| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ANK61569.1 | ANK61570.1 | AYR53_01605 | AYR53_01610 | Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| ANK61569.1 | ANK62058.1 | AYR53_01605 | AYR53_04320 | Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Glyoxalase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.800 |
| ANK61569.1 | ANK62059.1 | AYR53_01605 | AYR53_04325 | Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Glyoxal reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.800 |
| ANK61569.1 | ilvA | AYR53_01605 | AYR53_01690 | Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Threonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. | 0.917 |
| ANK61569.1 | trpA | AYR53_01605 | AYR53_01335 | Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Tryptophan synthase subunit alpha; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.930 |
| ANK61570.1 | ANK61569.1 | AYR53_01610 | AYR53_01605 | Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.999 |
| ANK61570.1 | ANK62058.1 | AYR53_01610 | AYR53_04320 | Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Glyoxalase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.800 |
| ANK61570.1 | ANK62059.1 | AYR53_01610 | AYR53_04325 | Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Glyoxal reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.800 |
| ANK61570.1 | ilvA | AYR53_01610 | AYR53_01690 | Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Threonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. | 0.935 |
| ANK61570.1 | trpA | AYR53_01610 | AYR53_01335 | Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Tryptophan synthase subunit alpha; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.929 |
| ANK62058.1 | ANK61569.1 | AYR53_04320 | AYR53_01605 | Glyoxalase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.800 |
| ANK62058.1 | ANK61570.1 | AYR53_04320 | AYR53_01610 | Glyoxalase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.800 |
| ANK62058.1 | ANK62059.1 | AYR53_04320 | AYR53_04325 | Glyoxalase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Glyoxal reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.955 |
| ANK62058.1 | ilvA | AYR53_04320 | AYR53_01690 | Glyoxalase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Threonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. | 0.806 |
| ANK62058.1 | trpA | AYR53_04320 | AYR53_01335 | Glyoxalase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Tryptophan synthase subunit alpha; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.800 |
| ANK62059.1 | ANK61569.1 | AYR53_04325 | AYR53_01605 | Glyoxal reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.800 |
| ANK62059.1 | ANK61570.1 | AYR53_04325 | AYR53_01610 | Glyoxal reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.800 |
| ANK62059.1 | ANK62058.1 | AYR53_04325 | AYR53_04320 | Glyoxal reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Glyoxalase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.955 |
| ANK62059.1 | ANK62060.1 | AYR53_04325 | AYR53_04330 | Glyoxal reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.518 |
| ANK62059.1 | ilvA | AYR53_04325 | AYR53_01690 | Glyoxal reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Threonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. | 0.804 |