STRINGSTRING
STRING protein interaction network
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.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
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Textmining
[Homology]
Score
Pnap_0882PFAM: cytochrome c oxidase, subunit III; KEGG: pol:Bpro_1249 cytochrome c oxidase, subunit III. (293 aa)    
Predicted Functional Partners:
Pnap_0878
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).
 
 0.999
Pnap_0879
Cytochrome-c oxidase; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B.
 0.999
ctaB
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.
 
 
 0.997
Pnap_0714
Cytochrome b/b6, N-terminal 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.
 
 
 0.995
Pnap_0713
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.
 
 0.991
Pnap_1326
KEGG: nmu:Nmul_A1998 nitrite reductase (NO-forming); TIGRFAM: nitrite reductase, copper-containing; PFAM: blue (type 1) copper domain protein; multicopper oxidase, type 2; multicopper oxidase, type 3; Belongs to the multicopper oxidase family.
  
 0.989
Pnap_1436
NADH dehydrogenase subunit M; KEGG: pol:Bpro_3244 proton-translocating NADH-quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I).
  
 
 0.981
nuoH
NADH dehydrogenase subunit H; 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.
  
 
 0.980
Pnap_0880
PFAM: cytochrome c oxidase assembly protein CtaG/Cox11; KEGG: pol:Bpro_1247 cytochrome c oxidase assembly protein CtaG/Cox11.
 
  
 0.973
Pnap_3779
Cytochrome c oxidase, cbb3-type, subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex.
  
 0.973
Your Current Organism:
Polaromonas naphthalenivorans
NCBI taxonomy Id: 365044
Other names: P. naphthalenivorans CJ2, Polaromonas naphthalenivorans CJ2, Polaromonas naphthalenivorans str. CJ2, Polaromonas naphthalenivorans strain CJ2
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