node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
THII_0196 | THII_3387 | THII_0196 | THII_3387 | Aspartate kinase, monofunctional class; Belongs to the aspartokinase family. | Prephenate dehydratase. | 0.623 |
THII_0196 | THII_3397 | THII_0196 | THII_3397 | Aspartate kinase, monofunctional class; Belongs to the aspartokinase family. | Homoserine dehydrogenase. | 0.963 |
THII_0196 | ilvA | THII_0196 | THII_1249 | Aspartate kinase, monofunctional class; Belongs to the aspartokinase 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. | 0.455 |
THII_0249 | THII_1495 | THII_0249 | THII_1495 | (p)ppGpp synthetase, RelA/SpoT family; In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. | RelA/SpoT family protein; In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. | 0.916 |
THII_1495 | THII_0249 | THII_1495 | THII_0249 | RelA/SpoT family protein; In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. | (p)ppGpp synthetase, RelA/SpoT family; In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. | 0.916 |
THII_2331 | THII_3387 | THII_2331 | THII_3387 | Acetolactate synthase, small subunit. | Prephenate dehydratase. | 0.716 |
THII_2331 | THII_3397 | THII_2331 | THII_3397 | Acetolactate synthase, small subunit. | Homoserine dehydrogenase. | 0.834 |
THII_2331 | ilvA | THII_2331 | THII_1249 | Acetolactate synthase, small subunit. | 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. | 0.980 |
THII_3387 | THII_0196 | THII_3387 | THII_0196 | Prephenate dehydratase. | Aspartate kinase, monofunctional class; Belongs to the aspartokinase family. | 0.623 |
THII_3387 | THII_2331 | THII_3387 | THII_2331 | Prephenate dehydratase. | Acetolactate synthase, small subunit. | 0.716 |
THII_3387 | THII_3397 | THII_3387 | THII_3397 | Prephenate dehydratase. | Homoserine dehydrogenase. | 0.571 |
THII_3387 | ilvA | THII_3387 | THII_1249 | Prephenate dehydratase. | 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. | 0.500 |
THII_3397 | THII_0196 | THII_3397 | THII_0196 | Homoserine dehydrogenase. | Aspartate kinase, monofunctional class; Belongs to the aspartokinase family. | 0.963 |
THII_3397 | THII_2331 | THII_3397 | THII_2331 | Homoserine dehydrogenase. | Acetolactate synthase, small subunit. | 0.834 |
THII_3397 | THII_3387 | THII_3397 | THII_3387 | Homoserine dehydrogenase. | Prephenate dehydratase. | 0.571 |
THII_3397 | ilvA | THII_3397 | THII_1249 | Homoserine dehydrogenase. | 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. | 0.543 |
ilvA | THII_0196 | THII_1249 | THII_0196 | 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. | Aspartate kinase, monofunctional class; Belongs to the aspartokinase family. | 0.455 |
ilvA | THII_2331 | THII_1249 | THII_2331 | 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. | 0.980 |
ilvA | THII_3387 | THII_1249 | THII_3387 | 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. | Prephenate dehydratase. | 0.500 |
ilvA | THII_3397 | THII_1249 | THII_3397 | 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. | Homoserine dehydrogenase. | 0.543 |