| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Bind_0846 | Bind_3031 | Bind_0846 | Bind_3031 | TIGRFAM: amino acid adenylation domain protein; PFAM: AMP-dependent synthetase and ligase; condensation domain protein; aminotransferase class-III; phosphopantetheine-binding; Beta-ketoacyl synthase; Acyl transferase; KEGG: mes:Meso_2580 amino acid adenylation domain; Belongs to the ATP-dependent AMP-binding enzyme family. | PFAM: glutamine amidotransferase class-II; glutamate synthase alpha subunit domain protein; ferredoxin-dependent glutamate synthase; glutamate synthase; KEGG: xau:Xaut_0477 glutamate synthase (ferredoxin). | 0.630 |
| Bind_0846 | gatA | Bind_0846 | Bind_1878 | TIGRFAM: amino acid adenylation domain protein; PFAM: AMP-dependent synthetase and ligase; condensation domain protein; aminotransferase class-III; phosphopantetheine-binding; Beta-ketoacyl synthase; Acyl transferase; KEGG: mes:Meso_2580 amino acid adenylation domain; Belongs to the ATP-dependent AMP-binding enzyme family. | glutamyl-tRNA(Gln) 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). | 0.589 |
| Bind_0846 | pyrB | Bind_0846 | Bind_3418 | TIGRFAM: amino acid adenylation domain protein; PFAM: AMP-dependent synthetase and ligase; condensation domain protein; aminotransferase class-III; phosphopantetheine-binding; Beta-ketoacyl synthase; Acyl transferase; KEGG: mes:Meso_2580 amino acid adenylation domain; Belongs to the ATP-dependent AMP-binding enzyme family. | KEGG: mex:Mext_3312 aspartate carbamoyltransferase; TIGRFAM: aspartate carbamoyltransferase; PFAM: aspartate/ornithine carbamoyltransferase Asp/Orn-binding region; aspartate/ornithine carbamoyltransferase carbamoyl-P binding domain; Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family. | 0.500 |
| Bind_3031 | Bind_0846 | Bind_3031 | Bind_0846 | PFAM: glutamine amidotransferase class-II; glutamate synthase alpha subunit domain protein; ferredoxin-dependent glutamate synthase; glutamate synthase; KEGG: xau:Xaut_0477 glutamate synthase (ferredoxin). | TIGRFAM: amino acid adenylation domain protein; PFAM: AMP-dependent synthetase and ligase; condensation domain protein; aminotransferase class-III; phosphopantetheine-binding; Beta-ketoacyl synthase; Acyl transferase; KEGG: mes:Meso_2580 amino acid adenylation domain; Belongs to the ATP-dependent AMP-binding enzyme family. | 0.630 |
| Bind_3031 | gatA | Bind_3031 | Bind_1878 | PFAM: glutamine amidotransferase class-II; glutamate synthase alpha subunit domain protein; ferredoxin-dependent glutamate synthase; glutamate synthase; KEGG: xau:Xaut_0477 glutamate synthase (ferredoxin). | glutamyl-tRNA(Gln) 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). | 0.534 |
| Bind_3031 | gatC | Bind_3031 | Bind_1879 | PFAM: glutamine amidotransferase class-II; glutamate synthase alpha subunit domain protein; ferredoxin-dependent glutamate synthase; glutamate synthase; KEGG: xau:Xaut_0477 glutamate synthase (ferredoxin). | 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. | 0.425 |
| Bind_3031 | pyrB | Bind_3031 | Bind_3418 | PFAM: glutamine amidotransferase class-II; glutamate synthase alpha subunit domain protein; ferredoxin-dependent glutamate synthase; glutamate synthase; KEGG: xau:Xaut_0477 glutamate synthase (ferredoxin). | KEGG: mex:Mext_3312 aspartate carbamoyltransferase; TIGRFAM: aspartate carbamoyltransferase; PFAM: aspartate/ornithine carbamoyltransferase Asp/Orn-binding region; aspartate/ornithine carbamoyltransferase carbamoyl-P binding domain; Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family. | 0.431 |
| Bind_3142 | gatA | Bind_3142 | Bind_1878 | TIGRFAM: urea amidolyase related protein; PFAM: Allophanate hydrolase subunit 2; KEGG: xau:Xaut_1495 UreA amidolyase related protein. | glutamyl-tRNA(Gln) 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). | 0.505 |
| aspS | gatA | Bind_1396 | Bind_1878 | 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. | glutamyl-tRNA(Gln) 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). | 0.789 |
| aspS | gatB | Bind_1396 | Bind_1877 | 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. | 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. | 0.994 |
| aspS | gatC | Bind_1396 | Bind_1879 | 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. | 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. | 0.894 |
| gatA | Bind_0846 | Bind_1878 | Bind_0846 | glutamyl-tRNA(Gln) 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). | TIGRFAM: amino acid adenylation domain protein; PFAM: AMP-dependent synthetase and ligase; condensation domain protein; aminotransferase class-III; phosphopantetheine-binding; Beta-ketoacyl synthase; Acyl transferase; KEGG: mes:Meso_2580 amino acid adenylation domain; Belongs to the ATP-dependent AMP-binding enzyme family. | 0.589 |
| gatA | Bind_3031 | Bind_1878 | Bind_3031 | glutamyl-tRNA(Gln) 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). | PFAM: glutamine amidotransferase class-II; glutamate synthase alpha subunit domain protein; ferredoxin-dependent glutamate synthase; glutamate synthase; KEGG: xau:Xaut_0477 glutamate synthase (ferredoxin). | 0.534 |
| gatA | Bind_3142 | Bind_1878 | Bind_3142 | glutamyl-tRNA(Gln) 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). | TIGRFAM: urea amidolyase related protein; PFAM: Allophanate hydrolase subunit 2; KEGG: xau:Xaut_1495 UreA amidolyase related protein. | 0.505 |
| gatA | aspS | Bind_1878 | Bind_1396 | glutamyl-tRNA(Gln) 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). | 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. | 0.789 |
| gatA | gatB | Bind_1878 | Bind_1877 | glutamyl-tRNA(Gln) 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). | 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 |
| gatA | gatC | Bind_1878 | Bind_1879 | glutamyl-tRNA(Gln) 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). | 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 |
| gatA | miaA | Bind_1878 | Bind_2853 | glutamyl-tRNA(Gln) 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). | tRNA delta(2)-isopentenylpyrophosphate transferase; Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A); Belongs to the IPP transferase family. | 0.501 |
| gatA | pyrB | Bind_1878 | Bind_3418 | glutamyl-tRNA(Gln) 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). | KEGG: mex:Mext_3312 aspartate carbamoyltransferase; TIGRFAM: aspartate carbamoyltransferase; PFAM: aspartate/ornithine carbamoyltransferase Asp/Orn-binding region; aspartate/ornithine carbamoyltransferase carbamoyl-P binding domain; Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family. | 0.666 |
| gatA | pyrE | Bind_1878 | Bind_2045 | glutamyl-tRNA(Gln) 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). | Orotate phosphoribosyltransferase; Catalyzes the transfer of a ribosyl phosphate group from 5- phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). | 0.491 |