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ACO45980.1Putative FAD dependent oxidoreductase. (489 aa)    
Predicted Functional Partners:
ACO46820.1
Putative Cytochrome-c oxidase (Cytochrome-c oxidase polypeptide I+III, Complex IV); putative membrane protein; Belongs to the heme-copper respiratory oxidase family.
  
 
 0.996
ctaC
Putative cytochrome-c oxidase, subunit 2; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
  
 
 0.990
ACO47087.1
Putative cytochrome b/b6; putative membrane protein.
  
 0.912
ACO46164.1
Putative Succinate dehydrogenase, flavoprotein subunit.
  
 
 0.841
ACO46165.1
Putative Succinate dehydrogenase, iron-sulfur protein.
  
 
 0.825
nuoI
Putative NADH dehydrogenase (quinone), subunit I (NADH-quinone oxidoreductase, subunit I); 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.
  
 
 0.815
nuoD
Putative NADH dehydrogenase (quinone), subunit D (NADH-quinone oxidoreductase, subunit D); 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 a menaquinone. 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 49 kDa subunit family.
   
 
 0.803
ACO45351.1
Putative NADH dehydrogenase (quinone), subunit G (NADH-quinone oxidoreductase, subunit 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.
  
 
 0.774
nuoC
Putative NADH dehydrogenase (quinone), subunit C (NADH-quinone oxidoreductase, subunit C); 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 a menaquinone. 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 30 kDa subunit family.
   
 
 0.772
ACO45349.1
Putative NADH dehydrogenase (quinone), subunit E (NADH-quinone oxidoreductase, subunit E).
   
 
 0.772
Your Current Organism:
Deinococcus deserti
NCBI taxonomy Id: 546414
Other names: D. deserti VCD115, Deinococcus deserti VCD115, Deinococcus deserti str. VCD115, Deinococcus deserti strain VCD115
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