STRINGSTRING
AGA88798.1 AGA88798.1 AGA87038.1 AGA87038.1 AGA88795.1 AGA88795.1 AGA88796.1 AGA88796.1 AGA87037.1 AGA87037.1 AGA87769.1 AGA87769.1 AGA88797.1 AGA88797.1 AGA87770.1 AGA87770.1 cyoE cyoE atpB atpB AGA86823.1 AGA86823.1
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
AGA88798.1Heme/copper-type cytochrome/quinol oxidase, subunit 3; PFAM: Cytochrome c oxidase subunit III. (298 aa)    
Predicted Functional Partners:
AGA87038.1
PFAM: Cytochrome C and Quinol oxidase polypeptide I; TIGRFAM: cytochrome c oxidase, subunit I; Belongs to the heme-copper respiratory oxidase family.
 
 0.999
AGA88795.1
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).
 
 0.998
AGA88796.1
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.
 0.997
AGA87037.1
PFAM: Cytochrome C oxidase subunit II, periplasmic domain; Cytochrome c; TIGRFAM: cytochrome c oxidase, subunit II.
 
 0.993
AGA87769.1
Cytochrome b subunit of the bc complex; 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.
 
 
 0.989
AGA88797.1
PFAM: Cytochrome c oxidase assembly protein CtaG/Cox11.
 
  
 0.985
AGA87770.1
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.
 
 
 0.974
cyoE
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.
 
  
 0.969
atpB
F0F1-type ATP synthase, alpha subunit; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. Belongs to the ATPase A chain family.
   
 
 0.965
AGA86823.1
Dissimilatory nitrite reductase (NO-forming), copper type apoprotein; PFAM: Multicopper oxidase; Copper binding proteins, plastocyanin/azurin family; TIGRFAM: nitrite reductase, copper-containing.
  
 0.950
Your Current Organism:
Pseudomonas stutzeri
NCBI taxonomy Id: 644801
Other names: P. stutzeri RCH2, Pseudomonas stutzeri RCH2, Pseudomonas stutzeri str. RCH2, Pseudomonas stutzeri strain RCH2
Server load: low (20%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.