| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AFZ71847.1 | gatA | Natgr_0598 | Natgr_0218 | acetyl/propionyl-CoA carboxylase, alpha subunit; PFAM: Carbamoyl-phosphate synthase L chain, ATP binding domain; Biotin carboxylase C-terminal domain; Carbamoyl-phosphate synthase L chain, N-terminal domain; Biotin-requiring enzyme; TIGRFAM: acetyl-CoA carboxylase, biotin carboxylase subunit. | 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). | 0.797 |
| AFZ73584.1 | gatA | Natgr_2415 | Natgr_0218 | Putative membrane-associated Zn-dependent protease; PFAM: Peptidase family M50. | 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). | 0.692 |
| aspC | gatA | Natgr_2086 | Natgr_0218 | 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). | 0.965 |
| aspC | gatB | Natgr_2086 | Natgr_3674 | 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. | 0.991 |
| aspC | gatC | Natgr_2086 | Natgr_0219 | 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, 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. | 0.971 |
| aspC | gatE | Natgr_2086 | Natgr_3830 | 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). | Archaeal Glu-tRNAGln amidotransferase subunit E (contains GAD domain); 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. | 0.487 |
| aspC | gltX | Natgr_2086 | Natgr_2571 | 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 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). | 0.822 |
| aspC | guaAB | Natgr_2086 | Natgr_1007 | 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). | GMP synthase, glutamine-hydrolyzing, C-terminal domain or B subunit; Catalyzes the synthesis of GMP from XMP. | 0.514 |
| carB | gatA | Natgr_3603 | Natgr_0218 | Carbamoyl-phosphate synthase, large subunit; PFAM: Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate synthase L chain, N-terminal domain; TIGRFAM: carbamoyl-phosphate synthase, large subunit; Belongs to the CarB family. | 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). | 0.765 |
| carB | gatB | Natgr_3603 | Natgr_3674 | Carbamoyl-phosphate synthase, large subunit; PFAM: Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate synthase L chain, N-terminal domain; TIGRFAM: carbamoyl-phosphate synthase, large subunit; Belongs to the CarB family. | 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. | 0.507 |
| carB | gatC | Natgr_3603 | Natgr_0219 | Carbamoyl-phosphate synthase, large subunit; PFAM: Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate synthase L chain, N-terminal domain; TIGRFAM: carbamoyl-phosphate synthase, large subunit; Belongs to the CarB family. | 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. | 0.519 |
| carB | gatD | Natgr_3603 | Natgr_0739 | Carbamoyl-phosphate synthase, large subunit; PFAM: Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate synthase L chain, N-terminal domain; TIGRFAM: carbamoyl-phosphate synthase, large subunit; Belongs to the CarB family. | 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. | 0.560 |
| carB | gatE | Natgr_3603 | Natgr_3830 | Carbamoyl-phosphate synthase, large subunit; PFAM: Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate synthase L chain, N-terminal domain; TIGRFAM: carbamoyl-phosphate synthase, large subunit; Belongs to the CarB family. | Archaeal Glu-tRNAGln amidotransferase subunit E (contains GAD domain); 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. | 0.550 |
| carB | gltX | Natgr_3603 | Natgr_2571 | Carbamoyl-phosphate synthase, large subunit; PFAM: Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate synthase L chain, N-terminal domain; TIGRFAM: carbamoyl-phosphate synthase, large subunit; Belongs to the CarB family. | 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). | 0.435 |
| carB | guaAB | Natgr_3603 | Natgr_1007 | Carbamoyl-phosphate synthase, large subunit; PFAM: Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate synthase L chain, N-terminal domain; TIGRFAM: carbamoyl-phosphate synthase, large subunit; Belongs to the CarB family. | GMP synthase, glutamine-hydrolyzing, C-terminal domain or B subunit; Catalyzes the synthesis of GMP from XMP. | 0.789 |
| gatA | AFZ71847.1 | Natgr_0218 | Natgr_0598 | 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). | acetyl/propionyl-CoA carboxylase, alpha subunit; PFAM: Carbamoyl-phosphate synthase L chain, ATP binding domain; Biotin carboxylase C-terminal domain; Carbamoyl-phosphate synthase L chain, N-terminal domain; Biotin-requiring enzyme; TIGRFAM: acetyl-CoA carboxylase, biotin carboxylase subunit. | 0.797 |
| gatA | AFZ73584.1 | Natgr_0218 | Natgr_2415 | 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). | Putative membrane-associated Zn-dependent protease; PFAM: Peptidase family M50. | 0.692 |
| gatA | aspC | Natgr_0218 | Natgr_2086 | 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). | 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). | 0.965 |
| gatA | carB | Natgr_0218 | Natgr_3603 | 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). | Carbamoyl-phosphate synthase, large subunit; PFAM: Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate synthase L chain, N-terminal domain; TIGRFAM: carbamoyl-phosphate synthase, large subunit; Belongs to the CarB family. | 0.765 |
| gatA | gatB | Natgr_0218 | Natgr_3674 | 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). | 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. | 0.998 |