node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
SFW11154.1 | SFW11268.1 | SAMN02910447_00103 | SAMN02910447_00130 | 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. | Acetaldehyde dehydrogenase / alcohol dehydrogenase; In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase family. | 0.953 |
SFW11154.1 | SFW11506.1 | SAMN02910447_00103 | SAMN02910447_00166 | 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. | Pyruvate-ferredoxin/flavodoxin oxidoreductase. | 0.965 |
SFW11154.1 | SFW35855.1 | SAMN02910447_00103 | SAMN02910447_02027 | 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. | Beta-ketoacyl synthase, C-terminal domain; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. | 0.428 |
SFW11154.1 | SFW39392.1 | SAMN02910447_00103 | SAMN02910447_02298 | 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. | 0.956 |
SFW11154.1 | SFW39413.1 | SAMN02910447_00103 | SAMN02910447_02301 | 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, small subunit. | 0.985 |
SFW11154.1 | ilvC | SAMN02910447_00103 | SAMN02910447_02302 | 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. | 0.848 |
SFW11154.1 | ilvD | SAMN02910447_00103 | SAMN02910447_00759 | 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. | 0.904 |
SFW11154.1 | leuA | SAMN02910447_00103 | SAMN02910447_02807 | 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. | 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 2 subfamily. | 0.634 |
SFW11154.1 | leuB | SAMN02910447_00103 | SAMN02910447_01194 | 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. | 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. | 0.957 |
SFW11268.1 | SFW11154.1 | SAMN02910447_00130 | SAMN02910447_00103 | Acetaldehyde dehydrogenase / alcohol dehydrogenase; In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase 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. | 0.953 |
SFW11268.1 | SFW11506.1 | SAMN02910447_00130 | SAMN02910447_00166 | Acetaldehyde dehydrogenase / alcohol dehydrogenase; In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase family. | Pyruvate-ferredoxin/flavodoxin oxidoreductase. | 0.977 |
SFW11268.1 | SFW35855.1 | SAMN02910447_00130 | SAMN02910447_02027 | Acetaldehyde dehydrogenase / alcohol dehydrogenase; In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase family. | Beta-ketoacyl synthase, C-terminal domain; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. | 0.988 |
SFW11268.1 | SFW39392.1 | SAMN02910447_00130 | SAMN02910447_02298 | Acetaldehyde dehydrogenase / alcohol dehydrogenase; In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase family. | Acetolactate synthase, large subunit. | 0.929 |
SFW11268.1 | SFW39413.1 | SAMN02910447_00130 | SAMN02910447_02301 | Acetaldehyde dehydrogenase / alcohol dehydrogenase; In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase family. | Acetolactate synthase, small subunit. | 0.567 |
SFW11268.1 | SFW48213.1 | SAMN02910447_00130 | SAMN02910447_03042 | Acetaldehyde dehydrogenase / alcohol dehydrogenase; In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase family. | Pyruvate kinase; Belongs to the pyruvate kinase family. | 0.952 |
SFW11268.1 | ilvC | SAMN02910447_00130 | SAMN02910447_02302 | Acetaldehyde dehydrogenase / alcohol dehydrogenase; In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase 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. | 0.497 |
SFW11268.1 | ilvD | SAMN02910447_00130 | SAMN02910447_00759 | Acetaldehyde dehydrogenase / alcohol dehydrogenase; In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase family. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.572 |
SFW11268.1 | leuA | SAMN02910447_00130 | SAMN02910447_02807 | Acetaldehyde dehydrogenase / alcohol dehydrogenase; In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase 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 2 subfamily. | 0.946 |
SFW11268.1 | leuB | SAMN02910447_00130 | SAMN02910447_01194 | Acetaldehyde dehydrogenase / alcohol dehydrogenase; In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase 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. | 0.765 |
SFW11506.1 | SFW11154.1 | SAMN02910447_00166 | SAMN02910447_00103 | Pyruvate-ferredoxin/flavodoxin oxidoreductase. | 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. | 0.965 |