| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| alsS | budA | lwe2026 | lwe2011 | Acetolactate synthase; Belongs to the TPP enzyme family. | Alpha-acetolactate decarboxylase. | 0.987 |
| alsS | ilvA | lwe2026 | lwe2010 | 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. | 0.933 |
| alsS | ilvB | lwe2026 | lwe2003 | Acetolactate synthase; Belongs to the TPP enzyme family. | Acetolactate synthase large subunit. | 0.921 |
| alsS | ilvC | lwe2026 | lwe2005 | 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. | 0.966 |
| alsS | ilvD | lwe2026 | lwe2002 | Acetolactate synthase; Belongs to the TPP enzyme family. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.694 |
| alsS | ilvN | lwe2026 | lwe2004 | Acetolactate synthase; Belongs to the TPP enzyme family. | Acetolactate synthase, small subunit. | 0.993 |
| alsS | leuA | lwe2026 | lwe2006 | 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. | 0.913 |
| alsS | leuB | lwe2026 | lwe2007 | 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. | 0.953 |
| alsS | lwe0691 | lwe2026 | lwe0691 | Acetolactate synthase; Belongs to the TPP enzyme family. | Pyruvate oxidase; Belongs to the TPP enzyme family. | 0.847 |
| alsS | nifJ | lwe2026 | lwe0820 | Acetolactate synthase; Belongs to the TPP enzyme family. | Pyruvate-flavodoxin oxidoreductase. | 0.958 |
| budA | alsS | lwe2011 | lwe2026 | Alpha-acetolactate decarboxylase. | Acetolactate synthase; Belongs to the TPP enzyme family. | 0.987 |
| budA | ilvA | lwe2011 | lwe2010 | Alpha-acetolactate decarboxylase. | 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. | 0.481 |
| budA | ilvB | lwe2011 | lwe2003 | Alpha-acetolactate decarboxylase. | Acetolactate synthase large subunit. | 0.963 |
| budA | ilvN | lwe2011 | lwe2004 | Alpha-acetolactate decarboxylase. | Acetolactate synthase, small subunit. | 0.931 |
| budA | leuA | lwe2011 | lwe2006 | Alpha-acetolactate decarboxylase. | 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. | 0.421 |
| budA | leuB | lwe2011 | lwe2007 | Alpha-acetolactate decarboxylase. | 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. | 0.421 |
| budA | lwe0691 | lwe2011 | lwe0691 | Alpha-acetolactate decarboxylase. | Pyruvate oxidase; Belongs to the TPP enzyme family. | 0.635 |
| ilvA | alsS | lwe2010 | lwe2026 | 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. | 0.933 |
| ilvA | budA | lwe2010 | lwe2011 | 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. | Alpha-acetolactate decarboxylase. | 0.481 |
| ilvA | ilvB | lwe2010 | lwe2003 | 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. | 0.967 |