Export your current network:
... as a vector graphic:
SVG: scalable vector graphic - can be opened and edited in Illustrator, CorelDraw, Dia, etc
... as short tabular text output:
TSV: tab separated values - can be opened in Excel and Cytoscape (lists only one-way edges: A-B)
... as tabular text output:
TSV: tab separated values - can be opened in Excel (lists reciprocal edges: A-B,B-A)
... as an XML summary:
structured XML interaction data, according to the 'PSI-MI' data standard
... protein node degrees:
node degree of proteins in your network (given the current score cut-off)
... network coordinates:
a flat-file format describing the coordinates and colors of nodes in the network
... protein sequences:
MFA: multi-fasta format - containing the aminoacid sequences in the network
... protein annotations:
a tab-delimited file describing the names, domains and descriptions of proteins in your network
... functional annotations:
a tab-delimited file containing all known functional terms of proteins in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| hom | ilvA-I | PP_1470 | PP_3446 | Homoserine dehydrogenase. | 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. | 0.849 |
| hom | ilvA-II | PP_1470 | PP_5149 | Homoserine dehydrogenase. | 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. | 0.849 |
| hom | ilvH | PP_1470 | PP_4679 | Homoserine dehydrogenase. | Acetohydroxybutanoate synthase / acetolactate synthase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Aminoacidbiosynthesis : Pyruvate family. | 0.815 |
| hom | lysC | PP_1470 | PP_4473 | Homoserine dehydrogenase. | Aspartokinase; Involved in the biosynthesis of L-aspartate-beta-semialdehyde which is a central intermediate in the biosynthesis of different amino acids (L-lysine, L-methionine, L-threonine). Catalyzes the phosphorylation of the beta-carboxyl group of L-aspartate to yield 4- phospho-L-aspartate. | 0.984 |
| hom | pheA | PP_1470 | PP_1769 | Homoserine dehydrogenase. | Chorismate mutase/Prephenate dehydratase; Function of strongly homologous gene; enzyme. | 0.875 |
| hom | serA | PP_1470 | PP_5155 | Homoserine dehydrogenase. | D-3-phosphoglycerate dehydrogenase / alpha-ketoglutarate reductase; Function experimentally demonstrated in the studied species; enzyme; Aminoacidbiosynthesis : Serine family; Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. | 0.713 |
| ilvA-I | hom | PP_3446 | PP_1470 | 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. | Homoserine dehydrogenase. | 0.849 |
| ilvA-I | ilvA-II | PP_3446 | PP_5149 | 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. | 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. | 0.901 |
| ilvA-I | ilvH | PP_3446 | PP_4679 | 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. | Acetohydroxybutanoate synthase / acetolactate synthase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Aminoacidbiosynthesis : Pyruvate family. | 0.904 |
| ilvA-I | serB | PP_3446 | PP_4909 | 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. | Phosphoserine phosphatase; Function experimentally demonstrated in the studied genus; enzyme; Aminoacidbiosynthesis : Serine family. | 0.909 |
| ilvA-II | hom | PP_5149 | PP_1470 | 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. | Homoserine dehydrogenase. | 0.849 |
| ilvA-II | ilvA-I | PP_5149 | PP_3446 | 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. | 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. | 0.901 |
| ilvA-II | ilvH | PP_5149 | PP_4679 | 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. | Acetohydroxybutanoate synthase / acetolactate synthase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Aminoacidbiosynthesis : Pyruvate family. | 0.903 |
| ilvA-II | serB | PP_5149 | PP_4909 | 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. | Phosphoserine phosphatase; Function experimentally demonstrated in the studied genus; enzyme; Aminoacidbiosynthesis : Serine family. | 0.909 |
| ilvH | hom | PP_4679 | PP_1470 | Acetohydroxybutanoate synthase / acetolactate synthase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Aminoacidbiosynthesis : Pyruvate family. | Homoserine dehydrogenase. | 0.815 |
| ilvH | ilvA-I | PP_4679 | PP_3446 | Acetohydroxybutanoate synthase / acetolactate synthase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Aminoacidbiosynthesis : Pyruvate family. | 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. | 0.904 |
| ilvH | ilvA-II | PP_4679 | PP_5149 | Acetohydroxybutanoate synthase / acetolactate synthase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Aminoacidbiosynthesis : Pyruvate family. | 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. | 0.903 |
| ilvH | pheA | PP_4679 | PP_1769 | Acetohydroxybutanoate synthase / acetolactate synthase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Aminoacidbiosynthesis : Pyruvate family. | Chorismate mutase/Prephenate dehydratase; Function of strongly homologous gene; enzyme. | 0.781 |
| ilvH | serA | PP_4679 | PP_5155 | Acetohydroxybutanoate synthase / acetolactate synthase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Aminoacidbiosynthesis : Pyruvate family. | D-3-phosphoglycerate dehydrogenase / alpha-ketoglutarate reductase; Function experimentally demonstrated in the studied species; enzyme; Aminoacidbiosynthesis : Serine family; Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. | 0.412 |
| lysC | hom | PP_4473 | PP_1470 | Aspartokinase; Involved in the biosynthesis of L-aspartate-beta-semialdehyde which is a central intermediate in the biosynthesis of different amino acids (L-lysine, L-methionine, L-threonine). Catalyzes the phosphorylation of the beta-carboxyl group of L-aspartate to yield 4- phospho-L-aspartate. | Homoserine dehydrogenase. | 0.984 |
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