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AEF20155.1 AEF20155.1 AEF22280.1 AEF22280.1 AEF23294.1 AEF23294.1 AEF22599.1 AEF22599.1 nuoB nuoB AEF22277.1 AEF22277.1 AEF22271.1 AEF22271.1 nuoH nuoH nuoA nuoA AEF23597.1 AEF23597.1 nuoN nuoN
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query proteins and first shell of interactors
white nodes:
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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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
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gene co-occurrence
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textmining
co-expression
protein homology
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[Homology]
Score
AEF20155.1PFAM: 4Fe-4S binding domain; KEGG: pmy:Pmen_4192 4Fe-4S ferredoxin iron-sulfur binding domain-containing protein. (83 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
AEF23294.1
NADH dehydrogenase (quinone); KEGG: pmy:Pmen_1441 putative monovalent cation/H+ antiporter subunit A; PFAM: NADH:ubiquinone/plastoquinone oxidoreductase; NADH:ubiquinone oxidoreductase, chain 5/L, N-terminal; Na+/H+ antiporter MnhB subunit-related protein.
  
 
 0.992
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.
   
 
 0.988
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.
  
 0.979
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.
  
 0.976
AEF22271.1
TIGRFAM: NADH-quinone oxidoreductase, chain M/4; KEGG: pmy:Pmen_2423 NADH dehydrogenase subunit M; PFAM: NADH:ubiquinone/plastoquinone oxidoreductase.
  
 0.974
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.
  
 0.974
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.
  
 0.974
AEF23597.1
PFAM: Semialdehyde dehydrogenase, NAD-binding; KEGG: pmy:Pmen_3812 NAD-dependent epimerase/dehydratase.
   
 0.973
nuoN
NAD(P)H-quinone oxidoreductase subunit 2; 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
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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