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
Oant_0048TIGRFAM: ubiquinol oxidase, subunit II; PFAM: cytochrome c oxidase subunit II; COX aromatic rich domain protein; KEGG: bmb:BruAb1_0042 CyoA, ubiquinol oxidase, subunit II. (335 aa)    
Predicted Functional Partners:
Oant_0049
TIGRFAM: Cytochrome o ubiquinol oxidase subunit I; PFAM: cytochrome c oxidase subunit I; KEGG: bme:BMEI1900 cytochrome O ubiquinol oxidase subunit I; Belongs to the heme-copper respiratory oxidase family.
 
 0.999
Oant_0050
TIGRFAM: Cytochrome o ubiquinol oxidase subunit III; PFAM: cytochrome c oxidase subunit III; KEGG: bms:BR0044 ubiquinol oxidase subunit III.
 
 0.999
Oant_0051
TIGRFAM: Cytochrome o ubiquinol oxidase subunit IV; PFAM: cytochrome C oxidase subunit IV; KEGG: bmb:BruAb1_0045 QoxD, ubiquinol oxidase subunit IV.
 
 0.999
Oant_0582
Cytochrome c oxidase subunit I type; 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.
 
 0.984
Oant_4384
PFAM: cytochrome c oxidase subunit III; KEGG: bms:BRA0246 cytochrome c oxidase, subunit III.
 
 0.976
Oant_2411
TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I); KEGG: bms:BR0814 NADH dehydrogenase I, M subunit.
   
 0.966
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.
   
 0.966
Oant_1624
Cytochrome b/b6 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.
  
 
 0.965
Oant_0586
PFAM: cytochrome c oxidase subunit III; KEGG: bmb:BruAb1_0494 CoxC, cytochrome c oxidase, subunit III.
  
 0.959
nuoA
NADH-ubiquinone/plastoquinone oxidoreductase chain 3; 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; Belongs to the complex I subunit 3 family.
   
 0.953
Your Current Organism:
Ochrobactrum anthropi
NCBI taxonomy Id: 439375
Other names: O. anthropi ATCC 49188, Ochrobactrum anthropi ATCC 49188, Ochrobactrum anthropi DSM 6882, Ochrobactrum anthropi LMG 3331, Ochrobactrum anthropi str. ATCC 49188, Ochrobactrum anthropi strain ATCC 49188
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