| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| KB13_999 | ilvA | KB13_999 | KB13_711 | [E] COG0460 Homoserine dehydrogenase. | 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. | 0.681 |
| KB13_999 | ilvN | KB13_999 | KB13_289 | [E] COG0460 Homoserine dehydrogenase. | [E] COG0440 Acetolactate synthase, small (regulatory) subunit. | 0.849 |
| KB13_999 | metH | KB13_999 | KB13_806 | [E] COG0460 Homoserine dehydrogenase. | Methionine synthase; Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate. | 0.927 |
| ilvA | KB13_999 | KB13_711 | KB13_999 | 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. | [E] COG0460 Homoserine dehydrogenase. | 0.681 |
| ilvA | ilvB_1 | KB13_711 | KB13_578 | 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. | [E] COG3962 Acetolactate synthase; Belongs to the TPP enzyme family. | 0.810 |
| ilvA | ilvB_2 | KB13_711 | KB13_33 | 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, large subunit, biosynthetic type; [EH] COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase]. | 0.901 |
| ilvA | ilvC | KB13_711 | KB13_541 | 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. | 0.632 |
| ilvA | ilvN | KB13_711 | KB13_289 | 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. | [E] COG0440 Acetolactate synthase, small (regulatory) subunit. | 0.955 |
| ilvA | leuC | KB13_711 | KB13_996 | 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 dehydratase, large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.441 |
| ilvA | leuD | KB13_711 | KB13_158 | 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 dehydratase, small subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily. | 0.441 |
| ilvA | metH | KB13_711 | KB13_806 | 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. | Methionine synthase; Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate. | 0.907 |
| ilvB_1 | ilvA | KB13_578 | KB13_711 | [E] COG3962 Acetolactate synthase; 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. | 0.810 |
| ilvB_1 | ilvB_2 | KB13_578 | KB13_33 | [E] COG3962 Acetolactate synthase; Belongs to the TPP enzyme family. | Acetolactate synthase, large subunit, biosynthetic type; [EH] COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase]. | 0.655 |
| ilvB_1 | ilvC | KB13_578 | KB13_541 | [E] COG3962 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. | 0.947 |
| ilvB_1 | ilvN | KB13_578 | KB13_289 | [E] COG3962 Acetolactate synthase; Belongs to the TPP enzyme family. | [E] COG0440 Acetolactate synthase, small (regulatory) subunit. | 0.990 |
| ilvB_1 | leuA | KB13_578 | KB13_1170 | [E] COG3962 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. | 0.768 |
| ilvB_1 | leuC | KB13_578 | KB13_996 | [E] COG3962 Acetolactate synthase; Belongs to the TPP enzyme family. | 3-isopropylmalate dehydratase, large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.525 |
| ilvB_1 | leuD | KB13_578 | KB13_158 | [E] COG3962 Acetolactate synthase; Belongs to the TPP enzyme family. | 3-isopropylmalate dehydratase, small subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily. | 0.566 |
| ilvB_1 | maeB | KB13_578 | KB13_303 | [E] COG3962 Acetolactate synthase; Belongs to the TPP enzyme family. | Bifunctional protein: malate dehydrogenase phosphotransacetylase; [C] COG0281 Malic enzyme. | 0.788 |
| ilvB_2 | ilvA | KB13_33 | KB13_711 | Acetolactate synthase, large subunit, biosynthetic type; [EH] COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase]. | 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. | 0.901 |
