxidoreductase, chain G; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. Belongs to the complex I 75 kDa subunit family.
      
 0.405
Your Current Organism:
Delftia acidovorans
NCBI taxonomy Id: 398578
Other names: D. acidovorans SPH-1, Delftia acidovorans SPH-1, Delftia acidovorans str. SPH-1, Delftia acidovorans strain SPH-1
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