| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| LHA_1119 | LHA_1995 | LHA_1119 | LHA_1995 | Long-chain-fatty-acid--CoA ligase [Beta-ketoacyl synthase active site]; Function of strongly homologous gene; enzyme. | Beta-ketoacyl synthase (fragment). | 0.999 |
| LHA_1119 | asnS | LHA_1119 | LHA_1048 | Long-chain-fatty-acid--CoA ligase [Beta-ketoacyl synthase active site]; Function of strongly homologous gene; enzyme. | Asparaginyl-tRNA synthetase. | 0.598 |
| LHA_1119 | aspS | LHA_1119 | LHA_1682 | Long-chain-fatty-acid--CoA ligase [Beta-ketoacyl synthase active site]; Function of strongly homologous gene; enzyme. | 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. | 0.429 |
| LHA_1119 | carB | LHA_1119 | LHA_0851 | Long-chain-fatty-acid--CoA ligase [Beta-ketoacyl synthase active site]; Function of strongly homologous gene; enzyme. | Carbamoyl-phosphate synthase large chain; Belongs to the CarB family. | 0.558 |
| LHA_1119 | gatA | LHA_1119 | LHA_1419 | Long-chain-fatty-acid--CoA ligase [Beta-ketoacyl synthase active site]; Function of strongly homologous gene; enzyme. | 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). | 0.655 |
| LHA_1119 | gatB | LHA_1119 | LHA_1418 | Long-chain-fatty-acid--CoA ligase [Beta-ketoacyl synthase active site]; Function of strongly homologous gene; enzyme. | Aspartyl/glutamyl-tRNA(Asn/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. | 0.418 |
| LHA_1119 | glnS | LHA_1119 | LHA_1915 | Long-chain-fatty-acid--CoA ligase [Beta-ketoacyl synthase active site]; Function of strongly homologous gene; enzyme. | Glutaminyl-tRNA synthetase. | 0.500 |
| LHA_1119 | guaA | LHA_1119 | LHA_1436 | Long-chain-fatty-acid--CoA ligase [Beta-ketoacyl synthase active site]; Function of strongly homologous gene; enzyme. | GMP synthase [glutamine-hydrolyzing]; Catalyzes the synthesis of GMP from XMP. | 0.507 |
| LHA_1995 | LHA_1119 | LHA_1995 | LHA_1119 | Beta-ketoacyl synthase (fragment). | Long-chain-fatty-acid--CoA ligase [Beta-ketoacyl synthase active site]; Function of strongly homologous gene; enzyme. | 0.999 |
| LHA_1995 | asnS | LHA_1995 | LHA_1048 | Beta-ketoacyl synthase (fragment). | Asparaginyl-tRNA synthetase. | 0.598 |
| LHA_1995 | aspS | LHA_1995 | LHA_1682 | Beta-ketoacyl synthase (fragment). | 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. | 0.429 |
| LHA_1995 | carB | LHA_1995 | LHA_0851 | Beta-ketoacyl synthase (fragment). | Carbamoyl-phosphate synthase large chain; Belongs to the CarB family. | 0.558 |
| LHA_1995 | gatA | LHA_1995 | LHA_1419 | Beta-ketoacyl synthase (fragment). | 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). | 0.655 |
| LHA_1995 | gatB | LHA_1995 | LHA_1418 | Beta-ketoacyl synthase (fragment). | Aspartyl/glutamyl-tRNA(Asn/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. | 0.418 |
| LHA_1995 | glnS | LHA_1995 | LHA_1915 | Beta-ketoacyl synthase (fragment). | Glutaminyl-tRNA synthetase. | 0.500 |
| LHA_1995 | guaA | LHA_1995 | LHA_1436 | Beta-ketoacyl synthase (fragment). | GMP synthase [glutamine-hydrolyzing]; Catalyzes the synthesis of GMP from XMP. | 0.507 |
| asnS | LHA_1119 | LHA_1048 | LHA_1119 | Asparaginyl-tRNA synthetase. | Long-chain-fatty-acid--CoA ligase [Beta-ketoacyl synthase active site]; Function of strongly homologous gene; enzyme. | 0.598 |
| asnS | LHA_1995 | LHA_1048 | LHA_1995 | Asparaginyl-tRNA synthetase. | Beta-ketoacyl synthase (fragment). | 0.598 |
| asnS | aspS | LHA_1048 | LHA_1682 | Asparaginyl-tRNA synthetase. | 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. | 0.442 |
| asnS | gatA | LHA_1048 | LHA_1419 | Asparaginyl-tRNA synthetase. | 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). | 0.950 |