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AEF23597.1 AEF23597.1 AEF22280.1 AEF22280.1 AEF22599.1 AEF22599.1 AEF22277.1 AEF22277.1 nuoB nuoB AEF20155.1 AEF20155.1 nuoI nuoI AEF22278.1 AEF22278.1 AEF22279.1 AEF22279.1 AEF20759.1 AEF20759.1 nuoH nuoH
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query proteins and first shell of interactors
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second shell of interactors
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Known Interactions
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experimentally determined
Predicted Interactions
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textmining
co-expression
protein homology
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Score
AEF23597.1PFAM: Semialdehyde dehydrogenase, NAD-binding; KEGG: pmy:Pmen_3812 NAD-dependent epimerase/dehydratase. (213 aa)    
Predicted Functional Partners:
AEF22280.1
NAD(P)H-quinone oxidoreductase subunit J; 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.
  
 0.999
AEF22599.1
Manually curated; TIGRFAM: Cytochrome c oxidase, subunit II; KEGG: pmy:Pmen_2266 cytochrome c, monohaem; PFAM: Cytochrome c oxidase subunit II C-terminal.
   
 
 0.986
AEF22277.1
NADH-quinone oxidoreductase, chain 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.
   
 0.979
nuoB
NAD(P)H-quinone oxidoreductase subunit K; 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.
   
 0.976
AEF20155.1
PFAM: 4Fe-4S binding domain; KEGG: pmy:Pmen_4192 4Fe-4S ferredoxin iron-sulfur binding domain-containing protein.
   
 0.973
nuoI
NAD(P)H-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.
   
 0.973
AEF22278.1
NADH-quinone oxidoreductase, F subunit; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family.
   
 0.964
AEF22279.1
TIGRFAM: NADH:ubiquinone oxidoreductase, 24kDa subunit; KEGG: pfl:PFL_3900 NADH dehydrogenase subunit E; PFAM: NADH:ubiquinone oxidoreductase, 24kDa subunit.
   
 0.964
AEF20759.1
Ubiquinol-cytochrome c reductase, iron-sulfur subunit; 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.
  
 
 0.957
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.
   
 0.927
Your Current Organism:
Pseudomonas fulva
NCBI taxonomy Id: 743720
Other names: P. fulva 12-X, Pseudomonas fulva 12-X, Pseudomonas fulva str. 12-X, Pseudomonas fulva strain 12-X
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