| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| alaS | aspS | ATE51_03190 | ATE51_02312 | Alanine--tRNA ligase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | Aspartate--tRNA ligase; 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. | 0.920 |
| alaS | glyQ | ATE51_03190 | ATE51_02214 | Alanine--tRNA ligase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | Glycine--tRNA ligase alpha subunit. | 0.663 |
| alaS | hisS | ATE51_03190 | ATE51_02118 | Alanine--tRNA ligase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | Histidine--tRNA ligase. | 0.709 |
| alaS | valS | ATE51_03190 | ATE51_02098 | Alanine--tRNA ligase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | Valine--tRNA ligase; 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. | 0.835 |
| aspS | alaS | ATE51_02312 | ATE51_03190 | Aspartate--tRNA ligase; 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. | Alanine--tRNA ligase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | 0.920 |
| aspS | fmt | ATE51_02312 | ATE51_04268 | Aspartate--tRNA ligase; 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. | 0.497 |
| aspS | glyQ | ATE51_02312 | ATE51_02214 | Aspartate--tRNA ligase; 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. | Glycine--tRNA ligase alpha subunit. | 0.561 |
| aspS | hisS | ATE51_02312 | ATE51_02118 | Aspartate--tRNA ligase; 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. | Histidine--tRNA ligase. | 0.926 |
| aspS | valS | ATE51_02312 | ATE51_02098 | Aspartate--tRNA ligase; 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. | Valine--tRNA ligase; 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. | 0.848 |
| coaD | cysE | ATE51_02114 | ATE51_02122 | Phosphopantetheine adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Belongs to the bacterial CoaD family. | Serine acetyltransferase. | 0.800 |
| coaD | hisS | ATE51_02114 | ATE51_02118 | Phosphopantetheine adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Belongs to the bacterial CoaD family. | Histidine--tRNA ligase. | 0.831 |
| coaD | speA | ATE51_02114 | ATE51_02120 | Phosphopantetheine adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Belongs to the bacterial CoaD family. | Biosynthetic arginine decarboxylase; Catalyzes the biosynthesis of agmatine from arginine. Belongs to the Orn/Lys/Arg decarboxylase class-II family. SpeA subfamily. | 0.802 |
| coaD | tmk_1 | ATE51_02114 | ATE51_02116 | Phosphopantetheine adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Belongs to the bacterial CoaD family. | Thymidylate kinase; Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis; Belongs to the thymidylate kinase family. | 0.815 |
| cysE | coaD | ATE51_02122 | ATE51_02114 | Serine acetyltransferase. | Phosphopantetheine adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Belongs to the bacterial CoaD family. | 0.800 |
| cysE | hisS | ATE51_02122 | ATE51_02118 | Serine acetyltransferase. | Histidine--tRNA ligase. | 0.803 |
| cysE | speA | ATE51_02122 | ATE51_02120 | Serine acetyltransferase. | Biosynthetic arginine decarboxylase; Catalyzes the biosynthesis of agmatine from arginine. Belongs to the Orn/Lys/Arg decarboxylase class-II family. SpeA subfamily. | 0.800 |
| cysE | tmk_1 | ATE51_02122 | ATE51_02116 | Serine acetyltransferase. | Thymidylate kinase; Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis; Belongs to the thymidylate kinase family. | 0.814 |
| fmt | aspS | ATE51_04268 | ATE51_02312 | 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. | Aspartate--tRNA ligase; 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. | 0.497 |
| fmt | hisS | ATE51_04268 | ATE51_02118 | 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. | Histidine--tRNA ligase. | 0.814 |
| glyQ | alaS | ATE51_02214 | ATE51_03190 | Glycine--tRNA ligase alpha subunit. | Alanine--tRNA ligase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | 0.663 |