node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
BU064_01845 | ilvA | GCA_001902315_02298 | GCA_001902315_00098 | Unannotated protein; Belongs to the TPP enzyme family. | Unannotated protein; 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. | 0.737 |
BU064_01845 | ilvB | GCA_001902315_02298 | GCA_001902315_00105 | Unannotated protein; Belongs to the TPP enzyme family. | Unannotated protein. | 0.910 |
BU064_01845 | ilvC | GCA_001902315_02298 | GCA_001902315_00103 | Unannotated protein; Belongs to the TPP enzyme family. | Unannotated protein; 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. | 0.937 |
BU064_01845 | ilvD | GCA_001902315_02298 | GCA_001902315_00106 | Unannotated protein; Belongs to the TPP enzyme family. | Unannotated protein; Belongs to the IlvD/Edd family. | 0.776 |
BU064_01845 | ilvN | GCA_001902315_02298 | GCA_001902315_00104 | Unannotated protein; Belongs to the TPP enzyme family. | Unannotated protein. | 0.994 |
BU064_01845 | leuA | GCA_001902315_02298 | GCA_001902315_00102 | Unannotated protein; Belongs to the TPP enzyme family. | Unannotated protein; 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. | 0.951 |
BU064_01845 | leuB | GCA_001902315_02298 | GCA_001902315_00101 | Unannotated protein; Belongs to the TPP enzyme family. | Unannotated protein; 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. | 0.800 |
BU064_01845 | leuC | GCA_001902315_02298 | GCA_001902315_00100 | Unannotated protein; Belongs to the TPP enzyme family. | Unannotated protein; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.941 |
BU064_01845 | leuD | GCA_001902315_02298 | GCA_001902315_00099 | Unannotated protein; Belongs to the TPP enzyme family. | Unannotated protein; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily. | 0.946 |
BU064_01845 | pyk | GCA_001902315_02298 | GCA_001902315_00387 | Unannotated protein; Belongs to the TPP enzyme family. | Unannotated protein; Belongs to the pyruvate kinase family. | 0.930 |
ilvA | BU064_01845 | GCA_001902315_00098 | GCA_001902315_02298 | Unannotated protein; 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. | Unannotated protein; Belongs to the TPP enzyme family. | 0.737 |
ilvA | ilvB | GCA_001902315_00098 | GCA_001902315_00105 | Unannotated protein; 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. | Unannotated protein. | 0.992 |
ilvA | ilvC | GCA_001902315_00098 | GCA_001902315_00103 | Unannotated protein; 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. | Unannotated protein; 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. | 0.901 |
ilvA | ilvD | GCA_001902315_00098 | GCA_001902315_00106 | Unannotated protein; 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. | Unannotated protein; Belongs to the IlvD/Edd family. | 0.948 |
ilvA | ilvN | GCA_001902315_00098 | GCA_001902315_00104 | Unannotated protein; 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. | Unannotated protein. | 0.995 |
ilvA | leuA | GCA_001902315_00098 | GCA_001902315_00102 | Unannotated protein; 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. | Unannotated protein; 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. | 0.890 |
ilvA | leuB | GCA_001902315_00098 | GCA_001902315_00101 | Unannotated protein; 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. | Unannotated protein; 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. | 0.988 |
ilvA | leuC | GCA_001902315_00098 | GCA_001902315_00100 | Unannotated protein; 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. | Unannotated protein; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.890 |
ilvA | leuD | GCA_001902315_00098 | GCA_001902315_00099 | Unannotated protein; 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. | Unannotated protein; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily. | 0.903 |
ilvB | BU064_01845 | GCA_001902315_00105 | GCA_001902315_02298 | Unannotated protein. | Unannotated protein; Belongs to the TPP enzyme family. | 0.910 |