| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Atu2737 | Atu2738 | Atu2737 | Atu2738 | Oxidoredutase. | Nucleoside-diphosphate-sugar epimerase. | 0.886 |
| Atu2737 | ilvA-2 | Atu2737 | Atu2735 | Oxidoredutase. | Threonine dehydratase. | 0.587 |
| Atu2737 | ilvD-2 | Atu2737 | Atu2736 | Oxidoredutase. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.811 |
| Atu2738 | Atu2737 | Atu2738 | Atu2737 | Nucleoside-diphosphate-sugar epimerase. | Oxidoredutase. | 0.886 |
| Atu2738 | ilvA-2 | Atu2738 | Atu2735 | Nucleoside-diphosphate-sugar epimerase. | Threonine dehydratase. | 0.552 |
| Atu2738 | ilvD-2 | Atu2738 | Atu2736 | Nucleoside-diphosphate-sugar epimerase. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.873 |
| Atu2738 | ilvD-3 | Atu2738 | Atu3219 | Nucleoside-diphosphate-sugar epimerase. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.471 |
| ilvA | ilvA-2 | Atu1205 | Atu2735 | 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 dehydratase. | 0.923 |
| ilvA | ilvC | Atu1205 | Atu2019 | 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. | Ketol-acid reductoisomerase; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. | 0.671 |
| ilvA | ilvD-2 | Atu1205 | Atu2736 | 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. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.777 |
| ilvA | ilvD-3 | Atu1205 | Atu3219 | 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. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.769 |
| ilvA | ilvE | Atu1205 | Atu0871 | 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. | Branched-chain-amino-acid aminotransferase. | 0.886 |
| ilvA | ilvH | Atu1205 | Atu2035 | 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. | Acetolactate synthase, small subunit. | 0.942 |
| ilvA | ilvI | Atu1205 | Atu2036 | 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. | Acetolactate synthase III, large subunit. | 0.953 |
| ilvA | leuC | Atu1205 | Atu2709 | 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. | 3-isopropylmalate dehydratase, large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.564 |
| ilvA-2 | Atu2737 | Atu2735 | Atu2737 | Threonine dehydratase. | Oxidoredutase. | 0.587 |
| ilvA-2 | Atu2738 | Atu2735 | Atu2738 | Threonine dehydratase. | Nucleoside-diphosphate-sugar epimerase. | 0.552 |
| ilvA-2 | ilvA | Atu2735 | Atu1205 | Threonine dehydratase. | 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. | 0.923 |
| ilvA-2 | ilvC | Atu2735 | Atu2019 | Threonine dehydratase. | Ketol-acid reductoisomerase; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. | 0.630 |
| ilvA-2 | ilvD-2 | Atu2735 | Atu2736 | Threonine dehydratase. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.876 |
