| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| BF49_2234 | BF49_3395 | BF49_2234 | BF49_3395 | COG1896 Predicted hydrolases of HD superfamily. | FIG00450379 hypothetical protein. | 0.704 |
| BF49_2234 | hisS | BF49_2234 | BF49_2991 | COG1896 Predicted hydrolases of HD superfamily. | HistidyltRNA synthetase EC 61121. | 0.707 |
| BF49_3395 | BF49_2234 | BF49_3395 | BF49_2234 | FIG00450379 hypothetical protein. | COG1896 Predicted hydrolases of HD superfamily. | 0.704 |
| BF49_3395 | hisG | BF49_3395 | BF49_3058 | FIG00450379 hypothetical protein. | ATP phosphoribosyltransferase EC 24217; Catalyzes the condensation of ATP and 5-phosphoribose 1- diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity. Belongs to the ATP phosphoribosyltransferase family. Long subfamily. | 0.485 |
| BF49_3395 | hisS | BF49_3395 | BF49_2991 | FIG00450379 hypothetical protein. | HistidyltRNA synthetase EC 61121. | 0.750 |
| alaS | aspS | BF49_5887 | BF49_0920 | AlanyltRNA synthetase EC 6117; 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. | AspartyltRNA synthetase EC 61112 AspartyltRNAAsn synthetase EC 61123; 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. | 0.866 |
| alaS | cysS | BF49_5887 | BF49_1262 | AlanyltRNA synthetase EC 6117; 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. | CysteinyltRNA synthetase EC 61116; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.736 |
| alaS | glyQ | BF49_5887 | BF49_2254 | AlanyltRNA synthetase EC 6117; 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. | GlycyltRNA synthetase alpha chain EC 61114. | 0.844 |
| alaS | hisS | BF49_5887 | BF49_2991 | AlanyltRNA synthetase EC 6117; 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. | HistidyltRNA synthetase EC 61121. | 0.837 |
| alaS | thrS | BF49_5887 | BF49_6108 | AlanyltRNA synthetase EC 6117; 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. | ThreonyltRNA synthetase EC 6113; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.928 |
| aspS | alaS | BF49_0920 | BF49_5887 | AspartyltRNA synthetase EC 61112 AspartyltRNAAsn synthetase EC 61123; 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. | AlanyltRNA synthetase EC 6117; 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. | 0.866 |
| aspS | cysS | BF49_0920 | BF49_1262 | AspartyltRNA synthetase EC 61112 AspartyltRNAAsn synthetase EC 61123; 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. | CysteinyltRNA synthetase EC 61116; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.589 |
| aspS | glyQ | BF49_0920 | BF49_2254 | AspartyltRNA synthetase EC 61112 AspartyltRNAAsn synthetase EC 61123; 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. | GlycyltRNA synthetase alpha chain EC 61114. | 0.756 |
| aspS | hisS | BF49_0920 | BF49_2991 | AspartyltRNA synthetase EC 61112 AspartyltRNAAsn synthetase EC 61123; 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. | HistidyltRNA synthetase EC 61121. | 0.898 |
| aspS | thrS | BF49_0920 | BF49_6108 | AspartyltRNA synthetase EC 61112 AspartyltRNAAsn synthetase EC 61123; 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. | ThreonyltRNA synthetase EC 6113; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.802 |
| cysS | alaS | BF49_1262 | BF49_5887 | CysteinyltRNA synthetase EC 61116; Belongs to the class-I aminoacyl-tRNA synthetase family. | AlanyltRNA synthetase EC 6117; 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. | 0.736 |
| cysS | aspS | BF49_1262 | BF49_0920 | CysteinyltRNA synthetase EC 61116; Belongs to the class-I aminoacyl-tRNA synthetase family. | AspartyltRNA synthetase EC 61112 AspartyltRNAAsn synthetase EC 61123; 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. | 0.589 |
| cysS | hisS | BF49_1262 | BF49_2991 | CysteinyltRNA synthetase EC 61116; Belongs to the class-I aminoacyl-tRNA synthetase family. | HistidyltRNA synthetase EC 61121. | 0.816 |
| cysS | thrS | BF49_1262 | BF49_6108 | CysteinyltRNA synthetase EC 61116; Belongs to the class-I aminoacyl-tRNA synthetase family. | ThreonyltRNA synthetase EC 6113; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.839 |
| ftsA | glyQ | BF49_5060 | BF49_2254 | Cell division protein FtsA; Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring. Belongs to the FtsA/MreB family. | GlycyltRNA synthetase alpha chain EC 61114. | 0.591 |