| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CED57418.1 | kbl | AWOD_II_0790 | AWOD_II_0791 | HTH-type transcriptional regulator, LysR-family; Belongs to the LysR transcriptional regulatory family. | 2-amino-3-ketobutyrate coenzyme A ligase; Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA. | 0.614 |
| CED57418.1 | tdh | AWOD_II_0790 | AWOD_II_0792 | HTH-type transcriptional regulator, LysR-family; Belongs to the LysR transcriptional regulatory family. | 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. | 0.614 |
| CED57773.1 | tdh | AWOD_II_1158 | AWOD_II_0792 | Putative exported hemolysin. | 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. | 0.579 |
| 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 | 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 | thrC | AWOD_I_1522 | AWOD_I_2196 | Putative threonine synthase. | Threonine synthase. | 0.900 |
| bioF | tdh | AWOD_II_0837 | AWOD_II_0792 | 8-amino-7-oxononanoate synthase; Catalyzes the decarboxylative condensation of pimeloyl-[acyl- carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide. | 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. | 0.743 |
| 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 | kbl | AWOD_II_0553 | AWOD_II_0791 | L-allo-threonine aldolase. | 2-amino-3-ketobutyrate coenzyme A ligase; Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA. | 0.910 |
| 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 | luxS | AWOD_I_2625 | AWOD_I_0523 | 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. | S-ribosylhomocysteine lyase; Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD). Belongs to the LuxS family. | 0.800 |
| 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 | thrC | AWOD_I_2625 | AWOD_I_2196 | 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. | Threonine synthase. | 0.950 |
| kbl | CED57418.1 | AWOD_II_0791 | AWOD_II_0790 | 2-amino-3-ketobutyrate coenzyme A ligase; Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA. | HTH-type transcriptional regulator, LysR-family; Belongs to the LysR transcriptional regulatory family. | 0.614 |
| kbl | gly | AWOD_II_0791 | AWOD_II_0553 | 2-amino-3-ketobutyrate coenzyme A ligase; Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA. | L-allo-threonine aldolase. | 0.910 |