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gatD protein (Methanococcus voltae) - STRING interaction network
"gatD" - Glutamyl-tRNA(Gln) amidotransferase subunit D in Methanococcus voltae
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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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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
gatDGlutamyl-tRNA(Gln) amidotransferase subunit D; 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). The GatDE system is specific for glutamate and does not act on aspartate (450 aa)    
Predicted Functional Partners:
gatE
Glutamyl-tRNA(Gln) amidotransferase subunit E; 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). The GatDE system is specific for glutamate and does not act on aspartate (645 aa)
 
 
  0.999
gatA
Glutamyl-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) (433 aa)
       
  0.969
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 (468 aa)
 
 
  0.945
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) (438 aa)
   
 
  0.921
pth
Peptidyl-tRNA hydrolase; The natural substrate for this enzyme may be peptidyl- tRNAs which drop off the ribosome during protein synthesis (116 aa)
 
   
    0.916
Mvol_0135
TIGRFAM- Asp/Glu amidotransferase, subunit C (79 aa)
       
    0.806
argH
KEGG- sat-SYN_02158 argininosuccinate lyase; TIGRFAM- argininosuccinate lyase; PFAM- fumarate lyase (489 aa)
   
   
  0.720
Mvol_0830
Glutamine synthetase; KEGG- dat-HRM2_45740 GlnA2; TIGRFAM- glutamine synthetase, type I; PFAM- glutamine synthetase catalytic region; glutamine synthetase beta-Grasp (446 aa)
 
   
  0.684
pyrD
Dihydroorotate dehydrogenase; Catalyzes the conversion of dihydroorotate to orotate (319 aa)
   
   
  0.682
sepS
O-phosphoserine--tRNA(Cys) ligase; Catalyzes the attachment of O-phosphoserine (Sep) to tRNA(Cys) (562 aa)
   
   
  0.655
Your Current Organism:
Methanococcus voltae
NCBI taxonomy Id: 456320
Other names: M. voltae A3, Methanococcus voltae, Methanococcus voltae A3, Methanococcus voltae str. A3, Methanococcus voltae strain A3
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