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cyoA cyoA cyoB cyoB cyoC cyoC cyoD cyoD cyoE2 cyoE2 nuoCD nuoCD ctaD1 ctaD1 ctaD2 ctaD2 ctaE2 ctaE2 ctaE1 ctaE1 nuoH nuoH
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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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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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[Homology]
Score
cyoA[C] COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. (314 aa)    
Predicted Functional Partners:
cyoB
[C] COG0843 Heme/copper-type cytochrome/quinol oxidases, subunit 1; Belongs to the heme-copper respiratory oxidase family.
 
 0.999
cyoC
[C] COG1845 Heme/copper-type cytochrome/quinol oxidase, subunit 3.
 
 0.999
cyoD
[C] COG3125 Heme/copper-type cytochrome/quinol oxidase, subunit 4.
 
 0.999
cyoE2
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.
 
  
 0.981
nuoCD
NADH-quinone oxidoreductase subunit C/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 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.
   
 
 0.970
ctaD1
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.
 
 0.953
ctaD2
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.
 
 0.952
ctaE2
[C] COG1845 Heme/copper-type cytochrome/quinol oxidase, subunit 3.
 
 0.942
ctaE1
[C] COG1845 Heme/copper-type cytochrome/quinol oxidase, subunit 3.
  
 0.929
nuoH
NADH-quinone oxidoreductase subunit 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.
   
 0.927
Your Current Organism:
Pseudomonas sp. UW4
NCBI taxonomy Id: 1207075
Other names: P. sp. UW4
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