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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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Swit_3875Cytochrome 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). (338 aa)    
Predicted Functional Partners:
Swit_3876
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.
 0.999
ctaB
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.
 
 
 0.999
Swit_3880
PFAM: cytochrome c oxidase, subunit III.
 
 0.999
Swit_1395
Cytochrome b/b6, N-terminal domain; 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.
 
 
 0.997
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.
 
 0.994
nuoA
NADH-ubiquinone/plastoquinone oxidoreductase, chain 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.
  
 0.988
Swit_2997
TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I).
 
 0.988
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.
 
 0.987
ctaG
Cytochrome c oxidase assembly protein CtaG/Cox11; Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I; Belongs to the COX11/CtaG family.
 
 
 0.981
Swit_1798
Cytochrome c oxidase, cbb3-type, subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex.
  
 0.980
Your Current Organism:
Sphingomonas wittichii
NCBI taxonomy Id: 392499
Other names: S. wittichii RW1, Sphingomonas sp. RW1, Sphingomonas wittichii DSM 6014, Sphingomonas wittichii RW1, Sphingomonas wittichii str. RW1, Sphingomonas wittichii strain RW1
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