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
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[Homology]
Score
gatAglutamyl-tRNA(Gln) and/or aspartyl-tRNA(Asn) amidotransferase, A subunit; 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). (494 aa)    
Predicted Functional Partners:
gatC
glutamyl-tRNA(Gln) and/or aspartyl-tRNA(Asn) amidotransferase, C subunit; 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
glutamyl-tRNA(Gln) and/or aspartyl-tRNA(Asn) amidotransferase, B subunit; 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
guaA
GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP.
  
 
 0.931
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.
  
 0.929
carB
Carbamoyl-phosphate synthase, large subunit; PFAM: Carbamoyl-phosphate synthase L chain, ATP binding domain; MGS-like domain; Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate synthase L chain, N-terminal domain; TIGRFAM: carbamoyl-phosphate synthase, large subunit; Belongs to the CarB family.
   
 
 0.928
carA
PFAM: Carbamoyl-phosphate synthase small chain, CPSase domain; Glutamine amidotransferase class-I; TIGRFAM: carbamoyl-phosphate synthase, small subunit; Belongs to the CarA family.
  
 
  0.900
hisH
Imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF.
  
 
 0.892
AGB26400.1
PFAM: Conserved region in glutamate synthase; GXGXG motif; Glutamate synthase central domain; Glutamine amidotransferases class-II.
    
 0.892
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.
  
 
 0.887
AGB24167.1
PFAM: Asparagine synthase; TIGRFAM: asparagine synthase (glutamine-hydrolyzing).
    
 0.885
Your Current Organism:
Mycobacterium sp. JS623
NCBI taxonomy Id: 212767
Other names: M. sp. JS623
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