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
gatBAspartyl/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. (485 aa)    
Predicted Functional Partners:
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).
 
 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.
 
 0.998
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.
 
 0.994
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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.
  
 0.987
guaA
GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP.
  
 
 0.956
pheT
COGs: COG0072 Phenylalanyl-tRNA synthetase beta subunit; HAMAP: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; InterPro IPR004532: IPR002547: IPR005146: IPR005147: IPR 005121; KEGG: tte:TTE1688 phenylalanyl-tRNA synthetase subunit beta; PFAM: B3/B4 tRNA-binding domain; tRNA-binding domain; tRNA synthetase, B5; Phenylalanyl-tRNA synthetase, beta subunit, ferrodoxin-fold anticodon-binding; SPTR: Phenylalanyl-tRNA synthetase beta chain; TIGRFAM: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; PFAM: tRNA synthetase B5 domain; B3/4 domain; Ferredoxin-fol [...]
  
  
 0.812
ADY73312.1
COGs: COG0518 GMP synthase - Glutamine amidotransferase domain; InterPro IPR000991; KEGG: hya:HY04AAS1_1393 glutamine amidotransferase class-I; PFAM: Glutamine amidotransferase class-I, C-terminal; SPTR: Glutamine amidotransferase class-I; PFAM: Glutamine amidotransferase class-I.
   
 
 0.681
rpmC
Ribosomal protein L29; InterPro IPR001854; KEGG: cth:Cthe_2911 50S ribosomal protein L29; PFAM: Ribosomal protein L29; SPTR: Ribosomal protein L29; TIGRFAM: Ribosomal protein L29; PFAM: Ribosomal L29 protein; TIGRFAM: ribosomal protein L29; Belongs to the universal ribosomal protein uL29 family.
   
    0.652
ADY73771.1
ATP citrate synthase; COGs: COG0074 Succinyl-CoA synthetase alpha subunit; InterPro IPR003781: IPR005811; KEGG: pmx:PERMA_1714 ATP-citrate synthase (ATP-citrate (pro-S-)-lyase)(citrate cleavage enzyme); PFAM: ATP-citrate lyase/succinyl-CoA ligase; CoA-binding; PRIAM: ATP citrate synthase; SPTR: ATP-citrate synthase (ATP-citrate (Pro-S-)-lyase)(Citrate cleavage enzyme); PFAM: CoA-ligase; Citrate synthase.
  
 
 0.639
ADY72889.1
COGs: COG0069 Glutamate synthase domain 2; InterPro IPR000583: IPR006982: IPR002932: IPR002489; KEGG: hth:HTH_0871 ferredoxin-dependent glutamate synthase; PFAM: Glutamate synthase, central-C; Glutamine amidotransferase, class-II; Glutamate synthase, central-N; Glutamate synthase, alpha subunit, C-terminal; PRIAM: Glutamate synthase (ferredoxin); SPTR: Ferredoxin-dependent glutamate synthase; PFAM: Conserved region in glutamate synthase; GXGXG motif; Glutamate synthase central domain; Glutamine amidotransferases class-II.
  
 
 0.630
Your Current Organism:
Desulfurobacterium thermolithotrophum
NCBI taxonomy Id: 868864
Other names: D. thermolithotrophum DSM 11699, Desulfurobacterium thermolithotrophum BSA, Desulfurobacterium thermolithotrophum DSM 11699, Desulfurobacterium thermolithotrophum str. DSM 11699, Desulfurobacterium thermolithotrophum strain DSM 11699
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