| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CCH86438.1 | ilvA | MODMU_0988 | MODMU_5312 | L-threonine ammonia-lyase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 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. | 0.699 |
| CCH86438.1 | ilvC | MODMU_0988 | MODMU_4478 | L-threonine ammonia-lyase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Ketol-acid reductoisomerase (NADP(+)); 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. | 0.778 |
| CCH86438.1 | ilvD | MODMU_0988 | MODMU_4483 | L-threonine ammonia-lyase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Dihydroxy-acid dehydratase (DAD); Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the IlvD/Edd family. | 0.855 |
| CCH86438.1 | ilvH | MODMU_0988 | MODMU_4479 | L-threonine ammonia-lyase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Acetolactate synthase small subunit (AHAS) (Acetohydroxy-acid synthase small subunit) (ALS); Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.986 |
| CCH86438.1 | ilvI | MODMU_0988 | MODMU_4480 | L-threonine ammonia-lyase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Acetolactate synthase large subunit (AHAS) (Acetohydroxy-acid synthase large subunit) (ALS); Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.978 |
| CCH86438.1 | korA | MODMU_0988 | MODMU_4952 | L-threonine ammonia-lyase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 2-oxoacid:ferredoxin oxidoreductase, alpha subunit; Function of strongly homologous gene; enzyme. | 0.962 |
| CCH86438.1 | korB | MODMU_0988 | MODMU_4953 | L-threonine ammonia-lyase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 2-oxoacid:ferredoxin oxidoreductase, beta subunit; Function of strongly homologous gene; enzyme. | 0.794 |
| CCH86438.1 | leuA | MODMU_0988 | MODMU_0583 | L-threonine ammonia-lyase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 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. | 0.419 |
| CCH86438.1 | leuB | MODMU_0988 | MODMU_4474 | L-threonine ammonia-lyase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 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. Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 2 subfamily. | 0.941 |
| CCH86438.1 | leuC | MODMU_0988 | MODMU_4463 | L-threonine ammonia-lyase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 3-isopropylmalate dehydratase (large subunit); Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.661 |
| ilvA | CCH86438.1 | MODMU_5312 | MODMU_0988 | 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. | L-threonine ammonia-lyase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.699 |
| ilvA | ilvC | MODMU_5312 | MODMU_4478 | 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 (NADP(+)); 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. | 0.682 |
| ilvA | ilvD | MODMU_5312 | MODMU_4483 | 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 (DAD); Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the IlvD/Edd family. | 0.827 |
| ilvA | ilvH | MODMU_5312 | MODMU_4479 | 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 (AHAS) (Acetohydroxy-acid synthase small subunit) (ALS); Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.901 |
| ilvA | ilvI | MODMU_5312 | MODMU_4480 | 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 (AHAS) (Acetohydroxy-acid synthase large subunit) (ALS); Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.923 |
| ilvA | korA | MODMU_5312 | MODMU_4952 | 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-oxoacid:ferredoxin oxidoreductase, alpha subunit; Function of strongly homologous gene; enzyme. | 0.844 |
| ilvA | korB | MODMU_5312 | MODMU_4953 | 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-oxoacid:ferredoxin oxidoreductase, beta subunit; Function of strongly homologous gene; enzyme. | 0.502 |
| ilvA | leuB | MODMU_5312 | MODMU_4474 | 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. Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 2 subfamily. | 0.750 |
| ilvA | leuC | MODMU_5312 | MODMU_4463 | 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 dehydratase (large subunit); Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.569 |
| ilvC | CCH86438.1 | MODMU_4478 | MODMU_0988 | Ketol-acid reductoisomerase (NADP(+)); 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. | L-threonine ammonia-lyase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.778 |
