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
Databases
Textmining
[Homology]
Score
ADD67783.1PFAM: cytochrome c oxidase subunit III; KEGG: dde:Dde_1824 cytochrome c oxidase, subunit III. (199 aa)    
Predicted Functional Partners:
ADD67780.1
PFAM: UbiA prenyltransferase; KEGG: dde:Dde_1827 protoheme IX farnesyltransferase, putative.
 
 
 0.999
ADD67781.1
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).
 
 0.999
ADD67784.1
Cytochrome c oxidase, subunit I; 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
ADD68308.1
KEGG: gbm:Gbem_1236 cytochrome c oxidase, cbb3- type, subunit II; TIGRFAM: cytochrome c oxidase, cbb3-type, subunit II; PFAM: cytochrome C oxidase mono-heme subunit/FixO; cytochrome c class I.
  
 0.998
ADD68561.1
PFAM: Cytochrome b/b6 domain; KEGG: glo:Glov_1196 cytochrome b/b6 domain.
 
 
 0.996
atpB
ATP synthase F0, A subunit; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
  
 
 0.995
ADD67782.1
TIGRFAM: caa(3)-type oxidase, subunit IV; KEGG: dde:Dde_1825 Caa(3)-type oxidase, subunit IV.
 
 
 0.995
ADD68560.1
PFAM: Rieske [2Fe-2S] iron-sulphur domain; KEGG: geo:Geob_1345 Rieske (2Fe-2S) domain protein.
  
 
 0.991
ADD66829.1
KEGG: gur:Gura_4232 proton-translocating NADH- quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I).
  
 
 0.988
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.
  
 
 0.987
Your Current Organism:
Denitrovibrio acetiphilus
NCBI taxonomy Id: 522772
Other names: D. acetiphilus DSM 12809, Denitrovibrio acetiphilus DSM 12809, Denitrovibrio acetiphilus N2460, Denitrovibrio acetiphilus str. DSM 12809, Denitrovibrio acetiphilus strain DSM 12809
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