| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ADU47988.1 | ADU48157.1 | Intca_1473 | Intca_1644 | Amidase; COGs: COG0154 Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit and related amidase; InterPro IPR000120; KEGG: rsa:RSal33209_2315 amidase; PFAM: Amidase; SPTR: Amidase; PFAM: Amidase. | Glutamate synthase (NADH) large subunit; COGs: COG0069 Glutamate synthase domain 2; InterProIPR017932: IPR000583: IPR006982: IPR002932: IPR 002489; KEGG: kfl:Kfla_3074 glutamate synthase (ferredoxin); PFAM: ferredoxin-dependent glutamate synthase; glutamine amidotransferase class-II; glutamate synthase; glutamate synthase alpha subunit domain protein; PRIAM: Glutamate synthase (ferredoxin); SPTR: Putative glutamate synthase (NADPH) large subunit; PFAM: Conserved region in glutamate synthase; GXGXG motif; Glutamate synthase central domain; Glutamine amidotransferases class-II. | 0.483 |
| ADU47988.1 | aspS | Intca_1473 | Intca_0647 | Amidase; COGs: COG0154 Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit and related amidase; InterPro IPR000120; KEGG: rsa:RSal33209_2315 amidase; PFAM: Amidase; SPTR: Amidase; PFAM: Amidase. | 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 2 subfamily. | 0.955 |
| ADU47988.1 | aspS-2 | Intca_1473 | Intca_1578 | Amidase; COGs: COG0154 Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit and related amidase; InterPro IPR000120; KEGG: rsa:RSal33209_2315 amidase; PFAM: Amidase; SPTR: Amidase; PFAM: Amidase. | 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. | 0.579 |
| ADU47988.1 | carB | Intca_1473 | Intca_1604 | Amidase; COGs: COG0154 Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit and related amidase; InterPro IPR000120; KEGG: rsa:RSal33209_2315 amidase; PFAM: Amidase; SPTR: Amidase; PFAM: Amidase. | COGs: COG0458 Carbamoylphosphate synthase large subunit (split gene in MJ); InterProIPR011761: IPR005483: IPR005479: IPR005481: IPR 005480: IPR011607: IPR006275; KEGG: kse:Ksed_12690 carbamoyl-phosphate synthase large subunit; PFAM: Carbamoyl-phosphate synthase L chain ATP-binding; Carbamoyl-phosphate synthetase large chain domain protein; Carbamoyl-phosphate synthetase large chain oligomerisation; MGS domain protein; SPTR: Carbamoylphosphate synthetase large chain; TIGRFAM: carbamoyl-phosphate synthase, large subunit; PFAM: Carbamoyl-phosphate synthase L chain, ATP binding domain; MGS [...] | 0.410 |
| ADU47988.1 | gatA | Intca_1473 | Intca_2375 | Amidase; COGs: COG0154 Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit and related amidase; InterPro IPR000120; KEGG: rsa:RSal33209_2315 amidase; PFAM: Amidase; SPTR: Amidase; PFAM: Amidase. | aspartyl/glutamyl-tRNA(Asn/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). | 0.927 |
| ADU47988.1 | gatB | Intca_1473 | Intca_2374 | Amidase; COGs: COG0154 Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit and related amidase; InterPro IPR000120; KEGG: rsa:RSal33209_2315 amidase; PFAM: Amidase; SPTR: Amidase; PFAM: Amidase. | 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. | 0.998 |
| ADU47988.1 | gatC | Intca_1473 | Intca_2376 | Amidase; COGs: COG0154 Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit and related amidase; InterPro IPR000120; KEGG: rsa:RSal33209_2315 amidase; PFAM: Amidase; SPTR: Amidase; PFAM: Amidase. | 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. | 0.997 |
| ADU47988.1 | gltX | Intca_1473 | Intca_2337 | Amidase; COGs: COG0154 Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit and related amidase; InterPro IPR000120; KEGG: rsa:RSal33209_2315 amidase; PFAM: Amidase; SPTR: Amidase; PFAM: Amidase. | 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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | 0.868 |
