node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
dmlA | ilvB | b1800 | b3671 | D-malate oxidase, NAD-dependent; Catalyzes the NAD(+)-dependent oxidative decarboxylation of D-malate into pyruvate. Is essential for aerobic growth on D-malate as the sole carbon source. But is not required for anaerobic D-malate utilization, although DmlA is expressed and active in those conditions. Appears to be not able to use L-tartrate as a substrate for dehydrogenation instead of D-malate; Belongs to the isocitrate and isopropylmalate dehydrogenases family. | Acetolactate synthase I,valine-sensitive, large subunit. | 0.952 |
dmlA | ilvC | b1800 | b3774 | D-malate oxidase, NAD-dependent; Catalyzes the NAD(+)-dependent oxidative decarboxylation of D-malate into pyruvate. Is essential for aerobic growth on D-malate as the sole carbon source. But is not required for anaerobic D-malate utilization, although DmlA is expressed and active in those conditions. Appears to be not able to use L-tartrate as a substrate for dehydrogenation instead of D-malate; Belongs to the isocitrate and isopropylmalate dehydrogenases family. | Ketol-acid reductoisomerase, NAD(P)-binding; 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. Also able to use 2-ketopantoate, 2-ketoisovalerate, 2-ketovalerate, 2-ketobutyrate [...] | 0.792 |
dmlA | ilvD | b1800 | b3771 | D-malate oxidase, NAD-dependent; Catalyzes the NAD(+)-dependent oxidative decarboxylation of D-malate into pyruvate. Is essential for aerobic growth on D-malate as the sole carbon source. But is not required for anaerobic D-malate utilization, although DmlA is expressed and active in those conditions. Appears to be not able to use L-tartrate as a substrate for dehydrogenation instead of D-malate; Belongs to the isocitrate and isopropylmalate dehydrogenases family. | Dihydroxyacid dehydratase. | 0.606 |
dmlA | ilvH | b1800 | b0078 | D-malate oxidase, NAD-dependent; Catalyzes the NAD(+)-dependent oxidative decarboxylation of D-malate into pyruvate. Is essential for aerobic growth on D-malate as the sole carbon source. But is not required for anaerobic D-malate utilization, although DmlA is expressed and active in those conditions. Appears to be not able to use L-tartrate as a substrate for dehydrogenation instead of D-malate; Belongs to the isocitrate and isopropylmalate dehydrogenases family. | Acetolactate synthase III, valine sensitive, small subunit. | 0.968 |
dmlA | ilvM | b1800 | b3769 | D-malate oxidase, NAD-dependent; Catalyzes the NAD(+)-dependent oxidative decarboxylation of D-malate into pyruvate. Is essential for aerobic growth on D-malate as the sole carbon source. But is not required for anaerobic D-malate utilization, although DmlA is expressed and active in those conditions. Appears to be not able to use L-tartrate as a substrate for dehydrogenation instead of D-malate; Belongs to the isocitrate and isopropylmalate dehydrogenases family. | Pseudogene, acetolactate synthase 2 large subunit, valine-insensitive; acetolactate synthase II, large subunit, cryptic, interrupted. | 0.908 |
dmlA | ilvN | b1800 | b3670 | D-malate oxidase, NAD-dependent; Catalyzes the NAD(+)-dependent oxidative decarboxylation of D-malate into pyruvate. Is essential for aerobic growth on D-malate as the sole carbon source. But is not required for anaerobic D-malate utilization, although DmlA is expressed and active in those conditions. Appears to be not able to use L-tartrate as a substrate for dehydrogenation instead of D-malate; Belongs to the isocitrate and isopropylmalate dehydrogenases family. | Acetolactate synthase I, valine sensitive, small subunit. | 0.958 |
dmlA | leuA | b1800 | b0074 | D-malate oxidase, NAD-dependent; Catalyzes the NAD(+)-dependent oxidative decarboxylation of D-malate into pyruvate. Is essential for aerobic growth on D-malate as the sole carbon source. But is not required for anaerobic D-malate utilization, although DmlA is expressed and active in those conditions. Appears to be not able to use L-tartrate as a substrate for dehydrogenation instead of D-malate; Belongs to the isocitrate and isopropylmalate dehydrogenases 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. | 0.704 |
ilvA | ilvB | b3772 | b3671 | L-threonine dehydratase, 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 I,valine-sensitive, large subunit. | 0.986 |
ilvA | ilvC | b3772 | b3774 | L-threonine dehydratase, 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, NAD(P)-binding; 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. Also able to use 2-ketopantoate, 2-ketoisovalerate, 2-ketovalerate, 2-ketobutyrate [...] | 0.948 |
ilvA | ilvD | b3772 | b3771 | L-threonine dehydratase, 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. | Dihydroxyacid dehydratase. | 0.999 |
ilvA | ilvH | b3772 | b0078 | L-threonine dehydratase, 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 III, valine sensitive, small subunit. | 0.991 |
ilvA | ilvM | b3772 | b3769 | L-threonine dehydratase, 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. | Pseudogene, acetolactate synthase 2 large subunit, valine-insensitive; acetolactate synthase II, large subunit, cryptic, interrupted. | 0.996 |
ilvA | ilvN | b3772 | b3670 | L-threonine dehydratase, 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 I, valine sensitive, small subunit. | 0.982 |
ilvA | leuA | b3772 | b0074 | L-threonine dehydratase, 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. | 0.915 |
ilvA | leuB | b3772 | b0073 | L-threonine dehydratase, 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, NAD(+)-dependent; 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. Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 1 subfamily. | 0.986 |
ilvA | tdcB | b3772 | b3117 | L-threonine dehydratase, 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. | L-threonine dehydratase, catabolic; 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. TdcB also dehydrates serine t [...] | 0.927 |
ilvB | dmlA | b3671 | b1800 | Acetolactate synthase I,valine-sensitive, large subunit. | D-malate oxidase, NAD-dependent; Catalyzes the NAD(+)-dependent oxidative decarboxylation of D-malate into pyruvate. Is essential for aerobic growth on D-malate as the sole carbon source. But is not required for anaerobic D-malate utilization, although DmlA is expressed and active in those conditions. Appears to be not able to use L-tartrate as a substrate for dehydrogenation instead of D-malate; Belongs to the isocitrate and isopropylmalate dehydrogenases family. | 0.952 |
ilvB | ilvA | b3671 | b3772 | Acetolactate synthase I,valine-sensitive, large subunit. | L-threonine dehydratase, 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. | 0.986 |
ilvB | ilvC | b3671 | b3774 | Acetolactate synthase I,valine-sensitive, large subunit. | Ketol-acid reductoisomerase, NAD(P)-binding; 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. Also able to use 2-ketopantoate, 2-ketoisovalerate, 2-ketovalerate, 2-ketobutyrate [...] | 0.998 |
ilvB | ilvD | b3671 | b3771 | Acetolactate synthase I,valine-sensitive, large subunit. | Dihydroxyacid dehydratase. | 0.983 |