| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ACX72031.1 | ACX73424.1 | Metvu_0164 | Metvu_1571 | TIGRFAM: asparagine synthase (glutamine-hydrolyzing); PFAM: asparagine synthase; glutamine amidotransferase class-II; KEGG: mja:MJ1116 asparagine synthetase (AsnB). | TIGRFAM: Asp/Glu amidotransferase, subunit C; KEGG: mja:MJ0243 aspartyl/glutamyl-tRNA amidotransferase subunit C. | 0.879 |
| ACX72031.1 | ACX73506.1 | Metvu_0164 | Metvu_1653 | TIGRFAM: asparagine synthase (glutamine-hydrolyzing); PFAM: asparagine synthase; glutamine amidotransferase class-II; KEGG: mja:MJ1116 asparagine synthetase (AsnB). | KEGG: mfe:Mefer_0195 acetolactate synthase, small subunit; TIGRFAM: acetolactate synthase, small subunit; PFAM: Acetolactate synthase, small subunit-like; amino acid-binding ACT domain protein. | 0.530 |
| ACX72031.1 | aspS | Metvu_0164 | Metvu_1266 | TIGRFAM: asparagine synthase (glutamine-hydrolyzing); PFAM: asparagine synthase; glutamine amidotransferase class-II; KEGG: mja:MJ1116 asparagine synthetase (AsnB). | 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). | 0.753 |
| ACX72031.1 | gatA | Metvu_0164 | Metvu_1709 | TIGRFAM: asparagine synthase (glutamine-hydrolyzing); PFAM: asparagine synthase; glutamine amidotransferase class-II; KEGG: mja:MJ1116 asparagine synthetase (AsnB). | glutamyl-tRNA(Gln) amidotransferase, A subunit; 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). | 0.940 |
| ACX72031.1 | gatB | Metvu_0164 | Metvu_1652 | TIGRFAM: asparagine synthase (glutamine-hydrolyzing); PFAM: asparagine synthase; glutamine amidotransferase class-II; KEGG: mja:MJ1116 asparagine synthetase (AsnB). | glutamyl-tRNA(Gln) amidotransferase, B subunit; 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. | 0.882 |
| ACX72031.1 | gatD | Metvu_0164 | Metvu_0698 | TIGRFAM: asparagine synthase (glutamine-hydrolyzing); PFAM: asparagine synthase; glutamine amidotransferase class-II; KEGG: mja:MJ1116 asparagine synthetase (AsnB). | 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. | 0.916 |
| ACX72031.1 | gatE | Metvu_0164 | Metvu_0695 | TIGRFAM: asparagine synthase (glutamine-hydrolyzing); PFAM: asparagine synthase; glutamine amidotransferase class-II; KEGG: mja:MJ1116 asparagine synthetase (AsnB). | aspartyl-tRNA(Asn) amidotransferase, B subunit; 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. | 0.827 |
| ACX72031.1 | gltX | Metvu_0164 | Metvu_1350 | TIGRFAM: asparagine synthase (glutamine-hydrolyzing); PFAM: asparagine synthase; glutamine amidotransferase class-II; KEGG: mja:MJ1116 asparagine synthetase (AsnB). | 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). | 0.768 |
| ACX72031.1 | proS | Metvu_0164 | Metvu_0171 | TIGRFAM: asparagine synthase (glutamine-hydrolyzing); PFAM: asparagine synthase; glutamine amidotransferase class-II; KEGG: mja:MJ1116 asparagine synthetase (AsnB). | 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). | 0.768 |
| ACX72031.1 | topA | Metvu_0164 | Metvu_0725 | TIGRFAM: asparagine synthase (glutamine-hydrolyzing); PFAM: asparagine synthase; glutamine amidotransferase class-II; KEGG: mja:MJ1116 asparagine synthetase (AsnB). | DNA topoisomerase I; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...] | 0.831 |
| ACX73424.1 | ACX72031.1 | Metvu_1571 | Metvu_0164 | TIGRFAM: Asp/Glu amidotransferase, subunit C; KEGG: mja:MJ0243 aspartyl/glutamyl-tRNA amidotransferase subunit C. | TIGRFAM: asparagine synthase (glutamine-hydrolyzing); PFAM: asparagine synthase; glutamine amidotransferase class-II; KEGG: mja:MJ1116 asparagine synthetase (AsnB). | 0.879 |
| ACX73424.1 | aspS | Metvu_1571 | Metvu_1266 | TIGRFAM: Asp/Glu amidotransferase, subunit C; KEGG: mja:MJ0243 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). | 0.981 |
| ACX73424.1 | gatA | Metvu_1571 | Metvu_1709 | TIGRFAM: Asp/Glu amidotransferase, subunit C; KEGG: mja:MJ0243 aspartyl/glutamyl-tRNA amidotransferase subunit C. | glutamyl-tRNA(Gln) amidotransferase, A subunit; 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 |
| ACX73424.1 | gatB | Metvu_1571 | Metvu_1652 | TIGRFAM: Asp/Glu amidotransferase, subunit C; KEGG: mja:MJ0243 aspartyl/glutamyl-tRNA amidotransferase subunit C. | glutamyl-tRNA(Gln) amidotransferase, B subunit; 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 |
| ACX73424.1 | gatD | Metvu_1571 | Metvu_0698 | TIGRFAM: Asp/Glu amidotransferase, subunit C; KEGG: mja:MJ0243 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. | 0.913 |
| ACX73424.1 | gatE | Metvu_1571 | Metvu_0695 | TIGRFAM: Asp/Glu amidotransferase, subunit C; KEGG: mja:MJ0243 aspartyl/glutamyl-tRNA amidotransferase subunit C. | aspartyl-tRNA(Asn) amidotransferase, B subunit; 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. | 0.910 |
| ACX73424.1 | topA | Metvu_1571 | Metvu_0725 | TIGRFAM: Asp/Glu amidotransferase, subunit C; KEGG: mja:MJ0243 aspartyl/glutamyl-tRNA amidotransferase subunit C. | DNA topoisomerase I; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...] | 0.739 |
| ACX73506.1 | ACX72031.1 | Metvu_1653 | Metvu_0164 | KEGG: mfe:Mefer_0195 acetolactate synthase, small subunit; TIGRFAM: acetolactate synthase, small subunit; PFAM: Acetolactate synthase, small subunit-like; amino acid-binding ACT domain protein. | TIGRFAM: asparagine synthase (glutamine-hydrolyzing); PFAM: asparagine synthase; glutamine amidotransferase class-II; KEGG: mja:MJ1116 asparagine synthetase (AsnB). | 0.530 |
| ACX73506.1 | gatB | Metvu_1653 | Metvu_1652 | KEGG: mfe:Mefer_0195 acetolactate synthase, small subunit; TIGRFAM: acetolactate synthase, small subunit; PFAM: Acetolactate synthase, small subunit-like; amino acid-binding ACT domain protein. | glutamyl-tRNA(Gln) amidotransferase, B subunit; 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. | 0.874 |
| aspS | ACX72031.1 | Metvu_1266 | Metvu_0164 | 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: asparagine synthase (glutamine-hydrolyzing); PFAM: asparagine synthase; glutamine amidotransferase class-II; KEGG: mja:MJ1116 asparagine synthetase (AsnB). | 0.753 |