| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CED71596.1 | gly | AWOD_I_1522 | AWOD_II_0553 | Putative threonine synthase. | L-allo-threonine aldolase. | 0.933 |
| CED71596.1 | ilvA | AWOD_I_1522 | AWOD_I_2625 | Putative threonine synthase. | 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. | 0.952 |
| CED71596.1 | lysC-2 | AWOD_I_1522 | AWOD_I_2335 | Putative threonine synthase. | Aspartokinase; Belongs to the aspartokinase family. | 0.591 |
| CED71596.1 | metL | AWOD_I_1522 | AWOD_I_0336 | Putative threonine synthase. | Bifunctional aspartokinase/homoserine dehydrogenase II; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.962 |
| CED71596.1 | pdxA | AWOD_I_1522 | AWOD_I_2392 | Putative threonine synthase. | 4-hydroxythreonine-4-phosphate dehydrogenase; Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L- threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP). | 0.903 |
| CED71596.1 | serC | AWOD_I_1522 | AWOD_I_0881 | Putative threonine synthase. | Phosphoserine aminotransferase; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily. | 0.939 |
| CED71596.1 | tdh | AWOD_I_1522 | AWOD_II_0792 | Putative threonine synthase. | L-threonine 3-dehydrogenase; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate; Belongs to the zinc-containing alcohol dehydrogenase family. | 0.904 |
| CED71596.1 | thrA | AWOD_I_1522 | AWOD_I_2198 | Putative threonine synthase. | Bifunctional aspartokinase/homoserine dehydrogenase I; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.962 |
| CED71596.1 | thrB | AWOD_I_1522 | AWOD_I_2197 | Putative threonine synthase. | Homoserine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. | 0.990 |
| CED71596.1 | thrC | AWOD_I_1522 | AWOD_I_2196 | Putative threonine synthase. | Threonine synthase. | 0.900 |
| gly | CED71596.1 | AWOD_II_0553 | AWOD_I_1522 | L-allo-threonine aldolase. | Putative threonine synthase. | 0.933 |
| gly | ilvA | AWOD_II_0553 | AWOD_I_2625 | L-allo-threonine aldolase. | 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. | 0.929 |
| gly | tdh | AWOD_II_0553 | AWOD_II_0792 | L-allo-threonine aldolase. | L-threonine 3-dehydrogenase; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate; Belongs to the zinc-containing alcohol dehydrogenase family. | 0.907 |
| gly | thrC | AWOD_II_0553 | AWOD_I_2196 | L-allo-threonine aldolase. | Threonine synthase. | 0.922 |
| ilvA | CED71596.1 | AWOD_I_2625 | AWOD_I_1522 | 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. | Putative threonine synthase. | 0.952 |
| ilvA | gly | AWOD_I_2625 | AWOD_II_0553 | 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. | L-allo-threonine aldolase. | 0.929 |
| ilvA | metL | AWOD_I_2625 | AWOD_I_0336 | 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. | Bifunctional aspartokinase/homoserine dehydrogenase II; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.669 |
| ilvA | tdh | AWOD_I_2625 | AWOD_II_0792 | 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. | L-threonine 3-dehydrogenase; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate; Belongs to the zinc-containing alcohol dehydrogenase family. | 0.915 |
| ilvA | thrA | AWOD_I_2625 | AWOD_I_2198 | 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. | Bifunctional aspartokinase/homoserine dehydrogenase I; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.669 |
| ilvA | thrB | AWOD_I_2625 | AWOD_I_2197 | 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. | Homoserine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. | 0.460 |
