| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ABD29509.1 | ABD29583.1 | SAOUHSC_00341 | SAOUHSC_00422 | Conserved hypothetical protein. | Trans-sulfuration enzyme family protein, putative. | 0.897 |
| ABD29509.1 | ABD29684.1 | SAOUHSC_00341 | SAOUHSC_00536 | Conserved hypothetical protein. | Branched-chain amino acid aminotransferase. | 0.898 |
| ABD29509.1 | ABD30418.1 | SAOUHSC_00341 | SAOUHSC_01320 | Conserved hypothetical protein. | Homoserine dehydrogenase, putative. | 0.915 |
| ABD29509.1 | ABD30692.1 | SAOUHSC_00341 | SAOUHSC_01613 | Conserved hypothetical protein. | 2-oxoisovalerate dehydrogenase, E1 component, alpha subunit, putative. | 0.886 |
| ABD29509.1 | ilvA | SAOUHSC_00341 | SAOUHSC_02289 | Conserved hypothetical protein. | Thereonine dehydratase, putative; 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 (By similarity). | 0.889 |
| ABD29509.1 | tdcB | SAOUHSC_00341 | SAOUHSC_01451 | Conserved hypothetical protein. | 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 (By similarity). Belongs to the serine/thre [...] | 0.889 |
| ABD29509.1 | thrB | SAOUHSC_00341 | SAOUHSC_01322 | Conserved hypothetical protein. | Homoserine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. | 0.898 |
| ABD29583.1 | ABD29509.1 | SAOUHSC_00422 | SAOUHSC_00341 | Trans-sulfuration enzyme family protein, putative. | Conserved hypothetical protein. | 0.897 |
| ABD29583.1 | ABD29684.1 | SAOUHSC_00422 | SAOUHSC_00536 | Trans-sulfuration enzyme family protein, putative. | Branched-chain amino acid aminotransferase. | 0.898 |
| ABD29583.1 | ABD30418.1 | SAOUHSC_00422 | SAOUHSC_01320 | Trans-sulfuration enzyme family protein, putative. | Homoserine dehydrogenase, putative. | 0.915 |
| ABD29583.1 | ABD30692.1 | SAOUHSC_00422 | SAOUHSC_01613 | Trans-sulfuration enzyme family protein, putative. | 2-oxoisovalerate dehydrogenase, E1 component, alpha subunit, putative. | 0.886 |
| ABD29583.1 | ilvA | SAOUHSC_00422 | SAOUHSC_02289 | Trans-sulfuration enzyme family protein, putative. | Thereonine dehydratase, putative; 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 (By similarity). | 0.889 |
| ABD29583.1 | tdcB | SAOUHSC_00422 | SAOUHSC_01451 | Trans-sulfuration enzyme family protein, putative. | 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 (By similarity). Belongs to the serine/thre [...] | 0.889 |
| ABD29583.1 | thrB | SAOUHSC_00422 | SAOUHSC_01322 | Trans-sulfuration enzyme family protein, putative. | Homoserine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. | 0.898 |
| ABD29684.1 | ABD29509.1 | SAOUHSC_00536 | SAOUHSC_00341 | Branched-chain amino acid aminotransferase. | Conserved hypothetical protein. | 0.898 |
| ABD29684.1 | ABD29583.1 | SAOUHSC_00536 | SAOUHSC_00422 | Branched-chain amino acid aminotransferase. | Trans-sulfuration enzyme family protein, putative. | 0.898 |
| ABD29684.1 | ABD30418.1 | SAOUHSC_00536 | SAOUHSC_01320 | Branched-chain amino acid aminotransferase. | Homoserine dehydrogenase, putative. | 0.929 |
| ABD29684.1 | ABD30691.1 | SAOUHSC_00536 | SAOUHSC_01612 | Branched-chain amino acid aminotransferase. | 2-oxoisovalerate dehydrogenase, E1 component, beta subunit, putative. | 0.972 |
| ABD29684.1 | ABD30692.1 | SAOUHSC_00536 | SAOUHSC_01613 | Branched-chain amino acid aminotransferase. | 2-oxoisovalerate dehydrogenase, E1 component, alpha subunit, putative. | 0.968 |
| ABD29684.1 | ilvA | SAOUHSC_00536 | SAOUHSC_02289 | Branched-chain amino acid aminotransferase. | Thereonine dehydratase, putative; 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 (By similarity). | 0.915 |