| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AGB01284.1 | AGB03139.1 | Metfor_0202 | Metfor_2133 | PFAM: Asparagine synthase; TIGRFAM: asparagine synthase (glutamine-hydrolyzing). | PFAM: Asparagine synthase. | 0.960 |
| AGB01284.1 | aspS | Metfor_0202 | Metfor_0232 | PFAM: Asparagine synthase; TIGRFAM: asparagine synthase (glutamine-hydrolyzing). | aspartyl-tRNA synthetase, archaeal type; 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). | 0.635 |
| AGB01284.1 | gatA | Metfor_0202 | Metfor_2135 | PFAM: Asparagine synthase; TIGRFAM: asparagine synthase (glutamine-hydrolyzing). | glutamyl-tRNA(Gln) and/or aspartyl-tRNA(Asn) 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). | 0.896 |
| AGB01284.1 | gatB | Metfor_0202 | Metfor_2136 | PFAM: Asparagine synthase; TIGRFAM: asparagine synthase (glutamine-hydrolyzing). | glutamyl-tRNA(Gln) and/or aspartyl-tRNA(Asn) 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. | 0.854 |
| AGB01284.1 | gatC | Metfor_0202 | Metfor_2134 | PFAM: Asparagine synthase; TIGRFAM: asparagine synthase (glutamine-hydrolyzing). | glutamyl-tRNA(Gln) and/or aspartyl-tRNA(Asn) amidotransferase, C 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 GatC family. | 0.860 |
| AGB01284.1 | gatD | Metfor_0202 | Metfor_2409 | PFAM: Asparagine synthase; TIGRFAM: asparagine synthase (glutamine-hydrolyzing). | 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. | 0.829 |
| AGB01284.1 | gatE | Metfor_0202 | Metfor_2410 | PFAM: Asparagine synthase; TIGRFAM: asparagine synthase (glutamine-hydrolyzing). | 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. | 0.764 |
| AGB01284.1 | gltX | Metfor_0202 | Metfor_0500 | PFAM: Asparagine synthase; TIGRFAM: asparagine synthase (glutamine-hydrolyzing). | glutamyl-tRNA synthetase, archaeal and eukaryotic family; 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). | 0.706 |
| AGB01284.1 | topA | Metfor_0202 | Metfor_2137 | PFAM: Asparagine synthase; TIGRFAM: asparagine synthase (glutamine-hydrolyzing). | Topoisomerase IA; 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 superco [...] | 0.775 |
| AGB01284.1 | valS | Metfor_0202 | Metfor_1278 | PFAM: Asparagine synthase; TIGRFAM: asparagine synthase (glutamine-hydrolyzing). | 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. | 0.874 |
| AGB03139.1 | AGB01284.1 | Metfor_2133 | Metfor_0202 | PFAM: Asparagine synthase. | PFAM: Asparagine synthase; TIGRFAM: asparagine synthase (glutamine-hydrolyzing). | 0.960 |
| AGB03139.1 | gatA | Metfor_2133 | Metfor_2135 | PFAM: Asparagine synthase. | glutamyl-tRNA(Gln) and/or aspartyl-tRNA(Asn) 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). | 0.877 |
| AGB03139.1 | gatB | Metfor_2133 | Metfor_2136 | PFAM: Asparagine synthase. | glutamyl-tRNA(Gln) and/or aspartyl-tRNA(Asn) 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. | 0.877 |
| AGB03139.1 | gatC | Metfor_2133 | Metfor_2134 | PFAM: Asparagine synthase. | glutamyl-tRNA(Gln) and/or aspartyl-tRNA(Asn) amidotransferase, C 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 GatC family. | 0.870 |
| AGB03139.1 | gltX | Metfor_2133 | Metfor_0500 | PFAM: Asparagine synthase. | glutamyl-tRNA synthetase, archaeal and eukaryotic family; 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). | 0.468 |
| AGB03139.1 | topA | Metfor_2133 | Metfor_2137 | PFAM: Asparagine synthase. | Topoisomerase IA; 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 superco [...] | 0.924 |
| AGB03139.1 | valS | Metfor_2133 | Metfor_1278 | PFAM: Asparagine synthase. | 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. | 0.737 |
| aspS | AGB01284.1 | Metfor_0232 | Metfor_0202 | aspartyl-tRNA synthetase, archaeal type; 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). | PFAM: Asparagine synthase; TIGRFAM: asparagine synthase (glutamine-hydrolyzing). | 0.635 |
| aspS | gatA | Metfor_0232 | Metfor_2135 | aspartyl-tRNA synthetase, archaeal type; 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) and/or aspartyl-tRNA(Asn) 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). | 0.994 |
| aspS | gatB | Metfor_0232 | Metfor_2136 | aspartyl-tRNA synthetase, archaeal type; 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) and/or aspartyl-tRNA(Asn) 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. | 0.997 |