| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ilvA | leuD1 | VME0621_04970 | VME0621_02248 | L-threonine dehydratase biosynthetic IlvA; 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 dehydratase small subunit 1; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily. | 0.629 |
| ilvA | ltaE | VME0621_04970 | VME0621_00146 | L-threonine dehydratase biosynthetic IlvA; 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. | Low specificity L-threonine aldolase. | 0.926 |
| ilvA | metL | VME0621_04970 | VME0621_04398 | L-threonine dehydratase biosynthetic IlvA; 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. | Bifunctional aspartokinase/homoserine dehydrogenase 2; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.682 |
| ilvA | tdh | VME0621_04970 | VME0621_00338 | L-threonine dehydratase biosynthetic IlvA; 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. | L-threonine 3-dehydrogenase; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate; Belongs to the zinc-containing alcohol dehydrogenase family. | 0.907 |
| ilvA | thrA | VME0621_04970 | VME0621_04086 | L-threonine dehydratase biosynthetic IlvA; 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. | Bifunctional aspartokinase/homoserine dehydrogenase 1; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.682 |
| ilvA | thrB | VME0621_04970 | VME0621_04085 | L-threonine dehydratase biosynthetic IlvA; 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. | Homoserine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. | 0.456 |
| ilvA | thrC | VME0621_04970 | VME0621_04084 | L-threonine dehydratase biosynthetic IlvA; 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. | 0.957 |
| leuD1 | ilvA | VME0621_02248 | VME0621_04970 | 3-isopropylmalate dehydratase small subunit 1; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily. | L-threonine dehydratase biosynthetic IlvA; 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. | 0.629 |
| leuD1 | metL | VME0621_02248 | VME0621_04398 | 3-isopropylmalate dehydratase small subunit 1; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily. | Bifunctional aspartokinase/homoserine dehydrogenase 2; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.753 |
| leuD1 | thrA | VME0621_02248 | VME0621_04086 | 3-isopropylmalate dehydratase small subunit 1; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily. | Bifunctional aspartokinase/homoserine dehydrogenase 1; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.753 |
| leuD1 | thrB | VME0621_02248 | VME0621_04085 | 3-isopropylmalate dehydratase small subunit 1; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily. | Homoserine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. | 0.686 |
| leuD1 | thrC | VME0621_02248 | VME0621_04084 | 3-isopropylmalate dehydratase small subunit 1; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily. | Threonine synthase. | 0.912 |
| ltaE | ilvA | VME0621_00146 | VME0621_04970 | Low specificity L-threonine aldolase. | L-threonine dehydratase biosynthetic IlvA; 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. | 0.926 |
| ltaE | tdh | VME0621_00146 | VME0621_00338 | Low specificity L-threonine aldolase. | L-threonine 3-dehydrogenase; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate; Belongs to the zinc-containing alcohol dehydrogenase family. | 0.904 |
| ltaE | thrC | VME0621_00146 | VME0621_04084 | Low specificity L-threonine aldolase. | Threonine synthase. | 0.927 |
| metL | ilvA | VME0621_04398 | VME0621_04970 | Bifunctional aspartokinase/homoserine dehydrogenase 2; In the C-terminal section; belongs to the homoserine dehydrogenase family. | L-threonine dehydratase biosynthetic IlvA; 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. | 0.682 |
| metL | leuD1 | VME0621_04398 | VME0621_02248 | Bifunctional aspartokinase/homoserine dehydrogenase 2; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 3-isopropylmalate dehydratase small subunit 1; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily. | 0.753 |
| metL | serC_1 | VME0621_04398 | VME0621_03610 | Bifunctional aspartokinase/homoserine dehydrogenase 2; In the C-terminal section; belongs to the homoserine dehydrogenase family. | Phosphoserine aminotransferase; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine. | 0.662 |
| metL | serC_2 | VME0621_04398 | VME0621_04028 | Bifunctional aspartokinase/homoserine dehydrogenase 2; In the C-terminal section; belongs to the homoserine dehydrogenase family. | Phosphoserine aminotransferase; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily. | 0.662 |
| metL | thrA | VME0621_04398 | VME0621_04086 | Bifunctional aspartokinase/homoserine dehydrogenase 2; In the C-terminal section; belongs to the homoserine dehydrogenase family. | Bifunctional aspartokinase/homoserine dehydrogenase 1; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.997 |