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query proteins and first shell of interactors
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second shell of interactors
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a 3D structure is known or predicted
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[Homology]
Score
AEB84617.1KEGG: ajs:Ajs_2775 ubiquinol oxidase, subunit II; TIGRFAM: Cytochrome o ubiquinol oxidase subunit II; PFAM: COX aromatic rich; Cytochrome c oxidase subunit II C-terminal. (329 aa)    
Predicted Functional Partners:
AEB84614.1
KEGG: ajs:Ajs_2778 cytochrome c oxidase subunit IV; TIGRFAM: Cytochrome o ubiquinol oxidase subunit IV; PFAM: Cytochrome C oxidase subunit IV prokaryotic.
 
 0.999
AEB84615.1
KEGG: dia:Dtpsy_2267 cytochrome o ubiquinol oxidase, subunit III; TIGRFAM: Cytochrome o ubiquinol oxidase, subunit III; PFAM: Cytochrome c oxidase, subunit III.
 
 0.999
AEB84616.1
TIGRFAM: Cytochrome o ubiquinol oxidase, subunit I; KEGG: ajs:Ajs_2776 cytochrome-c oxidase; PFAM: Cytochrome c oxidase, subunit I; Belongs to the heme-copper respiratory oxidase family.
 
 0.999
AEB86278.1
PFAM: Cytochrome c oxidase, subunit III; KEGG: dia:Dtpsy_2855 cytochrome c oxidase subunit III.
 
 0.979
AEB86274.1
Cytochrome c oxidase, subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B.
 
 0.973
nuoH
NADH dehydrogenase (quinone); 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.
   
 0.973
nuoA
NAD(P)H-quinone oxidoreductase subunit 3; 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.
   
 0.970
nuoN
Proton-translocating NADH-quinone oxidoreductase, chain N; 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 2 family.
   
 0.970
AEB86341.1
TIGRFAM: NADH-quinone oxidoreductase, chain M/4; KEGG: dia:Dtpsy_0884 proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH:ubiquinone/plastoquinone oxidoreductase; NADH:ubiquinone oxidoreductase, chain 4, N-terminal.
   
 0.967
AEB86229.1
Cytochrome-c oxidase; KEGG: app:CAP2UW1_1790 cytochrome c oxidase subunit I; PFAM: Cytochrome c oxidase, subunit I.
 
 0.962
Your Current Organism:
Alicycliphilus denitrificans
NCBI taxonomy Id: 596154
Other names: A. denitrificans K601, Alicycliphilus denitrificans DSM 14773, Alicycliphilus denitrificans K601, Alicycliphilus denitrificans str. K601, Alicycliphilus denitrificans strain K601, Pseudomonas sp. K601, beta proteobacterium K601
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