| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| EHA59278.1 | EHA64096.1 | Syn8016DRAFT_2648 | Syn8016DRAFT_1138 | KEGG: pmt:PMT1777 ferredoxin-dependent glutamate synthase; PFAM: Glutamate synthase, central-C; Glutamine amidotransferase, class-II; Glutamate synthase, central-N; Glutamate synthase, alpha subunit, C-terminal. | GatB region; PFAM: Glutamyl-tRNA(Gln) amidotransferase, subunit B/E, N-terminal; KEGG: pmf:P9303_28281 aspartyl/glutamyl-tRNA amidotransferase subunit B. | 0.904 |
| EHA59278.1 | aspS | Syn8016DRAFT_2648 | Syn8016DRAFT_2072 | KEGG: pmt:PMT1777 ferredoxin-dependent glutamate synthase; PFAM: Glutamate synthase, central-C; Glutamine amidotransferase, class-II; Glutamate synthase, central-N; Glutamate synthase, alpha subunit, C-terminal. | 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); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 0.877 |
| EHA59278.1 | gatA | Syn8016DRAFT_2648 | Syn8016DRAFT_0745 | KEGG: pmt:PMT1777 ferredoxin-dependent glutamate synthase; PFAM: Glutamate synthase, central-C; Glutamine amidotransferase, class-II; Glutamate synthase, central-N; Glutamate synthase, alpha subunit, C-terminal. | 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). | 0.928 |
| EHA59278.1 | gatB | Syn8016DRAFT_2648 | Syn8016DRAFT_1973 | KEGG: pmt:PMT1777 ferredoxin-dependent glutamate synthase; PFAM: Glutamate synthase, central-C; Glutamine amidotransferase, class-II; Glutamate synthase, central-N; Glutamate synthase, alpha subunit, C-terminal. | 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. | 0.904 |
| EHA59278.1 | gatC | Syn8016DRAFT_2648 | Syn8016DRAFT_1517 | KEGG: pmt:PMT1777 ferredoxin-dependent glutamate synthase; PFAM: Glutamate synthase, central-C; Glutamine amidotransferase, class-II; Glutamate synthase, central-N; Glutamate synthase, alpha subunit, C-terminal. | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C; 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. | 0.912 |
| EHA59278.1 | guaA | Syn8016DRAFT_2648 | Syn8016DRAFT_2868 | KEGG: pmt:PMT1777 ferredoxin-dependent glutamate synthase; PFAM: Glutamate synthase, central-C; Glutamine amidotransferase, class-II; Glutamate synthase, central-N; Glutamate synthase, alpha subunit, C-terminal. | GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP. | 0.966 |
| EHA59278.1 | pheT | Syn8016DRAFT_2648 | Syn8016DRAFT_0416 | KEGG: pmt:PMT1777 ferredoxin-dependent glutamate synthase; PFAM: Glutamate synthase, central-C; Glutamine amidotransferase, class-II; Glutamate synthase, central-N; Glutamate synthase, alpha subunit, C-terminal. | TIGRFAM: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; KEGG: pmf:P9303_14801 phenylalanyl-tRNA synthetase subunit beta; HAMAP: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial. | 0.653 |
| EHA59278.1 | pyrG | Syn8016DRAFT_2648 | Syn8016DRAFT_2076 | KEGG: pmt:PMT1777 ferredoxin-dependent glutamate synthase; PFAM: Glutamate synthase, central-C; Glutamine amidotransferase, class-II; Glutamate synthase, central-N; Glutamate synthase, alpha subunit, C-terminal. | CTP synthase; Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates. | 0.926 |
| EHA64096.1 | EHA59278.1 | Syn8016DRAFT_1138 | Syn8016DRAFT_2648 | GatB region; PFAM: Glutamyl-tRNA(Gln) amidotransferase, subunit B/E, N-terminal; KEGG: pmf:P9303_28281 aspartyl/glutamyl-tRNA amidotransferase subunit B. | KEGG: pmt:PMT1777 ferredoxin-dependent glutamate synthase; PFAM: Glutamate synthase, central-C; Glutamine amidotransferase, class-II; Glutamate synthase, central-N; Glutamate synthase, alpha subunit, C-terminal. | 0.904 |
