| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| KB13_1234 | ilvB_2 | KB13_1234 | KB13_33 | Conserved hypothetical protein TIGR00044; Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis; Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family. | Acetolactate synthase, large subunit, biosynthetic type; [EH] COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase]. | 0.613 |
| KB13_1234 | ilvC | KB13_1234 | KB13_541 | Conserved hypothetical protein TIGR00044; Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis; Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family. | 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. | 0.585 |
| KB13_1234 | ilvN | KB13_1234 | KB13_289 | Conserved hypothetical protein TIGR00044; Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis; Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family. | [E] COG0440 Acetolactate synthase, small (regulatory) subunit. | 0.613 |
| KB13_1234 | psd | KB13_1234 | KB13_78 | Conserved hypothetical protein TIGR00044; Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis; Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family. | Phosphatidylserine decarboxylase family protein; Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). | 0.585 |
| KB13_1234 | trmU | KB13_1234 | KB13_364 | Conserved hypothetical protein TIGR00044; Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis; Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family. | tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. | 0.795 |
| KB13_405 | KB13_777 | KB13_405 | KB13_777 | Isocitrate Dehydrogenase (Mutant With Ser 113 Replaced By Asp) (S113D); [CE] COG0473 Isocitrate/isopropylmalate dehydrogenase. | Oxidoreductase, FAD-binding; [C] COG0247 Fe-S oxidoreductase. | 0.657 |
| KB13_405 | ilvB_2 | KB13_405 | KB13_33 | Isocitrate Dehydrogenase (Mutant With Ser 113 Replaced By Asp) (S113D); [CE] COG0473 Isocitrate/isopropylmalate dehydrogenase. | Acetolactate synthase, large subunit, biosynthetic type; [EH] COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase]. | 0.733 |
| KB13_405 | oadA | KB13_405 | KB13_124 | Isocitrate Dehydrogenase (Mutant With Ser 113 Replaced By Asp) (S113D); [CE] COG0473 Isocitrate/isopropylmalate dehydrogenase. | [I] COG4770 Acetyl/propionyl-CoA carboxylase, alpha subunit. | 0.406 |
| KB13_777 | KB13_405 | KB13_777 | KB13_405 | Oxidoreductase, FAD-binding; [C] COG0247 Fe-S oxidoreductase. | Isocitrate Dehydrogenase (Mutant With Ser 113 Replaced By Asp) (S113D); [CE] COG0473 Isocitrate/isopropylmalate dehydrogenase. | 0.657 |
| 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]. | 0.803 |
| KB13_777 | ilvN | KB13_777 | KB13_289 | Oxidoreductase, FAD-binding; [C] COG0247 Fe-S oxidoreductase. | [E] COG0440 Acetolactate synthase, small (regulatory) subunit. | 0.665 |
| KB13_777 | oadA | KB13_777 | KB13_124 | Oxidoreductase, FAD-binding; [C] COG0247 Fe-S oxidoreductase. | [I] COG4770 Acetyl/propionyl-CoA carboxylase, alpha subunit. | 0.795 |
| 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]. | 0.727 |
| 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. | 0.604 |
| 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. | 0.910 |
| 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. | 0.942 |
| ilvB_2 | KB13_1234 | KB13_33 | KB13_1234 | Acetolactate synthase, large subunit, biosynthetic type; [EH] COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase]. | Conserved hypothetical protein TIGR00044; Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis; Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family. | 0.613 |
| ilvB_2 | KB13_405 | KB13_33 | KB13_405 | Acetolactate synthase, large subunit, biosynthetic type; [EH] COG0028 Thiamine pyrophosphate-requiring enzymes [acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase]. | Isocitrate Dehydrogenase (Mutant With Ser 113 Replaced By Asp) (S113D); [CE] COG0473 Isocitrate/isopropylmalate dehydrogenase. | 0.733 |
| 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. | 0.803 |
| 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. | 0.727 |