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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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.
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experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
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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). (496 aa)    
Predicted Functional Partners:
gatB
glutamyl-tRNA(Gln) 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
gatC
glutamyl-tRNA(Gln) 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
glnS
TIGRFAM: Glutaminyl-tRNA synthetase, class Ic; KEGG: ajs:Ajs_1608 glutaminyl-tRNA synthetase; PFAM: Glutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain; Glutamyl/glutaminyl-tRNA synthetase, class Ic, anti-codon binding domain.
  
 0.951
AEB85801.1
PFAM: Amidase; KEGG: ajs:Ajs_2586 amidase; Belongs to the amidase family.
 
  
 
0.931
AEB82672.1
PFAM: Amidase; KEGG: reh:H16_A1882 Asp-tRNA Asn / Glu-tRNA Gln amidotransferase A subunit or related amidase.
 
  
0.929
AEB83347.1
PFAM: Amidase; KEGG: dia:Dtpsy_0815 amidase.
 
  
0.927
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.
 
 
 0.838
guaA
GMP synthase, large subunit; Catalyzes the synthesis of GMP from XMP.
  
 
 0.711
AEB82750.1
Rod shape-determining protein MreC; Involved in formation and maintenance of cell shape.
  
    0.709
carB
SMART: Methylglyoxal synthase-like domain; TIGRFAM: Carbamoyl-phosphate synthase, large subunit; KEGG: dia:Dtpsy_1458 carbamoyl-phosphate synthase, large subunit; PFAM: Carbamoyl-phosphate synthetase, large subunit, ATP-binding; Carbamoyl-phosphate synthetase, large subunit, oligomerisation; Methylglyoxal synthase-like domain; Carbamoyl-phosphate synthase, large subunit, N-terminal; Belongs to the CarB family.
   
 
 0.682
Your Current Organism:
Alicycliphilus denitrificans
NCBI taxonomy Id: 596154
Other names: A. denitrificans K601, Alicycliphilus denitrificans DSM 14773, Alicycliphilus denitrificans K601, Alicycliphilus denitrificans str. K601, Alicycliphilus denitrificans strain K601, Pseudomonas sp. K601, beta proteobacterium K601
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