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AEF20989.1 AEF20989.1 AEF20990.1 AEF20990.1 AEF20991.1 AEF20991.1 AEF20992.1 AEF20992.1 cyoE cyoE AEF22280.1 AEF22280.1 AEF20532.1 AEF20532.1 AEF22600.1 AEF22600.1 AEF22271.1 AEF22271.1 nuoH nuoH AEF20760.1 AEF20760.1
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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
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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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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AEF20989.1KEGG: mfa:Mfla_1295 ubiquinol oxidase, subunit II; TIGRFAM: Cytochrome o ubiquinol oxidase subunit II; PFAM: COX aromatic rich; Cytochrome c oxidase subunit II C-terminal. (298 aa)    
Predicted Functional Partners:
AEF20990.1
KEGG: csa:Csal_0955 cytochrome-c oxidase; TIGRFAM: Cytochrome o ubiquinol oxidase, subunit I; PFAM: Cytochrome c oxidase, subunit I; Belongs to the heme-copper respiratory oxidase family.
 
 0.999
AEF20991.1
KEGG: sgl:SG0665 cytochrome o ubiquinol oxidase subunit III; TIGRFAM: Cytochrome o ubiquinol oxidase, subunit III; PFAM: Cytochrome c oxidase, subunit III.
 
 0.999
AEF20992.1
KEGG: smt:Smal_3792 cytochrome o ubiquinol oxidase subunit IV; TIGRFAM: Cytochrome o ubiquinol oxidase subunit IV; PFAM: Cytochrome C oxidase subunit IV prokaryotic.
 
 0.999
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
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.
   
 0.993
AEF20532.1
KEGG: sml:Smlt4400 putative ubiquinol oxidase polypeptide I; TIGRFAM: Cytochrome o ubiquinol oxidase, subunit I; PFAM: Cytochrome c oxidase, subunit I; Belongs to the heme-copper respiratory oxidase family.
 
 0.989
AEF22600.1
KEGG: pmy:Pmen_2267 cytochrome-c oxidase; TIGRFAM: Cytochrome c oxidase, subunit I bacterial type; PFAM: Cytochrome c oxidase, subunit I; Belongs to the heme-copper respiratory oxidase family.
 
 0.981
AEF22271.1
TIGRFAM: NADH-quinone oxidoreductase, chain M/4; KEGG: pmy:Pmen_2423 NADH dehydrogenase subunit M; PFAM: NADH:ubiquinone/plastoquinone oxidoreductase.
   
 0.958
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.
   
 0.958
AEF20760.1
Cytochrome b/b6 domain protein; 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.
  
 
 0.951
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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