| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AKB65118.1 | AKB66049.1 | MSMAS_1922 | MSMAS_2853 | Asparagine synthetase (glutamine-hydrolyzing). | Pyruvate carboxyl transferase subunit A. | 0.661 |
| AKB65118.1 | aspS | MSMAS_1922 | MSMAS_1255 | Asparagine synthetase (glutamine-hydrolyzing). | Aspartyl-tRNA synthetase / Aspartyl-tRNA(Asn) 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). | 0.567 |
| AKB65118.1 | carB | MSMAS_1922 | MSMAS_1290 | Asparagine synthetase (glutamine-hydrolyzing). | Carbamoyl-phosphate synthase large chain; Belongs to the CarB family. | 0.912 |
| AKB65118.1 | gatA | MSMAS_1922 | MSMAS_0085 | Asparagine synthetase (glutamine-hydrolyzing). | Aspartyl-tRNA(Asn) amidotransferase subunit A / 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). | 0.856 |
| AKB65118.1 | gatB | MSMAS_1922 | MSMAS_0084 | Asparagine synthetase (glutamine-hydrolyzing). | Aspartyl-tRNA(Asn) amidotransferase subunit B / Glutamyl-tRNA(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. | 0.929 |
| AKB65118.1 | gatC | MSMAS_1922 | MSMAS_0086 | Asparagine synthetase (glutamine-hydrolyzing). | Aspartyl-tRNA(Asn) amidotransferase subunit C / Glutamyl-tRNA(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. | 0.839 |
| AKB65118.1 | gatD | MSMAS_1922 | MSMAS_2395 | Asparagine synthetase (glutamine-hydrolyzing). | Glutamyl-tRNA(Gln) amidotransferase asparaginase 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). The GatDE system is specific for glutamate and does not act on aspartate. | 0.824 |
| AKB65118.1 | gatE | MSMAS_1922 | MSMAS_1278 | Asparagine synthetase (glutamine-hydrolyzing). | Glutamyl-tRNA(Gln) amidotransferase transferase 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). The GatDE system is specific for glutamate and does not act on aspartate. | 0.871 |
| AKB65118.1 | gltX | MSMAS_1922 | MSMAS_2930 | Asparagine synthetase (glutamine-hydrolyzing). | Glutamyl-tRNA synthetase / Glutamyl-tRNA(Gln) 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). | 0.410 |
| AKB65118.1 | proS | MSMAS_1922 | MSMAS_0606 | Asparagine synthetase (glutamine-hydrolyzing). | Prolyl-tRNA synthetase, archaeal/eukaryal type; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). | 0.410 |
| AKB66049.1 | AKB65118.1 | MSMAS_2853 | MSMAS_1922 | Pyruvate carboxyl transferase subunit A. | Asparagine synthetase (glutamine-hydrolyzing). | 0.661 |
| AKB66049.1 | carB | MSMAS_2853 | MSMAS_1290 | Pyruvate carboxyl transferase subunit A. | Carbamoyl-phosphate synthase large chain; Belongs to the CarB family. | 0.618 |
| AKB66049.1 | gatA | MSMAS_2853 | MSMAS_0085 | Pyruvate carboxyl transferase subunit A. | Aspartyl-tRNA(Asn) amidotransferase subunit A / 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). | 0.870 |
| AKB66049.1 | gatB | MSMAS_2853 | MSMAS_0084 | Pyruvate carboxyl transferase subunit A. | Aspartyl-tRNA(Asn) amidotransferase subunit B / Glutamyl-tRNA(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. | 0.758 |
| aspS | AKB65118.1 | MSMAS_1255 | MSMAS_1922 | Aspartyl-tRNA synthetase / Aspartyl-tRNA(Asn) 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). | Asparagine synthetase (glutamine-hydrolyzing). | 0.567 |
| aspS | gatA | MSMAS_1255 | MSMAS_0085 | Aspartyl-tRNA synthetase / Aspartyl-tRNA(Asn) 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). | Aspartyl-tRNA(Asn) amidotransferase subunit A / 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). | 0.998 |
| aspS | gatB | MSMAS_1255 | MSMAS_0084 | Aspartyl-tRNA synthetase / Aspartyl-tRNA(Asn) 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). | Aspartyl-tRNA(Asn) amidotransferase subunit B / Glutamyl-tRNA(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. | 0.999 |
| aspS | gatC | MSMAS_1255 | MSMAS_0086 | Aspartyl-tRNA synthetase / Aspartyl-tRNA(Asn) 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). | Aspartyl-tRNA(Asn) amidotransferase subunit C / Glutamyl-tRNA(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. | 0.994 |
| aspS | gatD | MSMAS_1255 | MSMAS_2395 | Aspartyl-tRNA synthetase / Aspartyl-tRNA(Asn) 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). | Glutamyl-tRNA(Gln) amidotransferase asparaginase 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). The GatDE system is specific for glutamate and does not act on aspartate. | 0.846 |
| aspS | gatE | MSMAS_1255 | MSMAS_1278 | Aspartyl-tRNA synthetase / Aspartyl-tRNA(Asn) 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). | Glutamyl-tRNA(Gln) amidotransferase transferase 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). The GatDE system is specific for glutamate and does not act on aspartate. | 0.864 |