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STRINGSTRING
gatA protein (Methylobacter tundripaludum) - STRING interaction network
"gatA" - Glutamyl-tRNA(Gln) amidotransferase subunit A in Methylobacter tundripaludum
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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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 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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Score
gatAGlutamyl-tRNA(Gln) amidotransferase 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) (483 aa)    
Predicted Functional Partners:
gatB
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase 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 (478 aa)
  0.999
gatC
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C; 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 (95 aa)
 
  0.998
gltX
Glutamate--tRNA ligase; 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) (467 aa)
   
  0.993
pth
Peptidyl-tRNA hydrolase; The natural substrate for this enzyme may be peptidyl- tRNAs which drop off the ribosome during protein synthesis; Belongs to the PTH family (189 aa)
       
    0.978
aspS
Aspartate--tRNA(Asp/Asn) ligase; 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 (596 aa)
 
  0.952
glnS
Glutamine--tRNA ligase; PFAM- Glutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain; Glutamyl/glutaminyl-tRNA synthetase, class Ic, anti-codon binding domain; TIGRFAM- Glutaminyl-tRNA synthetase, class Ic; HAMAP- Glutaminyl-tRNA synthetase; KEGG- gpb-HDN1F_33480 glutaminyl-tRNA synthetase (554 aa)
   
  0.933
gluQ
Glutamyl-Q tRNA(Asp) synthetase; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5- dihydroxy-2-cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon (301 aa)
   
  0.933
Mettu_1387
PFAM- Protein of unknown function DUF820; KEGG- dfe-Dfer_4673 protein of unknown function DUF820 (201 aa)
              0.831
Mettu_2634
TIGRFAM- Acetyl-CoA carboxylase, biotin carboxylase; KEGG- tgr-Tgr7_0368 acetyl-CoA carboxylase, biotin carboxylase; PFAM- Carbamoyl phosphate synthetase, large subunit, ATP-binding; Carbamoyl phosphate synthase, large subunit, N-terminal; Biotin carboxylase, C-terminal (447 aa)
 
  0.812
Mettu_2468
PFAM- Nitrilase/cyanide hydratase and apolipoprotein N-acyltransferase; KEGG- mca-MCA0381 carbon-nitrogen family hydrolase (267 aa)
       
  0.802
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum SV96, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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