| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| MTH_415 | aspS | MTH_415 | MTH_226 | Conserved protein; Function Code:14.01 - Unknown, Conserved protein; similar to, sp:LN:Y243_METJA AC:Q57694, p()=0.000000092, pid=37%. | 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). | 0.989 |
| MTH_415 | gatA | MTH_415 | MTH_1496 | Conserved protein; Function Code:14.01 - Unknown, Conserved protein; similar to, sp:LN:Y243_METJA AC:Q57694, p()=0.000000092, pid=37%. | Amidase; 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). | 0.999 |
| MTH_415 | gatB | MTH_415 | MTH_1280 | Conserved protein; Function Code:14.01 - Unknown, Conserved protein; similar to, sp:LN:Y243_METJA AC:Q57694, p()=0.000000092, pid=37%. | PET112-like protein; 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 |
| MTH_415 | gatD | MTH_415 | MTH_706 | Conserved protein; Function Code:14.01 - Unknown, Conserved protein; similar to, sp:LN:Y243_METJA AC:Q57694, p()=0.000000092, pid=37%. | L-asparaginase I; 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. | 0.914 |
| MTH_415 | gatE | MTH_415 | MTH_707 | Conserved protein; Function Code:14.01 - Unknown, Conserved protein; similar to, sp:LN:Y243_METJA AC:Q57694, p()=0.000000092, pid=37%. | PET112-like protein; 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. | 0.914 |
| MTH_702 | gatD | MTH_702 | MTH_706 | acetyl-CoA synthetase related protein; Function Code:1.08 - Carbohydrate Metabolism, Pyruvate and acetyl-CoA metabolism; similar to, pir:LN:A61209 AC:A61209, p()=9.9E-43, pid=62%. | L-asparaginase I; 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. | 0.780 |
| MTH_702 | gatE | MTH_702 | MTH_707 | acetyl-CoA synthetase related protein; Function Code:1.08 - Carbohydrate Metabolism, Pyruvate and acetyl-CoA metabolism; similar to, pir:LN:A61209 AC:A61209, p()=9.9E-43, pid=62%. | PET112-like protein; 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. | 0.780 |
| MTH_702 | vorA | MTH_702 | MTH_705 | acetyl-CoA synthetase related protein; Function Code:1.08 - Carbohydrate Metabolism, Pyruvate and acetyl-CoA metabolism; similar to, pir:LN:A61209 AC:A61209, p()=9.9E-43, pid=62%. | 2-oxoisovalerate oxidoreductase, alpha subunit; Function Code:2.08 - Energy Metabolism, Electron transport; similar to, pir:LN:A64367 AC:A64367, p()=5E-28, pid=16%. | 0.842 |
| MTH_702 | vorB | MTH_702 | MTH_704 | acetyl-CoA synthetase related protein; Function Code:1.08 - Carbohydrate Metabolism, Pyruvate and acetyl-CoA metabolism; similar to, pir:LN:A61209 AC:A61209, p()=9.9E-43, pid=62%. | 2-oxoisovalerate oxidoreductase, beta subunit; Function Code:2.08 - Energy Metabolism, Electron transport; similar to, pir:LN:E64334 AC:E64334, p()=1E-51, pid=34%. | 0.849 |
| MTH_702 | vorC | MTH_702 | MTH_703 | acetyl-CoA synthetase related protein; Function Code:1.08 - Carbohydrate Metabolism, Pyruvate and acetyl-CoA metabolism; similar to, pir:LN:A61209 AC:A61209, p()=9.9E-43, pid=62%. | 2-oxoisovalerate oxidoreductase, gamma subunit; Function Code:2.08 - Energy Metabolism, Electron transport; similar to, sp:LN:FER3_METJA AC:Q57610, p()=0.000015, pid=39%. | 0.921 |
| aspS | MTH_415 | MTH_226 | MTH_415 | 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). | Conserved protein; Function Code:14.01 - Unknown, Conserved protein; similar to, sp:LN:Y243_METJA AC:Q57694, p()=0.000000092, pid=37%. | 0.989 |
| aspS | gatA | MTH_226 | MTH_1496 | 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). | Amidase; 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). | 0.999 |
| aspS | gatB | MTH_226 | MTH_1280 | 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). | PET112-like protein; 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 | gatD | MTH_226 | MTH_706 | 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). | L-asparaginase I; 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. | 0.866 |
| aspS | gatE | MTH_226 | MTH_707 | 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). | PET112-like protein; 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. | 0.887 |
| aspS | mre11 | MTH_226 | MTH_541 | 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). | Rad32 related protein; Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Mre11 binds to DSB ends and has both double-stranded 3'-5' exonuclease activity and single-stranded endonuclease activity. Belongs to the MRE11/RAD32 family. | 0.770 |
| gatA | MTH_415 | MTH_1496 | MTH_415 | Amidase; 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). | Conserved protein; Function Code:14.01 - Unknown, Conserved protein; similar to, sp:LN:Y243_METJA AC:Q57694, p()=0.000000092, pid=37%. | 0.999 |
| gatA | aspS | MTH_1496 | MTH_226 | Amidase; 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). | 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). | 0.999 |
| gatA | gatB | MTH_1496 | MTH_1280 | Amidase; 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). | PET112-like protein; 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 | gatD | MTH_1496 | MTH_706 | Amidase; 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). | L-asparaginase I; 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. | 0.989 |