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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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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
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textmining
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experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
Daci_2985KEGG: aav:Aave_3388 cytochrome c553-like protein. (281 aa)    
Predicted Functional Partners:
Daci_2986
Gluconate 2-dehydrogenase (acceptor); PFAM: cytochrome c class I; KEGG: aav:Aave_3387 cytochrome c, class I.
 
 0.967
Daci_5501
PFAM: cytochrome c1; KEGG: aav:Aave_3694 cytochrome c1.
 
 
 0.901
Daci_5503
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.
 
 
 0.875
Daci_0498
PFAM: cytochrome c class I; KEGG: aav:Aave_0385 cytochrome c, class I.
 
 
 
 0.830
Daci_2987
PFAM: Thioredoxin domain; KEGG: aav:Aave_3386 hypothetical protein.
   
 
 0.780
Daci_5502
Cytochrome b/b6 domain; 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.
 
 
 0.739
Daci_3929
Gluconate 2-dehydrogenase (acceptor); PFAM: cytochrome c class I; KEGG: spe:Spro_2490 gluconate 2-dehydrogenase (acceptor).
 
 0.649
Daci_3169
Gluconate 2-dehydrogenase (acceptor); PFAM: cytochrome c class I; KEGG: spe:Spro_4016 gluconate 2-dehydrogenase (acceptor).
 
 0.629
Daci_2499
Gluconate 2-dehydrogenase (acceptor); PFAM: cytochrome c class I; KEGG: rme:Rmet_2155 cytochrome c, class I.
 
 0.603
Daci_1674
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).
 
 
 0.600
Your Current Organism:
Delftia acidovorans
NCBI taxonomy Id: 398578
Other names: D. acidovorans SPH-1, Delftia acidovorans SPH-1, Delftia acidovorans str. SPH-1, Delftia acidovorans strain SPH-1
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