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. | 0.627 |
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. | 0.647 |
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. | 0.825 |
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. | 0.614 |
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. | 0.991 |
VC_0030 | VC_1590 | VC_0030 | VC_1590 | Acetolactate synthase II, small subunit; Similar to GB:M87049 SP:P13048 GB:X02413 GB:X04890 PID:146459; identified by sequence similarity; putative. | Acetolactate synthase; Similar to GB:M73842 SP:P27696 GB:Y00525 PID:149211; identified by sequence similarity; putative; Belongs to the TPP enzyme family. | 0.683 |
VC_0030 | VC_2482 | VC_0030 | VC_2482 | Acetolactate synthase II, small subunit; Similar to GB:M87049 SP:P13048 GB:X02413 GB:X04890 PID:146459; identified by sequence similarity; putative. | Acetolactate synthase III, small subunit; Similar to PID:147816 GB:U00096 PID:1786266; identified by sequence similarity; putative. | 0.662 |
VC_0030 | VC_2483 | VC_0030 | VC_2483 | Acetolactate synthase II, small subunit; Similar to GB:M87049 SP:P13048 GB:X02413 GB:X04890 PID:146459; identified by sequence similarity; putative. | Acetolactate synthase III, large subunit; Similar to GB:D10483 SP:P00893 GB:X01609 PID:216494 PID:40845; identified by sequence similarity; putative. | 0.747 |
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. | 0.947 |
VC_0030 | ilvC | VC_0030 | VC_0162 | Acetolactate synthase II, small subunit; Similar to GB:M87049 SP:P13048 GB:X02413 GB:X04890 PID:146459; identified by sequence similarity; putative. | Ketol-acid reductoisomerase; 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. | 0.933 |
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. | 0.957 |
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. | 0.931 |
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. | 0.663 |
VC_0030 | leuB | VC_0030 | VC_2491 | Acetolactate synthase II, small subunit; Similar to GB:M87049 SP:P13048 GB:X02413 GB:X04890 PID:146459; identified by sequence similarity; putative. | 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 1 subfamily. | 0.668 |
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. | 0.991 |
VC_0031 | VC_1590 | VC_0031 | VC_1590 | Acetolactate synthase II, large subunit; Similar to SP:P00892; identified by sequence similarity; putative. | Acetolactate synthase; Similar to GB:M73842 SP:P27696 GB:Y00525 PID:149211; identified by sequence similarity; putative; Belongs to the TPP enzyme family. | 0.655 |
VC_0031 | VC_1977 | VC_0031 | VC_1977 | Acetolactate synthase II, large subunit; Similar to SP:P00892; identified by sequence similarity; putative. | Aspartate aminotransferase, putative; Similar to GB:U00096 PID:1788627 PID:1799660; identified by sequence similarity; putative. | 0.518 |
VC_0031 | VC_2482 | VC_0031 | VC_2482 | Acetolactate synthase II, large subunit; Similar to SP:P00892; identified by sequence similarity; putative. | Acetolactate synthase III, small subunit; Similar to PID:147816 GB:U00096 PID:1786266; identified by sequence similarity; putative. | 0.993 |
VC_0031 | VC_2483 | VC_0031 | VC_2483 | Acetolactate synthase II, large subunit; Similar to SP:P00892; identified by sequence similarity; putative. | Acetolactate synthase III, large subunit; Similar to GB:D10483 SP:P00893 GB:X01609 PID:216494 PID:40845; identified by sequence similarity; putative. | 0.781 |
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. | 0.955 |