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 |
| Rfer_0344 | Rfer_0929 | Rfer_0344 | Rfer_0929 | L-threonine ammonia-lyase; 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. | D-serine deaminase. | 0.905 |
| Rfer_0344 | Rfer_0964 | Rfer_0344 | Rfer_0964 | L-threonine ammonia-lyase; 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. | D-serine deaminase. | 0.905 |
| Rfer_0344 | Rfer_1084 | Rfer_0344 | Rfer_1084 | L-threonine ammonia-lyase; 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-serine ammonia-lyase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.926 |
| Rfer_0344 | Rfer_2144 | Rfer_0344 | Rfer_2144 | L-threonine ammonia-lyase; 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. | D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding. | 0.834 |
| Rfer_0344 | Rfer_2552 | Rfer_0344 | Rfer_2552 | L-threonine ammonia-lyase; 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 I. | 0.831 |
| Rfer_0344 | Rfer_2801 | Rfer_0344 | Rfer_2801 | L-threonine ammonia-lyase; 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. | 0.825 |
| Rfer_0344 | Rfer_3829 | Rfer_0344 | Rfer_3829 | L-threonine ammonia-lyase; 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. | D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding. | 0.849 |
| Rfer_0344 | ilvA | Rfer_0344 | Rfer_0733 | L-threonine ammonia-lyase; 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 ammonia-lyase; 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. | 0.915 |
| Rfer_0927 | Rfer_0929 | Rfer_0927 | Rfer_0929 | Dihydroorotase. | D-serine deaminase. | 0.914 |
| Rfer_0927 | Rfer_0964 | Rfer_0927 | Rfer_0964 | Dihydroorotase. | D-serine deaminase. | 0.791 |
| Rfer_0929 | Rfer_0344 | Rfer_0929 | Rfer_0344 | D-serine deaminase. | L-threonine ammonia-lyase; 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. | 0.905 |
| Rfer_0929 | Rfer_0927 | Rfer_0929 | Rfer_0927 | D-serine deaminase. | Dihydroorotase. | 0.914 |
| Rfer_0929 | Rfer_0964 | Rfer_0929 | Rfer_0964 | D-serine deaminase. | D-serine deaminase. | 0.904 |
| Rfer_0929 | Rfer_0978 | Rfer_0929 | Rfer_0978 | D-serine deaminase. | N-acyl-D-amino-acid deacylase. | 0.781 |
| Rfer_0929 | Rfer_1084 | Rfer_0929 | Rfer_1084 | D-serine deaminase. | L-serine ammonia-lyase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.904 |
| Rfer_0929 | Rfer_2144 | Rfer_0929 | Rfer_2144 | D-serine deaminase. | D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding. | 0.808 |
| Rfer_0929 | Rfer_2552 | Rfer_0929 | Rfer_2552 | D-serine deaminase. | Glyoxalase I. | 0.808 |
| Rfer_0929 | Rfer_2801 | Rfer_0929 | Rfer_2801 | D-serine deaminase. | Lactoylglutathione lyase. | 0.808 |
| Rfer_0929 | Rfer_3829 | Rfer_0929 | Rfer_3829 | D-serine deaminase. | D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding. | 0.800 |
| Rfer_0929 | ilvA | Rfer_0929 | Rfer_0733 | D-serine deaminase. | L-threonine ammonia-lyase; 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. | 0.905 |
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