| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ilvA | itaE | HMPREF0758_1130 | HMPREF0758_4468 | 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. | Beta-eliminating lyase; COG: COG2008; Pfam: PF01212; InterPro: IPR001597. | 0.918 |
| ilvA | metL | HMPREF0758_1130 | HMPREF0758_1159 | 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. | Homoserine dehydrogenase; COG: COG0460; Pfam: PF00742; InterPro: IPR001342. | 0.705 |
| ilvA | metM2 | HMPREF0758_1130 | HMPREF0758_1160 | 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. | Amino acid kinase family; COG: COG0527; Pfam: PF00696; InterPro: IPR001341. | 0.705 |
| ilvA | tdcB | HMPREF0758_1130 | HMPREF0758_1370 | 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. | Pyridoxal-phosphate dependent protein; COG: COG1171; Pfam: PF00291; InterPro: IPR001926. | 0.920 |
| ilvA | tdh | HMPREF0758_1130 | HMPREF0758_1243 | 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. | L-threonine 3-dehydrogenase; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate; Belongs to the zinc-containing alcohol dehydrogenase family. | 0.914 |
| ilvA | thrA | HMPREF0758_1130 | HMPREF0758_0591 | 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. | Homoserine dehydrogenase; COG: COG0527; Pfam: PF00696,PF01842,PF03447,PF00742; InterPro: IPR001341; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.705 |
| ilvA | thrB | HMPREF0758_1130 | HMPREF0758_0590 | 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. | Homoserine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. | 0.436 |
| ilvA | thrC | HMPREF0758_1130 | HMPREF0758_0589 | 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. | Threonine synthase; COG: COG0498; Pfam: PF00291; InterPro: IPR004450. | 0.949 |
| itaE | ilvA | HMPREF0758_4468 | HMPREF0758_1130 | Beta-eliminating lyase; COG: COG2008; Pfam: PF01212; InterPro: IPR001597. | 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. | 0.918 |
| itaE | metL | HMPREF0758_4468 | HMPREF0758_1159 | Beta-eliminating lyase; COG: COG2008; Pfam: PF01212; InterPro: IPR001597. | Homoserine dehydrogenase; COG: COG0460; Pfam: PF00742; InterPro: IPR001342. | 0.438 |
| itaE | metM2 | HMPREF0758_4468 | HMPREF0758_1160 | Beta-eliminating lyase; COG: COG2008; Pfam: PF01212; InterPro: IPR001597. | Amino acid kinase family; COG: COG0527; Pfam: PF00696; InterPro: IPR001341. | 0.438 |
| itaE | tdcB | HMPREF0758_4468 | HMPREF0758_1370 | Beta-eliminating lyase; COG: COG2008; Pfam: PF01212; InterPro: IPR001597. | Pyridoxal-phosphate dependent protein; COG: COG1171; Pfam: PF00291; InterPro: IPR001926. | 0.918 |
| itaE | tdh | HMPREF0758_4468 | HMPREF0758_1243 | Beta-eliminating lyase; COG: COG2008; Pfam: PF01212; InterPro: IPR001597. | L-threonine 3-dehydrogenase; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate; Belongs to the zinc-containing alcohol dehydrogenase family. | 0.900 |
| itaE | thrA | HMPREF0758_4468 | HMPREF0758_0591 | Beta-eliminating lyase; COG: COG2008; Pfam: PF01212; InterPro: IPR001597. | Homoserine dehydrogenase; COG: COG0527; Pfam: PF00696,PF01842,PF03447,PF00742; InterPro: IPR001341; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.438 |
| itaE | thrC | HMPREF0758_4468 | HMPREF0758_0589 | Beta-eliminating lyase; COG: COG2008; Pfam: PF01212; InterPro: IPR001597. | Threonine synthase; COG: COG0498; Pfam: PF00291; InterPro: IPR004450. | 0.926 |
| metL | ilvA | HMPREF0758_1159 | HMPREF0758_1130 | Homoserine dehydrogenase; COG: COG0460; Pfam: PF00742; InterPro: IPR001342. | 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. | 0.705 |
| metL | itaE | HMPREF0758_1159 | HMPREF0758_4468 | Homoserine dehydrogenase; COG: COG0460; Pfam: PF00742; InterPro: IPR001342. | Beta-eliminating lyase; COG: COG2008; Pfam: PF01212; InterPro: IPR001597. | 0.438 |
| metL | metM2 | HMPREF0758_1159 | HMPREF0758_1160 | Homoserine dehydrogenase; COG: COG0460; Pfam: PF00742; InterPro: IPR001342. | Amino acid kinase family; COG: COG0527; Pfam: PF00696; InterPro: IPR001341. | 0.998 |
| metL | serC | HMPREF0758_1159 | HMPREF0758_4386 | Homoserine dehydrogenase; COG: COG0460; Pfam: PF00742; InterPro: IPR001342. | Phosphoserine transaminase; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily. | 0.601 |
| metL | tdcB | HMPREF0758_1159 | HMPREF0758_1370 | Homoserine dehydrogenase; COG: COG0460; Pfam: PF00742; InterPro: IPR001342. | Pyridoxal-phosphate dependent protein; COG: COG1171; Pfam: PF00291; InterPro: IPR001926. | 0.705 |