| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| alsS | ilvA | AGA_2549 | AGA_1448 | Acetolactate synthase I/II/III large subunit; Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Belongs to the TPP enzyme family. | 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. | 0.950 |
| alsS | ilvE-2 | AGA_2549 | AGA_2431 | Acetolactate synthase I/II/III large subunit; Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Belongs to the TPP enzyme family. | Branched-chain amino acid aminotransferase. | 0.450 |
| alsS | ilvH | AGA_2549 | AGA_2285 | Acetolactate synthase I/II/III large subunit; Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Belongs to the TPP enzyme family. | Acetolactate synthase, small subunit, C-terminal. | 0.993 |
| alsS | ilvI | AGA_2549 | AGA_2286 | Acetolactate synthase I/II/III large subunit; Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Belongs to the TPP enzyme family. | Acetolactate synthase I/II/III large subunit; Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain. | 0.950 |
| alsS | leuB | AGA_2549 | AGA_2115 | Acetolactate synthase I/II/III large subunit; Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Belongs to the TPP enzyme family. | 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. | 0.903 |
| ilvA | alsS | AGA_1448 | AGA_2549 | 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. | Acetolactate synthase I/II/III large subunit; Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Belongs to the TPP enzyme family. | 0.950 |
| ilvA | ilvE-2 | AGA_1448 | AGA_2431 | 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. | 0.917 |
| ilvA | ilvH | AGA_1448 | AGA_2285 | 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. | Acetolactate synthase, small subunit, C-terminal. | 0.959 |
| ilvA | ilvI | AGA_1448 | AGA_2286 | 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. | Acetolactate synthase I/II/III large subunit; Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain. | 0.950 |
| ilvA | leuB | AGA_1448 | AGA_2115 | 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. | 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. | 0.891 |
| ilvA | ltaE | AGA_1448 | AGA_2566 | 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. | Threonine aldolase. | 0.883 |
| ilvA | metC | AGA_1448 | AGA_1674 | 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. | Cystathionine beta-lyase. | 0.890 |
| ilvA | metH | AGA_1448 | AGA_206 | 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. | 5-methyltetrahydrofolate--homocysteine methyltransferase; Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate. | 0.937 |
| ilvA | thrC | AGA_1448 | AGA_2080 | 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. | Threonine synthase. | 0.901 |
| ilvA | trpB-2 | AGA_1448 | AGA_824 | 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. | Tryptophan synthase beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.901 |
| ilvE-2 | alsS | AGA_2431 | AGA_2549 | Branched-chain amino acid aminotransferase. | Acetolactate synthase I/II/III large subunit; Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Belongs to the TPP enzyme family. | 0.450 |
| ilvE-2 | ilvA | AGA_2431 | AGA_1448 | Branched-chain amino acid aminotransferase. | 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. | 0.917 |
| ilvE-2 | ilvH | AGA_2431 | AGA_2285 | Branched-chain amino acid aminotransferase. | Acetolactate synthase, small subunit, C-terminal. | 0.724 |
| ilvE-2 | ilvI | AGA_2431 | AGA_2286 | Branched-chain amino acid aminotransferase. | Acetolactate synthase I/II/III large subunit; Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain. | 0.450 |
| ilvE-2 | metC | AGA_2431 | AGA_1674 | Branched-chain amino acid aminotransferase. | Cystathionine beta-lyase. | 0.594 |
