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
Swoo_0430TIGRFAM: cytochrome o ubiquinol oxidase subunit IV; PFAM: cytochrome C oxidase subunit IV; KEGG: shw:Sputw3181_0092 cytochrome c oxidase subunit IV. (111 aa)    
Predicted Functional Partners:
Swoo_0431
TIGRFAM: cytochrome o ubiquinol oxidase, subunit III; PFAM: cytochrome c oxidase subunit III; KEGG: sfr:Sfri_0222 cytochrome c oxidase, subunit III.
 
 0.999
Swoo_0432
KEGG: shm:Shewmr7_3915 cytochrome-c oxidase; TIGRFAM: cytochrome o ubiquinol oxidase, subunit I; PFAM: cytochrome c oxidase subunit I; Belongs to the heme-copper respiratory oxidase family.
 
 0.999
Swoo_0433
TIGRFAM: ubiquinol oxidase, subunit II; PFAM: cytochrome c oxidase subunit II; COX aromatic rich domain protein; KEGG: shn:Shewana3_4031 ubiquinol oxidase, subunit II.
 
 0.999
cyoE2
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.
 
  
 0.987
Swoo_0178
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).
  
 
 0.977
Swoo_0175
PFAM: cytochrome c oxidase subunit III; KEGG: sse:Ssed_0195 cytochrome c oxidase, subunit III.
  
 
 0.966
Swoo_0177
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.
  
 
 0.966
cyoE1
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.
  
  
 0.837
Swoo_1833
TIGRFAM: succinate dehydrogenase, cytochrome b556 subunit; PFAM: succinate dehydrogenase cytochrome b subunit; KEGG: sse:Ssed_2818 succinate dehydrogenase, cytochrome b subunit.
   
 
  0.692
nuoC
NADH dehydrogenase I, D subunit; 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; In the N-terminal section; belongs to the complex I 30 kDa subunit family.
   
 
 0.634
Your Current Organism:
Shewanella woodyi
NCBI taxonomy Id: 392500
Other names: S. woodyi ATCC 51908, Shewanella woodyi ATCC 51908, Shewanella woodyi str. ATCC 51908, Shewanella woodyi strain ATCC 51908
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.