| EHA64096.1 | aspS | Syn8016DRAFT_1138 | Syn8016DRAFT_2072 | GatB region; PFAM: Glutamyl-tRNA(Gln) amidotransferase, subunit B/E, N-terminal; KEGG: pmf:P9303_28281 aspartyl/glutamyl-tRNA amidotransferase subunit B. | 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); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 0.905 |
| EHA64096.1 | gatA | Syn8016DRAFT_1138 | Syn8016DRAFT_0745 | GatB region; PFAM: Glutamyl-tRNA(Gln) amidotransferase, subunit B/E, N-terminal; KEGG: pmf:P9303_28281 aspartyl/glutamyl-tRNA amidotransferase subunit B. | 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). | 0.994 |
| EHA64096.1 | gatC | Syn8016DRAFT_1138 | Syn8016DRAFT_1517 | GatB region; PFAM: Glutamyl-tRNA(Gln) amidotransferase, subunit B/E, N-terminal; KEGG: pmf:P9303_28281 aspartyl/glutamyl-tRNA amidotransferase subunit B. | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C; 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. | 0.987 |
| EHA64096.1 | guaA | Syn8016DRAFT_1138 | Syn8016DRAFT_2868 | GatB region; PFAM: Glutamyl-tRNA(Gln) amidotransferase, subunit B/E, N-terminal; KEGG: pmf:P9303_28281 aspartyl/glutamyl-tRNA amidotransferase subunit B. | GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP. | 0.985 |
| EHA64096.1 | pheT | Syn8016DRAFT_1138 | Syn8016DRAFT_0416 | GatB region; PFAM: Glutamyl-tRNA(Gln) amidotransferase, subunit B/E, N-terminal; KEGG: pmf:P9303_28281 aspartyl/glutamyl-tRNA amidotransferase subunit B. | TIGRFAM: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; KEGG: pmf:P9303_14801 phenylalanyl-tRNA synthetase subunit beta; HAMAP: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial. | 0.647 |
| EHA64096.1 | pyrG | Syn8016DRAFT_1138 | Syn8016DRAFT_2076 | GatB region; PFAM: Glutamyl-tRNA(Gln) amidotransferase, subunit B/E, N-terminal; KEGG: pmf:P9303_28281 aspartyl/glutamyl-tRNA amidotransferase subunit B. | CTP synthase; Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates. | 0.743 |
| aspS | EHA59278.1 | Syn8016DRAFT_2072 | Syn8016DRAFT_2648 | 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); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | KEGG: pmt:PMT1777 ferredoxin-dependent glutamate synthase; PFAM: Glutamate synthase, central-C; Glutamine amidotransferase, class-II; Glutamate synthase, central-N; Glutamate synthase, alpha subunit, C-terminal. | 0.877 |
| aspS | EHA64096.1 | Syn8016DRAFT_2072 | Syn8016DRAFT_1138 | 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); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | GatB region; PFAM: Glutamyl-tRNA(Gln) amidotransferase, subunit B/E, N-terminal; KEGG: pmf:P9303_28281 aspartyl/glutamyl-tRNA amidotransferase subunit B. | 0.905 |
| aspS | gatA | Syn8016DRAFT_2072 | Syn8016DRAFT_0745 | 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); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 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). | 0.915 |
| aspS | gatB | Syn8016DRAFT_2072 | Syn8016DRAFT_1973 | 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); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 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. | 0.986 |
| aspS | gatC | Syn8016DRAFT_2072 | Syn8016DRAFT_1517 | 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); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C; 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. | 0.955 |