| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CED56871.1 | aceE | AWOD_II_0221 | AWOD_I_0416 | Pyruvate formate lyase. | Pyruvate dehydrogenase E1 component; Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). | 0.902 |
| CED56871.1 | ilvA | AWOD_II_0221 | AWOD_I_2625 | Pyruvate formate lyase. | 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. | 0.812 |
| CED56871.1 | ilvG | AWOD_II_0221 | AWOD_I_2622 | Pyruvate formate lyase. | Acetolactate synthase isozyme II large subunit. | 0.906 |
| CED56871.1 | ilvH | AWOD_II_0221 | AWOD_I_0340 | Pyruvate formate lyase. | Acetolactate synthase isozyme III small subunit. | 0.900 |
| CED56871.1 | ilvI | AWOD_II_0221 | AWOD_I_0339 | Pyruvate formate lyase. | Acetolactate synthase isozyme III large subunit. | 0.906 |
| CED56871.1 | ilvM | AWOD_II_0221 | AWOD_I_2623 | Pyruvate formate lyase. | Acetolactate synthase small subunit. | 0.900 |
| CED56871.1 | pflB | AWOD_II_0221 | AWOD_I_1694 | Pyruvate formate lyase. | Formate acetyltransferase 1. | 0.901 |
| aceE | CED56871.1 | AWOD_I_0416 | AWOD_II_0221 | Pyruvate dehydrogenase E1 component; Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). | Pyruvate formate lyase. | 0.902 |
| aceE | ilvG | AWOD_I_0416 | AWOD_I_2622 | Pyruvate dehydrogenase E1 component; Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). | Acetolactate synthase isozyme II large subunit. | 0.812 |
| aceE | ilvH | AWOD_I_0416 | AWOD_I_0340 | Pyruvate dehydrogenase E1 component; Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). | Acetolactate synthase isozyme III small subunit. | 0.823 |
| aceE | ilvI | AWOD_I_0416 | AWOD_I_0339 | Pyruvate dehydrogenase E1 component; Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). | Acetolactate synthase isozyme III large subunit. | 0.812 |
| aceE | ilvM | AWOD_I_0416 | AWOD_I_2623 | Pyruvate dehydrogenase E1 component; Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). | Acetolactate synthase small subunit. | 0.849 |
| aceE | pflB | AWOD_I_0416 | AWOD_I_1694 | Pyruvate dehydrogenase E1 component; Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). | Formate acetyltransferase 1. | 0.902 |
| ilvA | CED56871.1 | AWOD_I_2625 | AWOD_II_0221 | 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. | Pyruvate formate lyase. | 0.812 |
| ilvA | ilvC | AWOD_I_2625 | AWOD_I_2595 | 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. | 0.801 |
| ilvA | ilvD | AWOD_I_2625 | AWOD_I_2624 | 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; The CDS appears to have a deletion of 130 amino acid residues after codon 297 in comparison to orthologues; Belongs to the IlvD/Edd family. | 0.984 |
| ilvA | ilvG | AWOD_I_2625 | AWOD_I_2622 | 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 isozyme II large subunit. | 0.990 |
| ilvA | ilvH | AWOD_I_2625 | AWOD_I_0340 | 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 isozyme III small subunit. | 0.973 |
| ilvA | ilvI | AWOD_I_2625 | AWOD_I_0339 | 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 isozyme III large subunit. | 0.963 |
| ilvA | ilvM | AWOD_I_2625 | AWOD_I_2623 | 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. | 0.984 |
