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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
iorBIndolepyruvate oxidoreductase subunit IorB. (191 aa)    
Predicted Functional Partners:
iorA
Indolepyruvate oxidoreductase subunit IorA; Catalyzes the ferredoxin-dependent oxidative decarboxylation of arylpyruvates.
 
 0.995
MCP_1959
Conserved hypothetical protein; Catalyzes the ferredoxin-dependent oxidative decarboxylation of arylpyruvates.
 
 0.827
MCP_1258
Pyruvate synthase beta chain; Similar to Ketoisovalerate oxidoreductase beta VorB in Pyrococcus furiosus (Q51802).
  
 
 0.825
MCP_2614
Similar to Pyruvate synthase beta chain PorB in Pyrococcus furiosus (Q51805).
  
 
 0.825
MCP_1257
Similar to Ketoisovalerate oxidoreductase alpha chain VorA in Pyrococcus furiosus (Q51801).
  
 
 0.715
MCP_2613
Similar to Pyruvate synthase alpha chain PorA in Pyrococcus furiosus (Q51804).
  
 
 0.715
MCP_1255
Pyruvate synthase delta chain; Similar to Ketoisovalerate oxidoreductase delta subunit VorB in Pyrococcus furiosus (Q51800).
  
 
 0.713
MCP_2612
Similar to Pyruvate synthase delta chain PorB in Pyrococcus furiosus (Q51803).
  
 
 0.713
aroC
Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
   
 
 0.660
MCP_1191
Conserved hypothetical protein; Contains two Amino acid-binding ACT domains (IPR002912).
 
    0.630
Your Current Organism:
Methanocella paludicola
NCBI taxonomy Id: 304371
Other names: M. paludicola SANAE, Methanocella paludicola SANAE, methanogenic archaeon SANAE, methanogenic archaeon str. SANAE, methanogenic archaeon strain SANAE
Server load: medium (48%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.