| ADU47988.1 | guaA | Intca_1473 | Intca_1035 | Amidase; COGs: COG0154 Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit and related amidase; InterPro IPR000120; KEGG: rsa:RSal33209_2315 amidase; PFAM: Amidase; SPTR: Amidase; PFAM: Amidase. | GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP. | 0.551 |
| ADU47988.1 | ligA | Intca_1473 | Intca_2382 | Amidase; COGs: COG0154 Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit and related amidase; InterPro IPR000120; KEGG: rsa:RSal33209_2315 amidase; PFAM: Amidase; SPTR: Amidase; PFAM: Amidase. | DNA ligase, NAD-dependent; DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double- stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA; Belongs to the NAD-dependent DNA ligase family. LigA subfamily. | 0.446 |
| ADU48157.1 | ADU47988.1 | Intca_1644 | Intca_1473 | Glutamate synthase (NADH) large subunit; COGs: COG0069 Glutamate synthase domain 2; InterProIPR017932: IPR000583: IPR006982: IPR002932: IPR 002489; KEGG: kfl:Kfla_3074 glutamate synthase (ferredoxin); PFAM: ferredoxin-dependent glutamate synthase; glutamine amidotransferase class-II; glutamate synthase; glutamate synthase alpha subunit domain protein; PRIAM: Glutamate synthase (ferredoxin); SPTR: Putative glutamate synthase (NADPH) large subunit; PFAM: Conserved region in glutamate synthase; GXGXG motif; Glutamate synthase central domain; Glutamine amidotransferases class-II. | Amidase; COGs: COG0154 Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit and related amidase; InterPro IPR000120; KEGG: rsa:RSal33209_2315 amidase; PFAM: Amidase; SPTR: Amidase; PFAM: Amidase. | 0.483 |
| ADU48157.1 | carB | Intca_1644 | Intca_1604 | Glutamate synthase (NADH) large subunit; COGs: COG0069 Glutamate synthase domain 2; InterProIPR017932: IPR000583: IPR006982: IPR002932: IPR 002489; KEGG: kfl:Kfla_3074 glutamate synthase (ferredoxin); PFAM: ferredoxin-dependent glutamate synthase; glutamine amidotransferase class-II; glutamate synthase; glutamate synthase alpha subunit domain protein; PRIAM: Glutamate synthase (ferredoxin); SPTR: Putative glutamate synthase (NADPH) large subunit; PFAM: Conserved region in glutamate synthase; GXGXG motif; Glutamate synthase central domain; Glutamine amidotransferases class-II. | COGs: COG0458 Carbamoylphosphate synthase large subunit (split gene in MJ); InterProIPR011761: IPR005483: IPR005479: IPR005481: IPR 005480: IPR011607: IPR006275; KEGG: kse:Ksed_12690 carbamoyl-phosphate synthase large subunit; PFAM: Carbamoyl-phosphate synthase L chain ATP-binding; Carbamoyl-phosphate synthetase large chain domain protein; Carbamoyl-phosphate synthetase large chain oligomerisation; MGS domain protein; SPTR: Carbamoylphosphate synthetase large chain; TIGRFAM: carbamoyl-phosphate synthase, large subunit; PFAM: Carbamoyl-phosphate synthase L chain, ATP binding domain; MGS [...] | 0.987 |
| ADU48157.1 | gatA | Intca_1644 | Intca_2375 | Glutamate synthase (NADH) large subunit; COGs: COG0069 Glutamate synthase domain 2; InterProIPR017932: IPR000583: IPR006982: IPR002932: IPR 002489; KEGG: kfl:Kfla_3074 glutamate synthase (ferredoxin); PFAM: ferredoxin-dependent glutamate synthase; glutamine amidotransferase class-II; glutamate synthase; glutamate synthase alpha subunit domain protein; PRIAM: Glutamate synthase (ferredoxin); SPTR: Putative glutamate synthase (NADPH) large subunit; PFAM: Conserved region in glutamate synthase; GXGXG motif; Glutamate synthase central domain; Glutamine amidotransferases class-II. | aspartyl/glutamyl-tRNA(Asn/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). | 0.730 |
