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
AEB84617.1KEGG: ajs:Ajs_2775 ubiquinol oxidase, subunit II; TIGRFAM: Cytochrome o ubiquinol oxidase subunit II; PFAM: COX aromatic rich; Cytochrome c oxidase subunit II C-terminal. (329 aa)    
Predicted Functional Partners:
AEB84614.1
KEGG: ajs:Ajs_2778 cytochrome c oxidase subunit IV; TIGRFAM: Cytochrome o ubiquinol oxidase subunit IV; PFAM: Cytochrome C oxidase subunit IV prokaryotic.
 
 0.999
AEB84615.1
KEGG: dia:Dtpsy_2267 cytochrome o ubiquinol oxidase, subunit III; TIGRFAM: Cytochrome o ubiquinol oxidase, subunit III; PFAM: Cytochrome c oxidase, subunit III.
 
 0.999
AEB84616.1
TIGRFAM: Cytochrome o ubiquinol oxidase, subunit I; KEGG: ajs:Ajs_2776 cytochrome-c oxidase; PFAM: Cytochrome c oxidase, subunit I; Belongs to the heme-copper respiratory oxidase family.
 
 0.999
AEB86278.1
PFAM: Cytochrome c oxidase, subunit III; KEGG: dia:Dtpsy_2855 cytochrome c oxidase subunit III.
 
 0.974
AEB86274.1
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.
 
 0.970
AEB86229.1
Cytochrome-c oxidase; KEGG: app:CAP2UW1_1790 cytochrome c oxidase subunit I; PFAM: Cytochrome c oxidase, subunit I.
 
 0.957
AEB86224.1
KEGG: app:CAP2UW1_3424 putative cytochrome c oxidase, subunit I.
  
 0.949
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.
   
 0.948
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.
   
 0.948
AEB83452.1
KEGG: dia:Dtpsy_2798 respiratory-chain NADH dehydrogenase domain 51 kDa subunit; PFAM: NADH:ubiquinone oxidoreductase, 51kDa subunit; NADH:ubiquinone oxidoreductase, 24kDa subunit; Soluble ligand binding domain; NADH ubiquinone oxidoreductase, F subunit, iron sulphur binding; SMART: NADH ubiquinone oxidoreductase, F subunit, iron sulphur binding.
   
 0.947
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
Server load: low (26%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.