| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ilvA | ilvB-3 | CH64_2743 | CH64_601 | Threonine ammonia-lyase, biosynthetic; 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. | Acolac_lg: acetolactate synthase, large subunit, biosynthetic type. | 0.943 |
| ilvA | ilvB_2 | CH64_2743 | CH64_1866 | Threonine ammonia-lyase, biosynthetic; 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. | Thiamine pyrophosphate enzyme, central domain protein; Belongs to the TPP enzyme family. | 0.934 |
| ilvA | ilvC | CH64_2743 | CH64_2745 | Threonine ammonia-lyase, biosynthetic; 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. | 0.770 |
| ilvA | ilvM | CH64_2743 | CH64_2740 | Threonine ammonia-lyase, biosynthetic; 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 2 small subunit. | 0.969 |
| ilvA | ilvN | CH64_2743 | CH64_3277 | Threonine ammonia-lyase, biosynthetic; 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. | Small subunit; acolac_sm: acetolactate synthase, small subunit. | 0.964 |
| ilvA | ilvN-2 | CH64_2743 | CH64_602 | Threonine ammonia-lyase, biosynthetic; 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 1 small subunit. | 0.945 |
| ilvA | leuA | CH64_2743 | CH64_3273 | Threonine ammonia-lyase, biosynthetic; 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. | 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. | 0.630 |
| ilvA | leuB | CH64_2743 | CH64_3272 | Threonine ammonia-lyase, biosynthetic; 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 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. | 0.971 |
| ilvA | tdcB | CH64_2743 | CH64_2544 | Threonine ammonia-lyase, biosynthetic; 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. | Pyridoxal-phosphate dependent enzyme family protein. | 0.916 |
| ilvB-3 | ilvA | CH64_601 | CH64_2743 | Acolac_lg: acetolactate synthase, large subunit, biosynthetic type. | Threonine ammonia-lyase, biosynthetic; 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. | 0.943 |
| ilvB-3 | ilvB_2 | CH64_601 | CH64_1866 | Acolac_lg: acetolactate synthase, large subunit, biosynthetic type. | Thiamine pyrophosphate enzyme, central domain protein; Belongs to the TPP enzyme family. | 0.925 |
| ilvB-3 | ilvC | CH64_601 | CH64_2745 | Acolac_lg: acetolactate synthase, large subunit, biosynthetic type. | 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. | 0.988 |
| ilvB-3 | ilvM | CH64_601 | CH64_2740 | Acolac_lg: acetolactate synthase, large subunit, biosynthetic type. | Acetolactate synthase isozyme 2 small subunit. | 0.921 |
| ilvB-3 | ilvN | CH64_601 | CH64_3277 | Acolac_lg: acetolactate synthase, large subunit, biosynthetic type. | Small subunit; acolac_sm: acetolactate synthase, small subunit. | 0.995 |
| ilvB-3 | ilvN-2 | CH64_601 | CH64_602 | Acolac_lg: acetolactate synthase, large subunit, biosynthetic type. | Acetolactate synthase; Isozyme 1 small subunit. | 0.998 |
| ilvB-3 | leuA | CH64_601 | CH64_3273 | Acolac_lg: acetolactate synthase, large subunit, biosynthetic type. | 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. | 0.973 |
| ilvB-3 | leuB | CH64_601 | CH64_3272 | Acolac_lg: acetolactate synthase, large subunit, biosynthetic type. | 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. | 0.986 |
| ilvB-3 | nifJ | CH64_601 | CH64_646 | Acolac_lg: acetolactate synthase, large subunit, biosynthetic type. | Pyruvate:ferredoxin (flavodoxin) oxidoreductase; pyruv_ox_red: pyruvate:ferredoxin (flavodoxin) oxidoreductase. | 0.910 |
| ilvB-3 | tdcB | CH64_601 | CH64_2544 | Acolac_lg: acetolactate synthase, large subunit, biosynthetic type. | Pyridoxal-phosphate dependent enzyme family protein. | 0.941 |
| ilvB_2 | ilvA | CH64_1866 | CH64_2743 | Thiamine pyrophosphate enzyme, central domain protein; Belongs to the TPP enzyme family. | Threonine ammonia-lyase, biosynthetic; 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. | 0.934 |
