| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CCH86438.1 | CCH89838.1 | MODMU_0988 | MODMU_4454 | L-threonine ammonia-lyase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Putative cystathionine gamma-lyase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.854 |
| CCH86438.1 | CCH90803.1 | MODMU_0988 | MODMU_5430 | L-threonine ammonia-lyase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Putative L-serine ammonia-lyase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.916 |
| 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. | 0.916 |
| 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. | 0.810 |
| CCH86438.1 | ilvE | MODMU_0988 | MODMU_4366 | L-threonine ammonia-lyase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Branched-chain amino acid aminotransferase protein (BCAT); Function of strongly homologous gene; enzyme. | 0.909 |
| 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. | 0.463 |
| CCH86438.1 | metB | MODMU_0988 | MODMU_4606 | L-threonine ammonia-lyase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Cystathionine gamma-synthase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.854 |
| CCH89838.1 | CCH86438.1 | MODMU_4454 | MODMU_0988 | Putative cystathionine gamma-lyase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | L-threonine ammonia-lyase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.854 |
| CCH89838.1 | CCH90803.1 | MODMU_4454 | MODMU_5430 | Putative cystathionine gamma-lyase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Putative L-serine ammonia-lyase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.838 |
| CCH89838.1 | ilvA | MODMU_4454 | MODMU_5312 | Putative cystathionine gamma-lyase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative 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. | 0.838 |
| CCH89838.1 | ilvE | MODMU_4454 | MODMU_4366 | Putative cystathionine gamma-lyase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Branched-chain amino acid aminotransferase protein (BCAT); Function of strongly homologous gene; enzyme. | 0.933 |
| CCH89838.1 | metB | MODMU_4454 | MODMU_4606 | Putative cystathionine gamma-lyase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Cystathionine gamma-synthase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.917 |
| CCH90803.1 | CCH86438.1 | MODMU_5430 | MODMU_0988 | Putative L-serine ammonia-lyase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | L-threonine ammonia-lyase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.916 |
| CCH90803.1 | CCH89838.1 | MODMU_5430 | MODMU_4454 | Putative L-serine ammonia-lyase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Putative cystathionine gamma-lyase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.838 |
| CCH90803.1 | ilvA | MODMU_5430 | MODMU_5312 | Putative L-serine ammonia-lyase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative 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. | 0.918 |
| CCH90803.1 | ilvD | MODMU_5430 | MODMU_4483 | Putative L-serine ammonia-lyase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Dihydroxy-acid dehydratase (DAD); Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the IlvD/Edd family. | 0.730 |
| CCH90803.1 | ilvE | MODMU_5430 | MODMU_4366 | Putative L-serine ammonia-lyase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Branched-chain amino acid aminotransferase protein (BCAT); Function of strongly homologous gene; enzyme. | 0.909 |
| CCH90803.1 | leuA | MODMU_5430 | MODMU_0583 | Putative L-serine ammonia-lyase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative 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. | 0.416 |
| CCH90803.1 | metB | MODMU_5430 | MODMU_4606 | Putative L-serine ammonia-lyase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Cystathionine gamma-synthase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.838 |
| 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. | 0.916 |