| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ADZ09419.1 | ADZ09420.1 | Metbo_1175 | Metbo_1176 | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mst:Msp_0489 aspartyl/glutamyl-tRNA amidotransferase subunit C. | KEGG: mst:Msp_0490 putative asparagine synthetase; TIGRFAM: Asparagine synthase, glutamine-hydrolyzing; PFAM: Asparagine synthase; Glutamine amidotransferase, class-II. | 0.925 |
| ADZ09419.1 | aspS | Metbo_1175 | Metbo_1366 | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mst:Msp_0489 aspartyl/glutamyl-tRNA amidotransferase subunit C. | 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). | 0.911 |
| ADZ09419.1 | gatA | Metbo_1175 | Metbo_0049 | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mst:Msp_0489 aspartyl/glutamyl-tRNA amidotransferase subunit C. | 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). | 0.999 |
| ADZ09419.1 | gatB | Metbo_1175 | Metbo_0314 | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mst:Msp_0489 aspartyl/glutamyl-tRNA amidotransferase subunit C. | 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. | 0.999 |
| ADZ09419.1 | gatD | Metbo_1175 | Metbo_2448 | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mst:Msp_0489 aspartyl/glutamyl-tRNA amidotransferase subunit C. | 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. | 0.557 |
| ADZ09419.1 | gatE | Metbo_1175 | Metbo_2447 | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mst:Msp_0489 aspartyl/glutamyl-tRNA amidotransferase subunit C. | 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. | 0.563 |
| ADZ09419.1 | hisH | Metbo_1175 | Metbo_0039 | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mst:Msp_0489 aspartyl/glutamyl-tRNA amidotransferase subunit C. | Imidazole glycerol phosphate synthase subunit hisH; IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF. | 0.662 |
| ADZ09419.1 | rpl13 | Metbo_1175 | Metbo_0810 | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mst:Msp_0489 aspartyl/glutamyl-tRNA amidotransferase subunit C. | Ribosomal protein L13; This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly. | 0.408 |
| ADZ09420.1 | ADZ09419.1 | Metbo_1176 | Metbo_1175 | KEGG: mst:Msp_0490 putative asparagine synthetase; TIGRFAM: Asparagine synthase, glutamine-hydrolyzing; PFAM: Asparagine synthase; Glutamine amidotransferase, class-II. | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mst:Msp_0489 aspartyl/glutamyl-tRNA amidotransferase subunit C. | 0.925 |
| 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 |
| ADZ09420.1 | hisH | Metbo_1176 | Metbo_0039 | KEGG: mst:Msp_0490 putative asparagine synthetase; TIGRFAM: Asparagine synthase, glutamine-hydrolyzing; PFAM: Asparagine synthase; Glutamine amidotransferase, class-II. | Imidazole glycerol phosphate synthase subunit hisH; IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF. | 0.823 |
| ADZ09420.1 | proS | Metbo_1176 | Metbo_1014 | KEGG: mst:Msp_0490 putative asparagine synthetase; TIGRFAM: Asparagine synthase, glutamine-hydrolyzing; PFAM: Asparagine synthase; Glutamine amidotransferase, class-II. | Prolyl-tRNA synthetase; 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). | 0.455 |
| aspS | ADZ09419.1 | Metbo_1366 | Metbo_1175 | 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). | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mst:Msp_0489 aspartyl/glutamyl-tRNA amidotransferase subunit C. | 0.911 |
| 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 | 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 |