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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
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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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EIC29575.1Cytochrome 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. (540 aa)    
Predicted Functional Partners:
EIC29574.1
Cytochrome c oxidase, subunit II; 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).
 0.999
EIC29577.1
Heme/copper-type cytochrome/quinol oxidase, subunit 3; PFAM: Cytochrome c oxidase subunit III.
 0.999
EIC28246.1
Heme/copper-type cytochrome/quinol oxidase, subunit 2; PFAM: Cytochrome C oxidase subunit II, periplasmic domain; Cytochrome c.
 
 0.998
EIC28368.1
PFAM: Cytochrome C oxidase subunit II, periplasmic domain; Cytochrome c; TIGRFAM: cytochrome c oxidase, subunit II.
 
 0.998
EIC28244.1
Heme/copper-type cytochrome/quinol oxidase, subunit 3; PFAM: Cytochrome c oxidase subunit III.
 0.997
cyoE
Protoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
 0.993
EIC28164.1
Cytochrome b subunit of the bc complex; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.
 
 0.988
nuoC
NADH/F420H2 dehydrogenase, 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 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; In the C-terminal section; belongs to the complex I 49 kDa subunit family.
   
 
 0.977
EIC29880.1
Heme/copper-type cytochrome/quinol oxidase, subunit 2; PFAM: Cytochrome C oxidase subunit II, periplasmic domain.
 
 0.973
nuoH
NADH:ubiquinone oxidoreductase subunit 1 (chain H); 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.
  
 
 0.935
Your Current Organism:
Methylomicrobium album
NCBI taxonomy Id: 686340
Other names: M. album BG8, Methylomicrobium album BG8, Methylomicrobium album str. BG8, Methylomicrobium album strain BG8
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