| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| F897_00230 | ilvD | F897_00230 | F897_00618 | 4-hydroxy-2-oxovalerate aldolase; Catalyzes the retro-aldol cleavage of 4-hydroxy-2- oxopentanoate to pyruvate and acetaldehyde. Is involved in the meta- cleavage pathway for the degradation of aromatic compounds. Belongs to the 4-hydroxy-2-oxovalerate aldolase family. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.728 |
| F897_00230 | ilvD-2 | F897_00230 | F897_00621 | 4-hydroxy-2-oxovalerate aldolase; Catalyzes the retro-aldol cleavage of 4-hydroxy-2- oxopentanoate to pyruvate and acetaldehyde. Is involved in the meta- cleavage pathway for the degradation of aromatic compounds. Belongs to the 4-hydroxy-2-oxovalerate aldolase family. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.728 |
| F897_00230 | ilvE | F897_00230 | F897_00053 | 4-hydroxy-2-oxovalerate aldolase; Catalyzes the retro-aldol cleavage of 4-hydroxy-2- oxopentanoate to pyruvate and acetaldehyde. Is involved in the meta- cleavage pathway for the degradation of aromatic compounds. Belongs to the 4-hydroxy-2-oxovalerate aldolase family. | Branched-chain-amino-acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.832 |
| F897_00836 | F897_02557 | F897_00836 | F897_02557 | Homoserine dehydrogenase. | Aminotran_1_2 domain-containing protein. | 0.503 |
| F897_00836 | ilvE | F897_00836 | F897_00053 | Homoserine dehydrogenase. | Branched-chain-amino-acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.847 |
| F897_02557 | F897_00836 | F897_02557 | F897_00836 | Aminotran_1_2 domain-containing protein. | Homoserine dehydrogenase. | 0.503 |
| F897_02557 | ilvD | F897_02557 | F897_00618 | Aminotran_1_2 domain-containing protein. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.905 |
| F897_02557 | ilvD-2 | F897_02557 | F897_00621 | Aminotran_1_2 domain-containing protein. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.905 |
| F897_02557 | ilvE | F897_02557 | F897_00053 | Aminotran_1_2 domain-containing protein. | Branched-chain-amino-acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.926 |
| F897_02557 | leuA | F897_02557 | F897_00130 | Aminotran_1_2 domain-containing protein. | 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. | 0.900 |
| gshA | ilvE | F897_00466 | F897_00053 | Glutamate--cysteine ligase; Belongs to the glutamate--cysteine ligase type 1 family. Type 1 subfamily. | Branched-chain-amino-acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.900 |
| ilvA | ilvD | F897_01944 | F897_00618 | L-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. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.710 |
| ilvA | ilvD-2 | F897_01944 | F897_00621 | L-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. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.733 |
| ilvA | ilvE | F897_01944 | F897_00053 | L-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. | Branched-chain-amino-acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.921 |
| ilvD | F897_00230 | F897_00618 | F897_00230 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 4-hydroxy-2-oxovalerate aldolase; Catalyzes the retro-aldol cleavage of 4-hydroxy-2- oxopentanoate to pyruvate and acetaldehyde. Is involved in the meta- cleavage pathway for the degradation of aromatic compounds. Belongs to the 4-hydroxy-2-oxovalerate aldolase family. | 0.728 |
| ilvD | F897_02557 | F897_00618 | F897_02557 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | Aminotran_1_2 domain-containing protein. | 0.905 |
| ilvD | ilvA | F897_00618 | F897_01944 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | L-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. | 0.710 |
| ilvD | ilvD-2 | F897_00618 | F897_00621 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.927 |
| ilvD | ilvE | F897_00618 | F897_00053 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | Branched-chain-amino-acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.988 |
| ilvD | leuA | F897_00618 | F897_00130 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 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. | 0.982 |