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 |
| bkdA1 | bkdA2 | Atu3473 | Atu3472 | 2-oxoisovalerate dehydrogenase alpha subunit. | 2-oxoisovalerate dehydrogenase beta subunit. | 0.999 |
| bkdA1 | ilvA | Atu3473 | Atu1205 | 2-oxoisovalerate dehydrogenase alpha 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. | 0.810 |
| bkdA1 | ilvE | Atu3473 | Atu0871 | 2-oxoisovalerate dehydrogenase alpha subunit. | Branched-chain-amino-acid aminotransferase. | 0.912 |
| bkdA2 | bkdA1 | Atu3472 | Atu3473 | 2-oxoisovalerate dehydrogenase beta subunit. | 2-oxoisovalerate dehydrogenase alpha subunit. | 0.999 |
| bkdA2 | ilvA | Atu3472 | Atu1205 | 2-oxoisovalerate dehydrogenase beta 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. | 0.810 |
| bkdA2 | ilvE | Atu3472 | Atu0871 | 2-oxoisovalerate dehydrogenase beta subunit. | Branched-chain-amino-acid aminotransferase. | 0.918 |
| gsh1 | ilvE | Atu0656 | Atu0871 | Glutamate-cysteine ligase; Catalyzes the synthesis of gamma-glutamylcysteine (gamma-GC). Belongs to the glutamate--cysteine ligase type 2 family. EgtA subfamily. | Branched-chain-amino-acid aminotransferase. | 0.900 |
| hom | ilvA | Atu1588 | Atu1205 | 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. | 0.429 |
| hom | ilvD | Atu1588 | Atu1918 | Homoserine dehydrogenase. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.421 |
| hom | ilvE | Atu1588 | Atu0871 | Homoserine dehydrogenase. | Branched-chain-amino-acid aminotransferase. | 0.876 |
| ilvA | bkdA1 | Atu1205 | Atu3473 | 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. | 2-oxoisovalerate dehydrogenase alpha subunit. | 0.810 |
| ilvA | bkdA2 | Atu1205 | Atu3472 | 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. | 2-oxoisovalerate dehydrogenase beta subunit. | 0.810 |
| ilvA | hom | Atu1205 | Atu1588 | 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. | 0.429 |
| ilvA | ilvD | Atu1205 | Atu1918 | 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. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.809 |
| ilvA | ilvD-3 | Atu1205 | Atu3219 | 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. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.783 |
| ilvA | ilvD-4 | Atu1205 | Atu3971 | 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. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.839 |
| ilvA | ilvE | Atu1205 | Atu0871 | 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. | 0.872 |
| ilvD | hom | Atu1918 | Atu1588 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | Homoserine dehydrogenase. | 0.421 |
| ilvD | ilvA | Atu1918 | Atu1205 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd 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. | 0.809 |
| ilvD | ilvD-3 | Atu1918 | Atu3219 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.916 |
page 1 of 3