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
gatAGlutamyl-tRNA(Gln) amidotransferase subunit A (Glu-ADT subunit A); Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). (491 aa)    
Predicted Functional Partners:
aspS
aspartyl-tRNA synthetase; 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.
 
 0.999
gatB
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B (Asp/Glu-ADT subunit B); 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.
 0.999
aspC
aspartyl-tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
 
 0.992
glnS
glutamyl-tRNA synthetase; Function of homologous gene experimentally demonstrated in an other organism; enzyme.
  
 0.979
gltX
glutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
  
 0.979
asnS
Asparaginyl tRNA synthetase; Function of homologous gene experimentally demonstrated in an other organism; enzyme.
  
 0.976
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.
    
 0.907
guaA
GMP synthetase (glutamine aminotransferase); Catalyzes the synthesis of GMP from XMP.
  
 
 0.818
carB
Carbamoyl-phosphate synthase large subunit; Function of homologous gene experimentally demonstrated in an other organism; enzyme.
   
 
 0.719
purD
Phosphoribosylamine--glycine ligase (modular protein); Belongs to the GARS family.
  
  
 0.701
Your Current Organism:
Acetoanaerobium sticklandii
NCBI taxonomy Id: 1511
Other names: A. sticklandii, ATCC 12662, BCRC 14485, CCRC 14485, CCRC:14485, CCUG 9281, Clostridium sticklandii, DSM 519, NCIMB 10654, strain StadtmanHF
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.