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
iaaHIndole acetimide hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the amidase family. (475 aa)    
Predicted Functional Partners:
gatB
glutamyl-tRNA amidotransferase; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily.
 0.991
gatC
glutamyl-tRNA amidotransferase; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family.
 
 0.984
accC
acetyl-CoA carboxylase biotin carboxylase subunit; This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.
 
 
 0.898
ALO39136.1
Carboxylase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.874
ALO38019.1
Aldehyde dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the aldehyde dehydrogenase family.
     
  0.863
ALO39027.1
Nitrilase; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
  0.862
ALO38558.1
3-methylcrotonyl-CoA carboxylase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.815
glnS
glutaminyl-tRNA synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.805
ALO38470.1
Amidase; Catalyzes the hydrolysis of a monocarboxylic acid amid to form a monocarboxylate and ammonia; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the amidase family.
  
  
 
0.733
aspS
aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
  
 0.725
Your Current Organism:
Alcaligenes faecalis
NCBI taxonomy Id: 511
Other names: A. faecalis, ATCC 8750, Achromobacter sp. ATCC8750, Alcaligenes sp. BP11, CIP 55.84, CIP 60.80, DSM 30030, IAM 12369, IFO 13111, JCM 20522, JCM 20663, NBRC 13111, NCAIM B.01104, NCIMB 8156, NCTC 11953
Server load: low (20%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.