| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| accB | glyQ | PANA_3571 | PANA_0100 | AccB; This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. | GlyQ; Glycyl-tRNA synthetase alpha chain; Similar to Dickeya zeae Ech1591, glycyl-tRNA synthetase, alpha subunit (NCBI: YP_003002414.1); COG: Translation, ribosomal structure and biogenesis; Subcellular localization as predicted by Psort 2.0: Cytoplasmic. | 0.591 |
| accB | guaA-2 | PANA_3571 | PANA_2848 | AccB; This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. | GuaA; Catalyzes the synthesis of GMP from XMP. | 0.522 |
| alaS | aspS | PANA_3032 | PANA_2206 | AlaS; 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; Belongs to the class-II aminoacyl-tRNA synthetase family. | AspS; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 0.830 |
| alaS | glyQ | PANA_3032 | PANA_0100 | AlaS; 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; Belongs to the class-II aminoacyl-tRNA synthetase family. | GlyQ; Glycyl-tRNA synthetase alpha chain; Similar to Dickeya zeae Ech1591, glycyl-tRNA synthetase, alpha subunit (NCBI: YP_003002414.1); COG: Translation, ribosomal structure and biogenesis; Subcellular localization as predicted by Psort 2.0: Cytoplasmic. | 0.698 |
| alaS | glyS | PANA_3032 | PANA_0101 | AlaS; 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; Belongs to the class-II aminoacyl-tRNA synthetase family. | GlyS; Glycyl-tRNA synthetase beta chain; Similar to Pantoea sp. At-9b, glycyl-tRNA synthetase, beta subunit (NCBI: ZP_05729699.1); COG: Translation, ribosomal structure and biogenesis; Subcellular localization as predicted by Psort 2.0: Cytoplasmic. | 0.627 |
| alaS | guaA-2 | PANA_3032 | PANA_2848 | AlaS; 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; Belongs to the class-II aminoacyl-tRNA synthetase family. | GuaA; Catalyzes the synthesis of GMP from XMP. | 0.633 |
| alaS | hisS | PANA_3032 | PANA_2857 | AlaS; 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; Belongs to the class-II aminoacyl-tRNA synthetase family. | HisS; Histidyl-tRNA synthetase; Similar to Pantoea sp. At-9b, histidyl-tRNA synthetase (NCBI: ZP_05727756.1); COG: Translation, ribosomal structure and biogenesis; Subcellular localization as predicted by Psort 2.0: Cytoplasmic. | 0.713 |
| alaS | ileS | PANA_3032 | PANA_0669 | AlaS; 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; Belongs to the class-II aminoacyl-tRNA synthetase family. | IleS; 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. | 0.786 |
| alaS | metG | PANA_3032 | PANA_2533 | AlaS; 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; Belongs to the class-II aminoacyl-tRNA synthetase family. | MetG; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.856 |
| alaS | pheS | PANA_3032 | PANA_1698 | AlaS; 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; Belongs to the class-II aminoacyl-tRNA synthetase family. | PheS; Phenylalanyl-tRNA synthetase alpha chain; Similar to Enterobacter cancerogenus ATCC 35316, phenylalanyl-tRNA synthetase subunit alpha (NCBI: ZP_05967377.1); COG: Translation, ribosomal structure and biogenesis; Subcellular localization as predicted by Psort 2.0: Cytoplasmic. | 0.513 |
| alaS | valS | PANA_3032 | PANA_0494 | AlaS; 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; Belongs to the class-II aminoacyl-tRNA synthetase family. | ValS; 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. | 0.899 |
| aspS | alaS | PANA_2206 | PANA_3032 | AspS; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | AlaS; 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; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.830 |
| aspS | glyQ | PANA_2206 | PANA_0100 | AspS; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | GlyQ; Glycyl-tRNA synthetase alpha chain; Similar to Dickeya zeae Ech1591, glycyl-tRNA synthetase, alpha subunit (NCBI: YP_003002414.1); COG: Translation, ribosomal structure and biogenesis; Subcellular localization as predicted by Psort 2.0: Cytoplasmic. | 0.645 |
| aspS | glyS | PANA_2206 | PANA_0101 | AspS; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | GlyS; Glycyl-tRNA synthetase beta chain; Similar to Pantoea sp. At-9b, glycyl-tRNA synthetase, beta subunit (NCBI: ZP_05729699.1); COG: Translation, ribosomal structure and biogenesis; Subcellular localization as predicted by Psort 2.0: Cytoplasmic. | 0.699 |
| aspS | guaA-2 | PANA_2206 | PANA_2848 | AspS; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | GuaA; Catalyzes the synthesis of GMP from XMP. | 0.843 |
| aspS | hisS | PANA_2206 | PANA_2857 | AspS; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | HisS; Histidyl-tRNA synthetase; Similar to Pantoea sp. At-9b, histidyl-tRNA synthetase (NCBI: ZP_05727756.1); COG: Translation, ribosomal structure and biogenesis; Subcellular localization as predicted by Psort 2.0: Cytoplasmic. | 0.897 |
| aspS | ileS | PANA_2206 | PANA_0669 | AspS; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | IleS; 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. | 0.681 |
| aspS | metG | PANA_2206 | PANA_2533 | AspS; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | MetG; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.757 |
| aspS | pheS | PANA_2206 | PANA_1698 | AspS; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | PheS; Phenylalanyl-tRNA synthetase alpha chain; Similar to Enterobacter cancerogenus ATCC 35316, phenylalanyl-tRNA synthetase subunit alpha (NCBI: ZP_05967377.1); COG: Translation, ribosomal structure and biogenesis; Subcellular localization as predicted by Psort 2.0: Cytoplasmic. | 0.668 |
| aspS | valS | PANA_2206 | PANA_0494 | AspS; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | ValS; 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. | 0.860 |