| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AF_1439 | aspS | AF_1439 | AF_0920 | Asparagine synthetase (asnB); Similar to GB:L77117 SP:Q58516 PID:1591755 percent identity: 36.88; identified by sequence similarity; putative. | aspartyl-tRNA synthetase (aspS); 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). | 0.471 |
| AF_1439 | gatA | AF_1439 | AF_2329 | Asparagine synthetase (asnB); Similar to GB:L77117 SP:Q58516 PID:1591755 percent identity: 36.88; identified by sequence similarity; putative. | Glu-tRNA amidotransferase, subunit A (gatA-2); 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) (By similarity). | 0.668 |
| AF_1439 | gatB | AF_1439 | AF_2116 | Asparagine synthetase (asnB); Similar to GB:L77117 SP:Q58516 PID:1591755 percent identity: 36.88; identified by sequence similarity; putative. | Glu-tRNA amidotransferase, subunit B (gatB-2); 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) (By similarity); Belongs to the GatB/GatE family. GatB subfamily. | 0.803 |
| AF_1439 | gatC | AF_1439 | AF_2328 | Asparagine synthetase (asnB); Similar to GB:L77117 SP:Q58516 PID:1591755 percent identity: 36.88; identified by sequence similarity; putative. | Glu-tRNA amidotransferase, subunit C (gatC); 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) (By similarity); Belongs to the GatC family. | 0.814 |
| AF_1439 | gatD | AF_1439 | AF_0882 | Asparagine synthetase (asnB); Similar to GB:L77117 SP:Q58516 PID:1591755 percent identity: 36.88; identified by sequence similarity; putative. | Asparaginase (asnA); 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. | 0.664 |
| AF_1439 | gatE | AF_1439 | AF_1440 | Asparagine synthetase (asnB); Similar to GB:L77117 SP:Q58516 PID:1591755 percent identity: 36.88; identified by sequence similarity; putative. | Glu-tRNA amidotransferase, subunit B (gatB-1); 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. | 0.863 |
| AF_1439 | guaAB | AF_1439 | AF_0253 | Asparagine synthetase (asnB); Similar to GB:L77117 SP:Q58516 PID:1591755 percent identity: 36.88; identified by sequence similarity; putative. | GMP synthase (guaA-1); Catalyzes the synthesis of GMP from XMP. | 0.420 |
| AF_1954 | aspS | AF_1954 | AF_0920 | Glu-tRNA amidotransferase, subunit A (gatA-1); Similar to SP:Q11056 PID:1480323 percent identity: 38.61; identified by sequence similarity; putative. | aspartyl-tRNA synthetase (aspS); 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). | 0.988 |
| AF_1954 | gatA | AF_1954 | AF_2329 | Glu-tRNA amidotransferase, subunit A (gatA-1); Similar to SP:Q11056 PID:1480323 percent identity: 38.61; identified by sequence similarity; putative. | Glu-tRNA amidotransferase, subunit A (gatA-2); 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) (By similarity). | 0.911 |
| AF_1954 | gatB | AF_1954 | AF_2116 | Glu-tRNA amidotransferase, subunit A (gatA-1); Similar to SP:Q11056 PID:1480323 percent identity: 38.61; identified by sequence similarity; putative. | Glu-tRNA amidotransferase, subunit B (gatB-2); 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) (By similarity); Belongs to the GatB/GatE family. GatB subfamily. | 0.999 |
| AF_1954 | gatC | AF_1954 | AF_2328 | Glu-tRNA amidotransferase, subunit A (gatA-1); Similar to SP:Q11056 PID:1480323 percent identity: 38.61; identified by sequence similarity; putative. | Glu-tRNA amidotransferase, subunit C (gatC); 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) (By similarity); Belongs to the GatC family. | 0.996 |
| AF_1954 | gatD | AF_1954 | AF_0882 | Glu-tRNA amidotransferase, subunit A (gatA-1); Similar to SP:Q11056 PID:1480323 percent identity: 38.61; identified by sequence similarity; putative. | Asparaginase (asnA); 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. | 0.949 |
| AF_1954 | gatE | AF_1954 | AF_1440 | Glu-tRNA amidotransferase, subunit A (gatA-1); Similar to SP:Q11056 PID:1480323 percent identity: 38.61; identified by sequence similarity; putative. | Glu-tRNA amidotransferase, subunit B (gatB-1); 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. | 0.966 |
| AF_1954 | gltX | AF_1954 | AF_0260 | Glu-tRNA amidotransferase, subunit A (gatA-1); Similar to SP:Q11056 PID:1480323 percent identity: 38.61; identified by sequence similarity; putative. | glutamyl-tRNA synthetase (gltX); 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). | 0.840 |
| AF_1954 | proS | AF_1954 | AF_1609 | Glu-tRNA amidotransferase, subunit A (gatA-1); Similar to SP:Q11056 PID:1480323 percent identity: 38.61; identified by sequence similarity; putative. | prolyl-tRNA synthetase (proS); 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). | 0.738 |
| aspS | AF_1439 | AF_0920 | AF_1439 | aspartyl-tRNA synthetase (aspS); 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 (asnB); Similar to GB:L77117 SP:Q58516 PID:1591755 percent identity: 36.88; identified by sequence similarity; putative. | 0.471 |
| aspS | AF_1954 | AF_0920 | AF_1954 | aspartyl-tRNA synthetase (aspS); 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). | Glu-tRNA amidotransferase, subunit A (gatA-1); Similar to SP:Q11056 PID:1480323 percent identity: 38.61; identified by sequence similarity; putative. | 0.988 |
| aspS | gatA | AF_0920 | AF_2329 | aspartyl-tRNA synthetase (aspS); 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). | Glu-tRNA amidotransferase, subunit A (gatA-2); 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) (By similarity). | 0.995 |
| aspS | gatB | AF_0920 | AF_2116 | aspartyl-tRNA synthetase (aspS); 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). | Glu-tRNA amidotransferase, subunit B (gatB-2); 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) (By similarity); Belongs to the GatB/GatE family. GatB subfamily. | 0.999 |
| aspS | gatC | AF_0920 | AF_2328 | aspartyl-tRNA synthetase (aspS); 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). | Glu-tRNA amidotransferase, subunit C (gatC); 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) (By similarity); Belongs to the GatC family. | 0.991 |