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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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co-expression
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gene neighborhood
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[Homology]
Score
AMS40589.1Cytochrome C. (131 aa)    
Predicted Functional Partners:
AMS41333.1
Ubiquinol-cytochrome C reductase; 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.
 
 0.973
AMS41335.1
Ribosomal protein P2; Pfam:pfam02167 Cytochrome C1 family.
 
 0.968
AMS41334.1
Cytochrome B; 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.
 
 0.930
AMS43288.1
Cysteine desulfurase; Pfam:pfam12796 Ankyrin repeats (3 copies).
  
 
0.929
AMS44384.1
Hypothetical protein.
  
  
 
0.916
AMS39754.1
Cytochrome CBB3; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex.
  
 
 0.906
AMS43900.1
Cbb3-type cytochrome c oxidase subunit; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex.
  
 
 0.906
AMS43162.1
Twin-arginine translocation pathway signal; Pfam:pfam00355 Rieske [2Fe-2S] domain.
  
 0.897
AMS40587.1
Pfam:pfam00510 Cytochrome c oxidase subunit III.
  
 0.849
nuoI
NADH-quinone oxidoreductase subunit I; 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.
  
 
 0.839
Your Current Organism:
Aminobacter aminovorans
NCBI taxonomy Id: 83263
Other names: A. aminovorans, ATCC 23314, ATCC 29600, Aminobacter heintzii, CCUG 2081, CIP 106737, Chelatobacter heintzii, DSM 10368, DSM 7048, JCM 7852, KCTC 2477, LMG 2122, LMG:2122, NCCB 26039, NCIB 9039, NCIB:9039, NCIMB 9039, NCTC 10684, Pseudomonas aminovorans, VKM B-2058
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