STRINGSTRING
AGA88797.1 AGA88797.1 cyoE cyoE AGA88802.1 AGA88802.1 AGA88798.1 AGA88798.1 AGA88795.1 AGA88795.1 AGA88800.1 AGA88800.1 AGA88796.1 AGA88796.1 AGA88801.1 AGA88801.1 AGA87037.1 AGA87037.1 AGA85406.1 AGA85406.1 AGA86922.1 AGA86922.1
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.
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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
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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
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[Homology]
Score
AGA88797.1PFAM: Cytochrome c oxidase assembly protein CtaG/Cox11. (191 aa)    
Predicted Functional Partners:
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.
 
 0.995
AGA88802.1
PFAM: Cytochrome oxidase assembly protein.
 
 0.993
AGA88798.1
Heme/copper-type cytochrome/quinol oxidase, subunit 3; PFAM: Cytochrome c oxidase subunit III.
 
  
 0.985
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).
 
  
 0.982
AGA88800.1
Hypothetical protein; PFAM: SURF1 family.
 
 
 0.968
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.
 
  
 0.919
AGA88801.1
Hypothetical protein.
 
 
 0.906
AGA87037.1
PFAM: Cytochrome C oxidase subunit II, periplasmic domain; Cytochrome c; TIGRFAM: cytochrome c oxidase, subunit II.
 
  
 0.819
AGA85406.1
Heme/copper-type cytochrome/quinol oxidase, subunit 3; PFAM: Cytochrome c oxidase subunit III.
 
  
 0.807
AGA86922.1
Putative NAD/FAD-binding protein; PFAM: Flavin containing amine oxidoreductase.
 
      0.802
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
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