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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experimentally determined
co-expression
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gene co-occurrence
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AEB86223.1KEGG: app:CAP2UW1_1324 oxidoreductase FAD-binding domain protein; PFAM: Oxidoreductase, FAD-binding domain; Ferredoxin; Cytochrome b/b6, N-terminal; Oxidoreductase FAD/NAD(P)-binding. (642 aa)    
Predicted Functional Partners:
AEB83274.1
Cytochrome c1; KEGG: ajs:Ajs_0791 cytochrome c1; manually curated; PFAM: Cytochrome c1.
  
 0.984
AEB83272.1
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.
  
 0.980
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).
  
 
 0.978
AEB86230.1
PFAM: Cytochrome c oxidase subunit II C-terminal; KEGG: app:CAP2UW1_1791 cytochrome c oxidase subunit II.
 
 
 0.976
pyrD
Dihydroorotate dehydrogenase; Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor; Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.
  
 
 0.971
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.
  
 
 0.970
AEB83456.1
PFAM: 4Fe-4S binding domain; KEGG: ajs:Ajs_3467 4Fe-4S ferredoxin iron-sulfur binding domain-containing protein.
  
 
 0.968
AEB86226.1
PFAM: Methyl-viologen-reducing hydrogenase, delta subunit; 4Fe-4S binding domain; KEGG: app:CAP2UW1_1327 methyl-viologen-reducing hydrogenase delta subunit.
 
 
0.966
AEB86341.1
TIGRFAM: NADH-quinone oxidoreductase, chain M/4; KEGG: dia:Dtpsy_0884 proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH:ubiquinone/plastoquinone oxidoreductase; NADH:ubiquinone oxidoreductase, chain 4, N-terminal.
  
 
 0.964
AEB83353.1
KEGG: dia:Dtpsy_0821 4Fe-4S ferredoxin iron-sulfur binding domain protein.
  
 
 0.959
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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