| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| budA | budB | WL1483_3191 | WL1483_1976 | Alpha-acetolactate decarboxylase. | Acetolactate synthase; Belongs to the TPP enzyme family. | 0.997 |
| budA | ilvH | WL1483_3191 | WL1483_218 | Alpha-acetolactate decarboxylase. | Acetolactate synthase 3 regulatory subunit. | 0.925 |
| budA | ilvI | WL1483_3191 | WL1483_248 | Alpha-acetolactate decarboxylase. | Acetolactate synthase, large subunit. | 0.969 |
| budA | ilvM | WL1483_3191 | WL1483_3006 | Alpha-acetolactate decarboxylase. | Acetolactate synthase II small subunit. | 0.902 |
| budB | budA | WL1483_1976 | WL1483_3191 | Acetolactate synthase; Belongs to the TPP enzyme family. | Alpha-acetolactate decarboxylase. | 0.997 |
| budB | ilvA | WL1483_1976 | WL1483_1569 | Acetolactate synthase; Belongs to the TPP enzyme family. | 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. | 0.928 |
| budB | ilvC | WL1483_1976 | WL1483_4 | Acetolactate synthase; Belongs to the TPP enzyme family. | 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. | 0.977 |
| budB | ilvD | WL1483_1976 | WL1483_2083 | Acetolactate synthase; Belongs to the TPP enzyme family. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.723 |
| budB | ilvH | WL1483_1976 | WL1483_218 | Acetolactate synthase; Belongs to the TPP enzyme family. | Acetolactate synthase 3 regulatory subunit. | 0.996 |
| budB | ilvI | WL1483_1976 | WL1483_248 | Acetolactate synthase; Belongs to the TPP enzyme family. | Acetolactate synthase, large subunit. | 0.922 |
| budB | ilvM | WL1483_1976 | WL1483_3006 | Acetolactate synthase; Belongs to the TPP enzyme family. | Acetolactate synthase II small subunit. | 0.930 |
| budB | leuA | WL1483_1976 | WL1483_3739 | Acetolactate synthase; Belongs to the TPP enzyme family. | 2-isopropylmalate synthase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily. | 0.922 |
| budB | leuB | WL1483_1976 | WL1483_903 | Acetolactate synthase; Belongs to the TPP enzyme family. | 3-isopropylmalate dehydrogenase; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. | 0.956 |
| budB | nifJ | WL1483_1976 | WL1483_3102 | Acetolactate synthase; Belongs to the TPP enzyme family. | Ferredoxin oxidoreductase. | 0.948 |
| ilvA | budB | WL1483_1569 | WL1483_1976 | 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; Belongs to the TPP enzyme family. | 0.928 |
| ilvA | ilvC | WL1483_1569 | WL1483_4 | 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. | 0.686 |
| ilvA | ilvD | WL1483_1569 | WL1483_2083 | 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. | 0.953 |
| ilvA | ilvH | WL1483_1569 | WL1483_218 | 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 3 regulatory subunit. | 0.978 |
| ilvA | ilvI | WL1483_1569 | WL1483_248 | 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, large subunit. | 0.940 |
| ilvA | ilvM | WL1483_1569 | WL1483_3006 | 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 II small subunit. | 0.963 |