| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ADZ09420.1 | aspS | Metbo_1176 | Metbo_1366 | KEGG: mst:Msp_0490 putative asparagine synthetase; TIGRFAM: Asparagine synthase, glutamine-hydrolyzing; PFAM: Asparagine synthase; Glutamine amidotransferase, class-II. | 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). | 0.417 |
| ADZ09420.1 | gatA | Metbo_1176 | Metbo_0049 | KEGG: mst:Msp_0490 putative asparagine synthetase; TIGRFAM: Asparagine synthase, glutamine-hydrolyzing; PFAM: Asparagine synthase; Glutamine amidotransferase, class-II. | 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). | 0.843 |
| ADZ09420.1 | gatB | Metbo_1176 | Metbo_0314 | KEGG: mst:Msp_0490 putative asparagine synthetase; TIGRFAM: Asparagine synthase, glutamine-hydrolyzing; PFAM: Asparagine synthase; Glutamine amidotransferase, class-II. | 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. | 0.939 |
| ADZ09420.1 | gatD | Metbo_1176 | Metbo_2448 | KEGG: mst:Msp_0490 putative asparagine synthetase; TIGRFAM: Asparagine synthase, glutamine-hydrolyzing; PFAM: Asparagine synthase; Glutamine amidotransferase, class-II. | Glutamyl-tRNA(Gln) amidotransferase subunit D; 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. | 0.693 |
| ADZ09420.1 | gatE | Metbo_1176 | Metbo_2447 | KEGG: mst:Msp_0490 putative asparagine synthetase; TIGRFAM: Asparagine synthase, glutamine-hydrolyzing; PFAM: Asparagine synthase; Glutamine amidotransferase, class-II. | Glutamyl-tRNA(Gln) amidotransferase subunit E; 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. | 0.641 |
| ADZ09420.1 | gltX | Metbo_1176 | Metbo_0823 | KEGG: mst:Msp_0490 putative asparagine synthetase; TIGRFAM: Asparagine synthase, glutamine-hydrolyzing; PFAM: Asparagine synthase; Glutamine amidotransferase, class-II. | 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). | 0.521 |
| ADZ10659.1 | aspS | Metbo_2446 | Metbo_1366 | KEGG: mmg:MTBMA_c10960 thioredoxin reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase. | 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). | 0.532 |
| ADZ10659.1 | cysS | Metbo_2446 | Metbo_1210 | KEGG: mmg:MTBMA_c10960 thioredoxin reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase. | SMART: Cysteinyl-tRNA synthetase, class Ia, DALR; TIGRFAM: Cysteinyl-tRNA synthetase, class Ia; KEGG: mst:Msp_0124 hypothetical protein; PFAM: Cysteinyl-tRNA synthetase, class Ia; Cysteinyl-tRNA synthetase, class Ia, DALR; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.647 |
| ADZ10659.1 | gatD | Metbo_2446 | Metbo_2448 | KEGG: mmg:MTBMA_c10960 thioredoxin reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase. | Glutamyl-tRNA(Gln) amidotransferase subunit D; 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. | 0.752 |
| ADZ10659.1 | gatE | Metbo_2446 | Metbo_2447 | KEGG: mmg:MTBMA_c10960 thioredoxin reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase. | Glutamyl-tRNA(Gln) amidotransferase subunit E; 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. | 0.770 |
| ADZ10659.1 | gltX | Metbo_2446 | Metbo_0823 | KEGG: mmg:MTBMA_c10960 thioredoxin reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase. | 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). | 0.533 |
| ADZ10659.1 | valS | Metbo_2446 | Metbo_0943 | KEGG: mmg:MTBMA_c10960 thioredoxin reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase. | Valyl-tRNA synthetase; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 2 subfamily. | 0.572 |
| aspS | ADZ09420.1 | Metbo_1366 | Metbo_1176 | 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). | KEGG: mst:Msp_0490 putative asparagine synthetase; TIGRFAM: Asparagine synthase, glutamine-hydrolyzing; PFAM: Asparagine synthase; Glutamine amidotransferase, class-II. | 0.417 |
| aspS | ADZ10659.1 | Metbo_1366 | Metbo_2446 | 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). | KEGG: mmg:MTBMA_c10960 thioredoxin reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase. | 0.532 |
| aspS | cysS | Metbo_1366 | Metbo_1210 | 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). | SMART: Cysteinyl-tRNA synthetase, class Ia, DALR; TIGRFAM: Cysteinyl-tRNA synthetase, class Ia; KEGG: mst:Msp_0124 hypothetical protein; PFAM: Cysteinyl-tRNA synthetase, class Ia; Cysteinyl-tRNA synthetase, class Ia, DALR; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.638 |
| aspS | gatA | Metbo_1366 | Metbo_0049 | 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(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). | 0.992 |
| aspS | gatB | Metbo_1366 | Metbo_0314 | 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). | 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. | 0.998 |
| aspS | gatD | Metbo_1366 | Metbo_2448 | 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(Gln) amidotransferase subunit D; 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. | 0.686 |
| aspS | gatE | Metbo_1366 | Metbo_2447 | 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(Gln) amidotransferase subunit E; 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. | 0.666 |
| aspS | gltX | Metbo_1366 | Metbo_0823 | 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). | 0.934 |