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 |
| FAES_0177 | FAES_0257 | FAES_0177 | FAES_0257 | Hypothetical protein. | Glyoxalase/bleomycin resistance protein/dioxygenase. | 0.900 |
| FAES_0177 | FAES_1143 | FAES_0177 | FAES_1143 | Hypothetical protein. | Lactoylglutathione lyase. | 0.900 |
| FAES_0177 | FAES_3578 | FAES_0177 | FAES_3578 | Hypothetical protein. | Serine dehydratase alpha chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.800 |
| FAES_0177 | ilvA | FAES_0177 | FAES_4922 | Hypothetical protein. | 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. | 0.800 |
| FAES_0257 | FAES_0177 | FAES_0257 | FAES_0177 | Glyoxalase/bleomycin resistance protein/dioxygenase. | Hypothetical protein. | 0.900 |
| FAES_0257 | FAES_1143 | FAES_0257 | FAES_1143 | Glyoxalase/bleomycin resistance protein/dioxygenase. | Lactoylglutathione lyase. | 0.900 |
| FAES_0257 | FAES_3578 | FAES_0257 | FAES_3578 | Glyoxalase/bleomycin resistance protein/dioxygenase. | Serine dehydratase alpha chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.801 |
| FAES_0257 | ilvA | FAES_0257 | FAES_4922 | Glyoxalase/bleomycin resistance protein/dioxygenase. | 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. | 0.808 |
| FAES_1143 | FAES_0177 | FAES_1143 | FAES_0177 | Lactoylglutathione lyase. | Hypothetical protein. | 0.900 |
| FAES_1143 | FAES_0257 | FAES_1143 | FAES_0257 | Lactoylglutathione lyase. | Glyoxalase/bleomycin resistance protein/dioxygenase. | 0.900 |
| FAES_1143 | FAES_3578 | FAES_1143 | FAES_3578 | Lactoylglutathione lyase. | Serine dehydratase alpha chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.801 |
| FAES_1143 | ilvA | FAES_1143 | FAES_4922 | Lactoylglutathione lyase. | 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. | 0.808 |
| FAES_3578 | FAES_0177 | FAES_3578 | FAES_0177 | Serine dehydratase alpha chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Hypothetical protein. | 0.800 |
| FAES_3578 | FAES_0257 | FAES_3578 | FAES_0257 | Serine dehydratase alpha chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Glyoxalase/bleomycin resistance protein/dioxygenase. | 0.801 |
| FAES_3578 | FAES_1143 | FAES_3578 | FAES_1143 | Serine dehydratase alpha chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Lactoylglutathione lyase. | 0.801 |
| FAES_3578 | ilvA | FAES_3578 | FAES_4922 | Serine dehydratase alpha chain; Belongs to the iron-sulfur dependent L-serine dehydratase 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. | 0.925 |
| ilvA | FAES_0177 | FAES_4922 | FAES_0177 | 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. | Hypothetical protein. | 0.800 |
| ilvA | FAES_0257 | FAES_4922 | FAES_0257 | 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. | Glyoxalase/bleomycin resistance protein/dioxygenase. | 0.808 |
| ilvA | FAES_1143 | FAES_4922 | FAES_1143 | 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. | Lactoylglutathione lyase. | 0.808 |
| ilvA | FAES_3578 | FAES_4922 | FAES_3578 | 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. | Serine dehydratase alpha chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.925 |