| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Noca_2631 | Noca_3943 | Noca_2631 | Noca_3943 | Methionine synthase (B12-dependent); Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate. | Cystathionine gamma-synthase; PFAM: Cys/Met metabolism pyridoxal-phosphate-dependent enzymes; KEGG: sco:SCO1294 cystathionine gamma-synthase. | 0.978 |
| Noca_2631 | fmt | Noca_2631 | Noca_2442 | Methionine synthase (B12-dependent); Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate. | methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | 0.926 |
| Noca_2631 | gltX | Noca_2631 | Noca_3336 | Methionine synthase (B12-dependent); Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate. | 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). | 0.573 |
| Noca_2631 | leuS | Noca_2631 | Noca_1884 | Methionine synthase (B12-dependent); Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate. | TIGRFAM: leucyl-tRNA synthetase; KEGG: pac:PPA0893 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.605 |
| Noca_2631 | metG | Noca_2631 | Noca_1386 | Methionine synthase (B12-dependent); Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate. | methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.922 |
| Noca_3943 | Noca_2631 | Noca_3943 | Noca_2631 | Cystathionine gamma-synthase; PFAM: Cys/Met metabolism pyridoxal-phosphate-dependent enzymes; KEGG: sco:SCO1294 cystathionine gamma-synthase. | Methionine synthase (B12-dependent); Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate. | 0.978 |
| Noca_3943 | metG | Noca_3943 | Noca_1386 | Cystathionine gamma-synthase; PFAM: Cys/Met metabolism pyridoxal-phosphate-dependent enzymes; KEGG: sco:SCO1294 cystathionine gamma-synthase. | methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.913 |
| argS | aspS | Noca_1742 | Noca_1189 | KEGG: fal:FRAAL5953 arginyl-tRNA synthetase (arginine--tRNA ligase); TIGRFAM: arginyl-tRNA synthetase. | 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. | 0.829 |
| argS | gltX | Noca_1742 | Noca_3336 | KEGG: fal:FRAAL5953 arginyl-tRNA synthetase (arginine--tRNA ligase); TIGRFAM: arginyl-tRNA synthetase. | 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). | 0.976 |
| argS | ileS | Noca_1742 | Noca_1198 | KEGG: fal:FRAAL5953 arginyl-tRNA synthetase (arginine--tRNA ligase); TIGRFAM: arginyl-tRNA synthetase. | 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 2 subfamily. | 0.978 |
| argS | leuS | Noca_1742 | Noca_1884 | KEGG: fal:FRAAL5953 arginyl-tRNA synthetase (arginine--tRNA ligase); TIGRFAM: arginyl-tRNA synthetase. | TIGRFAM: leucyl-tRNA synthetase; KEGG: pac:PPA0893 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.942 |
| argS | metG | Noca_1742 | Noca_1386 | KEGG: fal:FRAAL5953 arginyl-tRNA synthetase (arginine--tRNA ligase); TIGRFAM: arginyl-tRNA synthetase. | methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.935 |
| argS | pheT | Noca_1742 | Noca_2466 | KEGG: fal:FRAAL5953 arginyl-tRNA synthetase (arginine--tRNA ligase); TIGRFAM: arginyl-tRNA synthetase. | TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; KEGG: sma:SAV6743 putative phenylalanyl-tRNA synthetase beta subunit; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.948 |
| argS | proS | Noca_1742 | Noca_3197 | KEGG: fal:FRAAL5953 arginyl-tRNA synthetase (arginine--tRNA ligase); TIGRFAM: arginyl-tRNA synthetase. | prolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...] | 0.955 |
| aspS | argS | Noca_1189 | Noca_1742 | 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. | KEGG: fal:FRAAL5953 arginyl-tRNA synthetase (arginine--tRNA ligase); TIGRFAM: arginyl-tRNA synthetase. | 0.829 |
| aspS | gltX | Noca_1189 | Noca_3336 | 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. | 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). | 0.819 |
| aspS | ileS | Noca_1189 | Noca_1198 | 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. | 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 2 subfamily. | 0.912 |
| aspS | leuS | Noca_1189 | Noca_1884 | 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. | TIGRFAM: leucyl-tRNA synthetase; KEGG: pac:PPA0893 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.830 |
| aspS | metG | Noca_1189 | Noca_1386 | 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. | methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.909 |
| aspS | pheT | Noca_1189 | Noca_2466 | 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. | TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; KEGG: sma:SAV6743 putative phenylalanyl-tRNA synthetase beta subunit; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.864 |