Nodes:
Network nodes represent proteins
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
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
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from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
AEB86230.1PFAM: Cytochrome c oxidase subunit II C-terminal; KEGG: app:CAP2UW1_1791 cytochrome c oxidase subunit II. (179 aa)    
Predicted Functional Partners:
AEB86229.1
Cytochrome-c oxidase; KEGG: app:CAP2UW1_1790 cytochrome c oxidase subunit I; PFAM: Cytochrome c oxidase, subunit I.
 
 0.999
AEB86224.1
KEGG: app:CAP2UW1_3424 putative cytochrome c oxidase, subunit I.
 
 0.998
AEB86226.1
PFAM: Methyl-viologen-reducing hydrogenase, delta subunit; 4Fe-4S binding domain; KEGG: app:CAP2UW1_1327 methyl-viologen-reducing hydrogenase delta subunit.
 
 
 0.985
AEB86223.1
KEGG: app:CAP2UW1_1324 oxidoreductase FAD-binding domain protein; PFAM: Oxidoreductase, FAD-binding domain; Ferredoxin; Cytochrome b/b6, N-terminal; Oxidoreductase FAD/NAD(P)-binding.
 
 
 0.976
AEB86227.1
PFAM: Copper chaperone SCO1/SenC; KEGG: app:CAP2UW1_1788 electron transport protein SCO1/SenC.
 
 0.970
AEB86273.1
Cytochrome 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).
 
 0.964
AEB84615.1
KEGG: dia:Dtpsy_2267 cytochrome o ubiquinol oxidase, subunit III; TIGRFAM: Cytochrome o ubiquinol oxidase, subunit III; PFAM: Cytochrome c oxidase, subunit III.
 
 0.958
AEB86278.1
PFAM: Cytochrome c oxidase, subunit III; KEGG: dia:Dtpsy_2855 cytochrome c oxidase subunit III.
 
 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.
   
 0.948
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.
   
 0.944
Your Current Organism:
Alicycliphilus denitrificans
NCBI taxonomy Id: 596154
Other names: A. denitrificans K601, Alicycliphilus denitrificans DSM 14773, Alicycliphilus denitrificans K601, Alicycliphilus denitrificans str. K601, Alicycliphilus denitrificans strain K601, Pseudomonas sp. K601, beta proteobacterium K601
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