close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING • newly available directed regulatory networks • a new typed view showing functional, physical, and regulatory edges in one network • new clustering options and cluster-based layouts • … and much more!
Explore STRING v12.5 →
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
KMK94609.1Glycyl radical-activating protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (315 aa)    
Predicted Functional Partners:
KMK94172.1
Pyruvate-flavodoxin oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.997
KMK94608.1
Formate acetyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.965
KMK97530.1
With YgfM and YgfN forms a selenate reductase, which seems to catalyze the reduction of selenate to selenite; YgfK mutants are unable to reduce selenate; involved in purine salvage process; seems to act as an oxidoreductase, but sequence similarity suggests it is a dihydrothymine dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.937
KMK98221.1
Formate acetyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.931
KMK93496.1
Pyruvate formate-lyase; Formate acetyltransferase; catalyzes the formation of formate and acetyl-CoA from pyruvate; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.927
mdh
Malate dehydrogenase; Catalyzes the reversible oxidation of malate to oxaloacetate.
  
 
 0.916
KMK93260.1
Acetaldehyde dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase family.
 
 
 0.907
gltB
Catalyzes the formation of glutamate from glutamine and alpha-ketoglutarate; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.889
KMK94611.1
Phosphate propanoyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
   
 0.851
KMK90399.1
Phosphate acetyltransferase; Involved in acetate metabolism. In the N-terminal section; belongs to the CobB/CobQ family.
    
 0.846
Your Current Organism:
Aeromonas enteropelogenes
NCBI taxonomy Id: 29489
Other names: A. enteropelogenes, ATCC 49657 [[Aeromonas trota]], ATCC 49803, Aeromonas sp. LK14, Aeromonas trota, Aeromonas tructi, CCUG 29544 [[Aeromonas trota]], CCUG 30367 [[Aeromonas trota]], CECT 4255 [[Aeromonas trota]], CECT 4487, CIP 103677 [[Aeromonas trota]], CIP 104434, DSM 6394, DSM 7312 [[Aeromonas trota]], JCM 8315 [[Aeromonas trota]], JCM 8355, LMG 12223 [[Aeromonas trota]], LMG 12646, LMG:12223 [[Aeromonas trota]], LMG:12646, strain AH2 [[Aeromonas trota]], strain J11
Server load: low (40%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.