| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| IlvM | ilvA | HMPREF0758_1133 | HMPREF0758_1130 | Hypothetical protein; COG: COG3978; 2.2.1.6. | 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. | 0.959 |
| IlvM | ilvB-3 | HMPREF0758_1133 | HMPREF0758_1134 | Hypothetical protein; COG: COG3978; 2.2.1.6. | Acetolactate synthase, large subunit, biosynthetic type; COG: COG0028; Pfam: PF02776,PF00205,PF02775; InterPro: IPR012846. | 0.993 |
| IlvM | ilvD | HMPREF0758_1133 | HMPREF0758_1131 | Hypothetical protein; COG: COG3978; 2.2.1.6. | Dihydroxy-acid dehydratase; COG: COG0129; Pfam: PF00920; InterPro: IPR004404; Belongs to the IlvD/Edd family. | 0.893 |
| IlvM | ilvE | HMPREF0758_1133 | HMPREF0758_1132 | Hypothetical protein; COG: COG3978; 2.2.1.6. | Branched-chain-amino-acid transaminase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.919 |
| IlvM | leuA | HMPREF0758_1133 | HMPREF0758_0530 | Hypothetical protein; COG: COG3978; 2.2.1.6. | 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. | 0.817 |
| IlvM | leuA-2 | HMPREF0758_1133 | HMPREF0758_4216 | Hypothetical protein; COG: COG3978; 2.2.1.6. | 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). | 0.817 |
| avtA | ilvD | HMPREF0758_1384 | HMPREF0758_1131 | Aminotransferase, class I/II; COG: COG3977; Pfam: PF00155; InterPro: IPR004839. | Dihydroxy-acid dehydratase; COG: COG0129; Pfam: PF00920; InterPro: IPR004404; Belongs to the IlvD/Edd family. | 0.913 |
| avtA | ilvE | HMPREF0758_1384 | HMPREF0758_1132 | Aminotransferase, class I/II; COG: COG3977; Pfam: PF00155; InterPro: IPR004839. | Branched-chain-amino-acid transaminase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.918 |
| avtA | leuA | HMPREF0758_1384 | HMPREF0758_0530 | Aminotransferase, class I/II; COG: COG3977; Pfam: PF00155; InterPro: IPR004839. | 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. | 0.906 |
| avtA | leuA-2 | HMPREF0758_1384 | HMPREF0758_4216 | Aminotransferase, class I/II; COG: COG3977; Pfam: PF00155; InterPro: IPR004839. | 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). | 0.906 |
| ilvA | IlvM | HMPREF0758_1130 | HMPREF0758_1133 | 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. | Hypothetical protein; COG: COG3978; 2.2.1.6. | 0.959 |
| ilvA | ilvB-3 | HMPREF0758_1130 | HMPREF0758_1134 | 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. | Acetolactate synthase, large subunit, biosynthetic type; COG: COG0028; Pfam: PF02776,PF00205,PF02775; InterPro: IPR012846. | 0.963 |
| ilvA | ilvD | HMPREF0758_1130 | HMPREF0758_1131 | 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. | Dihydroxy-acid dehydratase; COG: COG0129; Pfam: PF00920; InterPro: IPR004404; Belongs to the IlvD/Edd family. | 0.937 |
| ilvA | ilvE | HMPREF0758_1130 | HMPREF0758_1132 | 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. | Branched-chain-amino-acid transaminase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.941 |
| 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 | 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 |
| ilvB-3 | IlvM | HMPREF0758_1134 | HMPREF0758_1133 | Acetolactate synthase, large subunit, biosynthetic type; COG: COG0028; Pfam: PF02776,PF00205,PF02775; InterPro: IPR012846. | Hypothetical protein; COG: COG3978; 2.2.1.6. | 0.993 |
| ilvB-3 | ilvA | HMPREF0758_1134 | HMPREF0758_1130 | Acetolactate synthase, large subunit, biosynthetic type; COG: COG0028; Pfam: PF02776,PF00205,PF02775; InterPro: IPR012846. | 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. | 0.963 |
| ilvB-3 | ilvD | HMPREF0758_1134 | HMPREF0758_1131 | Acetolactate synthase, large subunit, biosynthetic type; COG: COG0028; Pfam: PF02776,PF00205,PF02775; InterPro: IPR012846. | Dihydroxy-acid dehydratase; COG: COG0129; Pfam: PF00920; InterPro: IPR004404; Belongs to the IlvD/Edd family. | 0.949 |
| ilvB-3 | ilvE | HMPREF0758_1134 | HMPREF0758_1132 | Acetolactate synthase, large subunit, biosynthetic type; COG: COG0028; Pfam: PF02776,PF00205,PF02775; InterPro: IPR012846. | Branched-chain-amino-acid transaminase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.933 |