| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| KB13_777 | ilvB_2 | KB13_777 | KB13_33 | Oxidoreductase, FAD-binding; [C] COG0247 Fe-S oxidoreductase. | Acetolactate synthase, large subunit, biosynthetic type; [EH] COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase]. | 0.902 |
| KB13_777 | ilvN | KB13_777 | KB13_289 | Oxidoreductase, FAD-binding; [C] COG0247 Fe-S oxidoreductase. | [E] COG0440 Acetolactate synthase, small (regulatory) subunit. | 0.812 |
| KB13_777 | leuA | KB13_777 | KB13_1170 | Oxidoreductase, FAD-binding; [C] COG0247 Fe-S oxidoreductase. | 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. | 0.803 |
| KB13_777 | maeB | KB13_777 | KB13_303 | Oxidoreductase, FAD-binding; [C] COG0247 Fe-S oxidoreductase. | Bifunctional protein: malate dehydrogenase phosphotransacetylase; [C] COG0281 Malic enzyme. | 0.889 |
| KB13_777 | oadA | KB13_777 | KB13_124 | Oxidoreductase, FAD-binding; [C] COG0247 Fe-S oxidoreductase. | [I] COG4770 Acetyl/propionyl-CoA carboxylase, alpha subunit. | 0.854 |
| KB13_777 | ppsA | KB13_777 | KB13_11 | Oxidoreductase, FAD-binding; [C] COG0247 Fe-S oxidoreductase. | Phosphoenolpyruvate synthase; Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate; Belongs to the PEP-utilizing enzyme family. | 0.898 |
| ilvA | ilvB_2 | KB13_711 | KB13_33 | 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; [EH] COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase]. | 0.901 |
| ilvA | ilvC | KB13_711 | KB13_541 | 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. | 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. | 0.632 |
| ilvA | ilvD | KB13_711 | KB13_839 | 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. | [EG] COG0129 Dihydroxyacid dehydratase/phosphogluconate dehydratase; Belongs to the IlvD/Edd family. | 0.895 |
| ilvA | ilvN | KB13_711 | KB13_289 | 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. | [E] COG0440 Acetolactate synthase, small (regulatory) subunit. | 0.955 |
| ilvB_2 | KB13_777 | KB13_33 | KB13_777 | Acetolactate synthase, large subunit, biosynthetic type; [EH] COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase]. | Oxidoreductase, FAD-binding; [C] COG0247 Fe-S oxidoreductase. | 0.902 |
| ilvB_2 | ilvA | KB13_33 | KB13_711 | Acetolactate synthase, large subunit, biosynthetic type; [EH] COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase]. | 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. | 0.901 |
| ilvB_2 | ilvC | KB13_33 | KB13_541 | Acetolactate synthase, large subunit, biosynthetic type; [EH] COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase]. | 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. | 0.995 |
| ilvB_2 | ilvD | KB13_33 | KB13_839 | Acetolactate synthase, large subunit, biosynthetic type; [EH] COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase]. | [EG] COG0129 Dihydroxyacid dehydratase/phosphogluconate dehydratase; Belongs to the IlvD/Edd family. | 0.810 |
| ilvB_2 | ilvN | KB13_33 | KB13_289 | Acetolactate synthase, large subunit, biosynthetic type; [EH] COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase]. | [E] COG0440 Acetolactate synthase, small (regulatory) subunit. | 0.999 |
| ilvB_2 | leuA | KB13_33 | KB13_1170 | Acetolactate synthase, large subunit, biosynthetic type; [EH] COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase]. | 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. | 0.800 |
| ilvB_2 | maeB | KB13_33 | KB13_303 | Acetolactate synthase, large subunit, biosynthetic type; [EH] COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase]. | Bifunctional protein: malate dehydrogenase phosphotransacetylase; [C] COG0281 Malic enzyme. | 0.788 |
| ilvB_2 | oadA | KB13_33 | KB13_124 | Acetolactate synthase, large subunit, biosynthetic type; [EH] COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase]. | [I] COG4770 Acetyl/propionyl-CoA carboxylase, alpha subunit. | 0.786 |
| ilvB_2 | ppsA | KB13_33 | KB13_11 | Acetolactate synthase, large subunit, biosynthetic type; [EH] COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase]. | Phosphoenolpyruvate synthase; Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate; Belongs to the PEP-utilizing enzyme family. | 0.729 |
| ilvB_2 | psd | KB13_33 | KB13_78 | Acetolactate synthase, large subunit, biosynthetic type; [EH] COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase]. | Phosphatidylserine decarboxylase family protein; Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). | 0.747 |