| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CCH88760.1 | CCH88762.1 | MODMU_3347 | MODMU_3349 | Putative aryl-alcohol dehydrogenase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Putative enzymemetal binding hydrolase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.777 |
| CCH88760.1 | aspS | MODMU_3347 | MODMU_3346 | Putative aryl-alcohol dehydrogenase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative 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. | 0.631 |
| CCH88760.1 | hisS | MODMU_3347 | MODMU_3348 | Putative aryl-alcohol dehydrogenase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Histidyl-tRNA synthetase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.778 |
| CCH88762.1 | CCH88760.1 | MODMU_3349 | MODMU_3347 | Putative enzymemetal binding hydrolase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Putative aryl-alcohol dehydrogenase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.777 |
| CCH88762.1 | aspS | MODMU_3349 | MODMU_3346 | Putative enzymemetal binding hydrolase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative 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. | 0.735 |
| CCH88762.1 | hisS | MODMU_3349 | MODMU_3348 | Putative enzymemetal binding hydrolase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Histidyl-tRNA synthetase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.837 |
| aspS | CCH88760.1 | MODMU_3346 | MODMU_3347 | 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. | Putative aryl-alcohol dehydrogenase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.631 |
| aspS | CCH88762.1 | MODMU_3346 | MODMU_3349 | 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. | Putative enzymemetal binding hydrolase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.735 |
| aspS | fmt | MODMU_3346 | MODMU_3306 | 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. | 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. | 0.527 |
| aspS | guaA | MODMU_3346 | MODMU_4851 | 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] (Glutamine amidotransferase) (GMP synthetase); Catalyzes the synthesis of GMP from XMP. | 0.886 |
| aspS | hisS | MODMU_3346 | MODMU_3348 | 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. | Histidyl-tRNA synthetase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.970 |
| aspS | pheT | MODMU_3346 | MODMU_3220 | 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. | Phenylalanyl-tRNA synthetase beta chain; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.908 |
| aspS | thrS | MODMU_3346 | MODMU_3368 | 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. | Threonyl-tRNA synthetase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.738 |
| fmt | aspS | MODMU_3306 | MODMU_3346 | 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. | 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. | 0.527 |
| fmt | guaA | MODMU_3306 | MODMU_4851 | 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. | GMP synthase [glutamine-hydrolyzing] (Glutamine amidotransferase) (GMP synthetase); Catalyzes the synthesis of GMP from XMP. | 0.622 |
| fmt | hisS | MODMU_3306 | MODMU_3348 | 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. | Histidyl-tRNA synthetase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.808 |
| fmt | ispG | MODMU_3306 | MODMU_4385 | 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. | 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase; Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME- 2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. Belongs to the IspG family. | 0.466 |
| fmt | pheT | MODMU_3306 | MODMU_3220 | 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. | Phenylalanyl-tRNA synthetase beta chain; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.911 |
| guaA | aspS | MODMU_4851 | MODMU_3346 | GMP synthase [glutamine-hydrolyzing] (Glutamine amidotransferase) (GMP synthetase); Catalyzes the synthesis of GMP from XMP. | 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. | 0.886 |
| guaA | fmt | MODMU_4851 | MODMU_3306 | GMP synthase [glutamine-hydrolyzing] (Glutamine amidotransferase) (GMP synthetase); Catalyzes the synthesis of GMP from XMP. | 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. | 0.622 |