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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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[Homology]
Score
cyaA-2Cytochrome d ubiquinol oxidase, subunit I. (466 aa)    
Predicted Functional Partners:
cydB
Cytochrome d ubiquinol oxidase, subunit II.
 0.999
cydB-2
Cytochrome d ubiquinol oxidase, subunit II.
 0.999
ybgT
Cyd operon protein YbgT.
  
 0.964
cyaA
Cytochrome d ubiquinol oxidase, subunit I.
  
  
 
0.949
cyoD
Cytochrome o ubiquinol oxidase subunit IV.
     
 0.598
GLE_4935
Hypothetical protein.
       0.571
putA
Proline dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family.
     
 0.564
nuoA
NADH-quinone oxidoreductase A subunit; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. 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 subunit 3 family.
     
 0.564
nuoH
NADH dehydrogenase, H subunit; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. 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. This subunit may bind ubiquinone.
     
 0.564
nuoJ
NADH dehydrogenase, J subunit; 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.
     
 0.564
Your Current Organism:
Lysobacter enzymogenes
NCBI taxonomy Id: 69
Other names: ATCC 29487, DSM 2043, L. enzymogenes, LMG 8762, LMG:8762, Lysobacter enzymogenes subsp. enzymogenes, UASM 495
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