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_415 | gltX | MTH_415 | MTH_51 | Conserved protein; Function Code:14.01 - Unknown, Conserved protein; similar to, sp:LN:Y243_METJA AC:Q57694, p()=0.000000092, pid=37%. | glutamyl-tRNA 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). | 0.413 |
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 | gltX | MTH_226 | MTH_51 | 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). | glutamyl-tRNA 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). | 0.971 |
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 |