| ADU48157.1 | gatB | Intca_1644 | Intca_2374 | Glutamate synthase (NADH) large subunit; COGs: COG0069 Glutamate synthase domain 2; InterProIPR017932: IPR000583: IPR006982: IPR002932: IPR 002489; KEGG: kfl:Kfla_3074 glutamate synthase (ferredoxin); PFAM: ferredoxin-dependent glutamate synthase; glutamine amidotransferase class-II; glutamate synthase; glutamate synthase alpha subunit domain protein; PRIAM: Glutamate synthase (ferredoxin); SPTR: Putative glutamate synthase (NADPH) large subunit; PFAM: Conserved region in glutamate synthase; GXGXG motif; Glutamate synthase central domain; Glutamine amidotransferases 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. | 0.701 |
| ADU48157.1 | gatC | Intca_1644 | Intca_2376 | Glutamate synthase (NADH) large subunit; COGs: COG0069 Glutamate synthase domain 2; InterProIPR017932: IPR000583: IPR006982: IPR002932: IPR 002489; KEGG: kfl:Kfla_3074 glutamate synthase (ferredoxin); PFAM: ferredoxin-dependent glutamate synthase; glutamine amidotransferase class-II; glutamate synthase; glutamate synthase alpha subunit domain protein; PRIAM: Glutamate synthase (ferredoxin); SPTR: Putative glutamate synthase (NADPH) large subunit; PFAM: Conserved region in glutamate synthase; GXGXG motif; Glutamate synthase central domain; Glutamine amidotransferases class-II. | 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. | 0.711 |
| ADU48157.1 | gltX | Intca_1644 | Intca_2337 | Glutamate synthase (NADH) large subunit; COGs: COG0069 Glutamate synthase domain 2; InterProIPR017932: IPR000583: IPR006982: IPR002932: IPR 002489; KEGG: kfl:Kfla_3074 glutamate synthase (ferredoxin); PFAM: ferredoxin-dependent glutamate synthase; glutamine amidotransferase class-II; glutamate synthase; glutamate synthase alpha subunit domain protein; PRIAM: Glutamate synthase (ferredoxin); SPTR: Putative glutamate synthase (NADPH) large subunit; PFAM: Conserved region in glutamate synthase; GXGXG motif; Glutamate synthase central domain; Glutamine amidotransferases 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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | 0.942 |
| ADU48157.1 | guaA | Intca_1644 | Intca_1035 | Glutamate synthase (NADH) large subunit; COGs: COG0069 Glutamate synthase domain 2; InterProIPR017932: IPR000583: IPR006982: IPR002932: IPR 002489; KEGG: kfl:Kfla_3074 glutamate synthase (ferredoxin); PFAM: ferredoxin-dependent glutamate synthase; glutamine amidotransferase class-II; glutamate synthase; glutamate synthase alpha subunit domain protein; PRIAM: Glutamate synthase (ferredoxin); SPTR: Putative glutamate synthase (NADPH) large subunit; PFAM: Conserved region in glutamate synthase; GXGXG motif; Glutamate synthase central domain; Glutamine amidotransferases class-II. | GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP. | 0.891 |
| aspS | ADU47988.1 | Intca_0647 | Intca_1473 | 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 2 subfamily. | Amidase; COGs: COG0154 Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit and related amidase; InterPro IPR000120; KEGG: rsa:RSal33209_2315 amidase; PFAM: Amidase; SPTR: Amidase; PFAM: Amidase. | 0.955 |
| aspS | aspS-2 | Intca_0647 | Intca_1578 | 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 2 subfamily. | 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. | 0.939 |
| aspS | gatA | Intca_0647 | Intca_2375 | 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 2 subfamily. | aspartyl/glutamyl-tRNA(Asn/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). | 0.954 |