| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| VC_0019 | VC_1977 | VC_0019 | VC_1977 | Valine-pyruvate aminotransferase; Similar to SP:P09053 PID:466710 GB:U00096 PID:1789996; identified by sequence similarity; putative. | Aspartate aminotransferase, putative; Similar to GB:U00096 PID:1788627 PID:1799660; identified by sequence similarity; putative. | 0.912 |
| VC_0019 | ilvD | VC_0019 | VC_0028 | Valine-pyruvate aminotransferase; Similar to SP:P09053 PID:466710 GB:U00096 PID:1789996; identified by sequence similarity; putative. | Dihydroxy-acid dehydratase; Similar to GP:288532; identified by sequence similarity; putative; Belongs to the IlvD/Edd family. | 0.902 |
| VC_0019 | ilvE | VC_0019 | VC_0029 | Valine-pyruvate aminotransferase; Similar to SP:P09053 PID:466710 GB:U00096 PID:1789996; identified by sequence similarity; putative. | Branched-chain amino acid amiotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.922 |
| VC_0019 | leuA | VC_0019 | VC_2490 | Valine-pyruvate aminotransferase; Similar to SP:P09053 PID:466710 GB:U00096 PID:1789996; identified by sequence similarity; putative. | 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. | 0.905 |
| VC_0030 | VC_0031 | VC_0030 | VC_0031 | Acetolactate synthase II, small subunit; Similar to GB:M87049 SP:P13048 GB:X02413 GB:X04890 PID:146459; identified by sequence similarity; putative. | Acetolactate synthase II, large subunit; Similar to SP:P00892; identified by sequence similarity; putative. | 0.982 |
| VC_0030 | ilvA | VC_0030 | VC_0027 | Acetolactate synthase II, small subunit; Similar to GB:M87049 SP:P13048 GB:X02413 GB:X04890 PID:146459; identified by sequence similarity; putative. | 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. | 0.989 |
| VC_0030 | ilvD | VC_0030 | VC_0028 | Acetolactate synthase II, small subunit; Similar to GB:M87049 SP:P13048 GB:X02413 GB:X04890 PID:146459; identified by sequence similarity; putative. | Dihydroxy-acid dehydratase; Similar to GP:288532; identified by sequence similarity; putative; Belongs to the IlvD/Edd family. | 0.976 |
| VC_0030 | ilvE | VC_0030 | VC_0029 | Acetolactate synthase II, small subunit; Similar to GB:M87049 SP:P13048 GB:X02413 GB:X04890 PID:146459; identified by sequence similarity; putative. | Branched-chain amino acid amiotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.950 |
| VC_0030 | leuA | VC_0030 | VC_2490 | Acetolactate synthase II, small subunit; Similar to GB:M87049 SP:P13048 GB:X02413 GB:X04890 PID:146459; identified by sequence similarity; putative. | 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. | 0.831 |
| VC_0031 | VC_0030 | VC_0031 | VC_0030 | Acetolactate synthase II, large subunit; Similar to SP:P00892; identified by sequence similarity; putative. | Acetolactate synthase II, small subunit; Similar to GB:M87049 SP:P13048 GB:X02413 GB:X04890 PID:146459; identified by sequence similarity; putative. | 0.982 |
| VC_0031 | VC_2364 | VC_0031 | VC_2364 | Acetolactate synthase II, large subunit; Similar to SP:P00892; identified by sequence similarity; putative. | Aspartokinase I/homoserine dehydrogenase, threonine-sensitive; Similar to SP:P27725; identified by sequence similarity; putative; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.621 |
| VC_0031 | VC_2684 | VC_0031 | VC_2684 | Acetolactate synthase II, large subunit; Similar to SP:P00892; identified by sequence similarity; putative. | Aspartokinase II/homoserine dehydrogenase, methionine-sensitive; Similar to GB:L19201 SP:P00562 GB:J01651 GB:V00305 PID:146841; identified by sequence similarity; putative; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.562 |
| VC_0031 | ilvA | VC_0031 | VC_0027 | Acetolactate synthase II, large subunit; Similar to SP:P00892; identified by sequence similarity; putative. | 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. | 0.994 |
| VC_0031 | ilvD | VC_0031 | VC_0028 | Acetolactate synthase II, large subunit; Similar to SP:P00892; identified by sequence similarity; putative. | Dihydroxy-acid dehydratase; Similar to GP:288532; identified by sequence similarity; putative; Belongs to the IlvD/Edd family. | 0.983 |
| VC_0031 | ilvE | VC_0031 | VC_0029 | Acetolactate synthase II, large subunit; Similar to SP:P00892; identified by sequence similarity; putative. | Branched-chain amino acid amiotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.933 |
| VC_0031 | leuA | VC_0031 | VC_2490 | Acetolactate synthase II, large subunit; Similar to SP:P00892; identified by sequence similarity; putative. | 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. | 0.970 |
| VC_1977 | VC_0019 | VC_1977 | VC_0019 | Aspartate aminotransferase, putative; Similar to GB:U00096 PID:1788627 PID:1799660; identified by sequence similarity; putative. | Valine-pyruvate aminotransferase; Similar to SP:P09053 PID:466710 GB:U00096 PID:1789996; identified by sequence similarity; putative. | 0.912 |
| VC_1977 | VC_2364 | VC_1977 | VC_2364 | Aspartate aminotransferase, putative; Similar to GB:U00096 PID:1788627 PID:1799660; identified by sequence similarity; putative. | Aspartokinase I/homoserine dehydrogenase, threonine-sensitive; Similar to SP:P27725; identified by sequence similarity; putative; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.841 |
| VC_1977 | VC_2684 | VC_1977 | VC_2684 | Aspartate aminotransferase, putative; Similar to GB:U00096 PID:1788627 PID:1799660; identified by sequence similarity; putative. | Aspartokinase II/homoserine dehydrogenase, methionine-sensitive; Similar to GB:L19201 SP:P00562 GB:J01651 GB:V00305 PID:146841; identified by sequence similarity; putative; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.841 |
| VC_1977 | ilvA | VC_1977 | VC_0027 | Aspartate aminotransferase, putative; Similar to GB:U00096 PID:1788627 PID:1799660; identified by sequence similarity; putative. | 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. | 0.407 |