node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Rmag_0394 | Rmag_0395 | Rmag_0394 | Rmag_0395 | PFAM: protein of unknown function DUF28; KEGG: ilo:IL1088 uncharacterized conserved enzyme. | Quinolinate synthetase A; Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate. | 0.682 |
Rmag_0394 | Rmag_0397 | Rmag_0394 | Rmag_0397 | PFAM: protein of unknown function DUF28; KEGG: ilo:IL1088 uncharacterized conserved enzyme. | PFAM: protein of unknown function DUF502; KEGG: mfa:Mfla_2385 protein of unknown function DUF502. | 0.679 |
Rmag_0394 | aspS | Rmag_0394 | Rmag_0396 | PFAM: protein of unknown function DUF28; KEGG: ilo:IL1088 uncharacterized conserved enzyme. | 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. | 0.793 |
Rmag_0395 | Rmag_0394 | Rmag_0395 | Rmag_0394 | Quinolinate synthetase A; Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate. | PFAM: protein of unknown function DUF28; KEGG: ilo:IL1088 uncharacterized conserved enzyme. | 0.682 |
Rmag_0395 | Rmag_0397 | Rmag_0395 | Rmag_0397 | Quinolinate synthetase A; Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate. | PFAM: protein of unknown function DUF502; KEGG: mfa:Mfla_2385 protein of unknown function DUF502. | 0.793 |
Rmag_0395 | aspS | Rmag_0395 | Rmag_0396 | Quinolinate synthetase A; Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate. | 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. | 0.793 |
Rmag_0395 | valS | Rmag_0395 | Rmag_0464 | Quinolinate synthetase A; Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate. | 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 1 subfamily. | 0.675 |
Rmag_0397 | Rmag_0394 | Rmag_0397 | Rmag_0394 | PFAM: protein of unknown function DUF502; KEGG: mfa:Mfla_2385 protein of unknown function DUF502. | PFAM: protein of unknown function DUF28; KEGG: ilo:IL1088 uncharacterized conserved enzyme. | 0.679 |
Rmag_0397 | Rmag_0395 | Rmag_0397 | Rmag_0395 | PFAM: protein of unknown function DUF502; KEGG: mfa:Mfla_2385 protein of unknown function DUF502. | Quinolinate synthetase A; Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate. | 0.793 |
Rmag_0397 | aspS | Rmag_0397 | Rmag_0396 | PFAM: protein of unknown function DUF502; KEGG: mfa:Mfla_2385 protein of unknown function DUF502. | 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. | 0.793 |
aspS | Rmag_0394 | Rmag_0396 | Rmag_0394 | 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. | PFAM: protein of unknown function DUF28; KEGG: ilo:IL1088 uncharacterized conserved enzyme. | 0.793 |
aspS | Rmag_0395 | Rmag_0396 | Rmag_0395 | 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. | Quinolinate synthetase A; Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate. | 0.793 |
aspS | Rmag_0397 | Rmag_0396 | Rmag_0397 | 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. | PFAM: protein of unknown function DUF502; KEGG: mfa:Mfla_2385 protein of unknown function DUF502. | 0.793 |
aspS | gatB | Rmag_0396 | Rmag_0345 | 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. | 0.972 |
aspS | gatC | Rmag_0396 | Rmag_0343 | 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. | 0.871 |
aspS | guaA | Rmag_0396 | Rmag_0914 | 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. | GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP. | 0.818 |
aspS | hisS | Rmag_0396 | Rmag_0671 | 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: ppu:PP0854 histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; PFAM: tRNA synthetase, class II (G, H, P and S); Anticodon-binding domain protein. | 0.890 |
aspS | ileS | Rmag_0396 | Rmag_0340 | 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. | Isoleucyl-tRNA synthetase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily. | 0.703 |
aspS | pheT | Rmag_0396 | Rmag_0642 | 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. | TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; KEGG: sde:Sde_1582 phenylalanine--tRNA ligase. | 0.696 |
aspS | valS | Rmag_0396 | Rmag_0464 | 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. | 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 1 subfamily. | 0.833 |