| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ilvA | ilvD | plu4681 | plu4682 | Threonine dehydratase biosynthetic (threonine deaminase); 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 (DAD); Belongs to the IlvD/Edd family. | 0.943 |
| ilvA | ilvE | plu4681 | plu4683 | Threonine dehydratase biosynthetic (threonine deaminase); 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 (transaminase B) (BCAT); Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.918 |
| ilvA | ilvE-2 | plu4681 | plu3042 | Threonine dehydratase biosynthetic (threonine deaminase); 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. | 0.856 |
| ilvA | ilvG | plu4681 | plu4685 | Threonine dehydratase biosynthetic (threonine deaminase); 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 isozyme II large subunit (AHAS-II) (acetohydroxy-acid synthase II large subunit) (ALS-II). | 0.963 |
| ilvA | ilvM | plu4681 | plu4684 | Threonine dehydratase biosynthetic (threonine deaminase); 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 isozyme II small subunit (AHAS-II) (acetohydroxy-acid synthase II small subunit) (ALS-II). | 0.956 |
| ilvA | plu1883 | plu4681 | plu1883 | Threonine dehydratase biosynthetic (threonine deaminase); 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. | Transket_pyr domain-containing protein; Unnamed protein product; Similar to 3-methyl-2-oxobutanoate dehydrogenase (lipoamide) alpha/beta E1 chain CP0743. | 0.861 |
| ilvA | plu2795 | plu4681 | plu2795 | Threonine dehydratase biosynthetic (threonine deaminase); 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. | Transket_pyr domain-containing protein; Unnamed protein product; Similar to 3-methyl-2-oxobutanoate dehydrogenase (lipoamide). Putative transmembrane protein. | 0.861 |
| ilvA | thrA | plu4681 | plu0563 | Threonine dehydratase biosynthetic (threonine deaminase); 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. | Aspartokinase I-homoserine dehydrogenase I; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.703 |
| ilvD | ilvA | plu4682 | plu4681 | Dihydroxy-acid dehydratase (DAD); Belongs to the IlvD/Edd family. | Threonine dehydratase biosynthetic (threonine deaminase); 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. | 0.943 |
| ilvD | ilvE | plu4682 | plu4683 | Dihydroxy-acid dehydratase (DAD); Belongs to the IlvD/Edd family. | Branched-chain amino acid aminotransferase (transaminase B) (BCAT); Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.990 |
| ilvD | ilvE-2 | plu4682 | plu3042 | Dihydroxy-acid dehydratase (DAD); 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. | 0.983 |
| ilvD | ilvG | plu4682 | plu4685 | Dihydroxy-acid dehydratase (DAD); Belongs to the IlvD/Edd family. | Acetolactate synthase isozyme II large subunit (AHAS-II) (acetohydroxy-acid synthase II large subunit) (ALS-II). | 0.979 |
| ilvD | ilvM | plu4682 | plu4684 | Dihydroxy-acid dehydratase (DAD); Belongs to the IlvD/Edd family. | Acetolactate synthase isozyme II small subunit (AHAS-II) (acetohydroxy-acid synthase II small subunit) (ALS-II). | 0.936 |
| ilvD | leuA | plu4682 | plu3673 | Dihydroxy-acid dehydratase (DAD); Belongs to the IlvD/Edd family. | 2-isopropylmalate synthase (alpha-isopropylmalate synthase) (alpha-IPM synthetase); 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. | 0.984 |
| ilvD | panB | plu4682 | plu0872 | Dihydroxy-acid dehydratase (DAD); Belongs to the IlvD/Edd family. | 3-methyl-2-oxobutanoate hydroxymethyltransferase; Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha- ketoisovalerate to form ketopantoate; Belongs to the PanB family. | 0.951 |
| ilvD | thrA | plu4682 | plu0563 | Dihydroxy-acid dehydratase (DAD); Belongs to the IlvD/Edd family. | Aspartokinase I-homoserine dehydrogenase I; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.704 |
| ilvE | ilvA | plu4683 | plu4681 | Branched-chain amino acid aminotransferase (transaminase B) (BCAT); Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | Threonine dehydratase biosynthetic (threonine deaminase); 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. | 0.918 |
| ilvE | ilvD | plu4683 | plu4682 | Branched-chain amino acid aminotransferase (transaminase B) (BCAT); Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | Dihydroxy-acid dehydratase (DAD); Belongs to the IlvD/Edd family. | 0.990 |
| ilvE | ilvE-2 | plu4683 | plu3042 | Branched-chain amino acid aminotransferase (transaminase B) (BCAT); Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | Branched-chain-amino-acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.920 |
| ilvE | ilvG | plu4683 | plu4685 | Branched-chain amino acid aminotransferase (transaminase B) (BCAT); Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | Acetolactate synthase isozyme II large subunit (AHAS-II) (acetohydroxy-acid synthase II large subunit) (ALS-II). | 0.937 |
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