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 protiens in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| SEP70506.1 | SEQ03537.1 | SAMN04488558_101395 | SAMN04488558_104113 | 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 dehydratase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.872 |
| SEP70506.1 | SEQ08329.1 | SAMN04488558_101395 | SAMN04488558_10523 | 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. | Aldo/keto reductase. | 0.567 |
| SEP70506.1 | SEQ17911.1 | SAMN04488558_101395 | SAMN04488558_10631 | 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. | 0.928 |
| SEP70506.1 | SEQ25179.1 | SAMN04488558_101395 | SAMN04488558_10738 | 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. | Lactate dehydrogenase; Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. | 0.588 |
| SEP70506.1 | SEQ26264.1 | SAMN04488558_101395 | SAMN04488558_10766 | 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. | Putative intracellular protease/amidase. | 0.535 |
| SEQ03537.1 | SEP70506.1 | SAMN04488558_104113 | SAMN04488558_101395 | L-serine dehydratase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 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. | 0.872 |
| SEQ03537.1 | SEQ17911.1 | SAMN04488558_104113 | SAMN04488558_10631 | L-serine dehydratase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Lactoylglutathione lyase. | 0.894 |
| SEQ03537.1 | SEQ25179.1 | SAMN04488558_104113 | SAMN04488558_10738 | L-serine dehydratase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Lactate dehydrogenase; Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. | 0.555 |
| SEQ03537.1 | SEQ26264.1 | SAMN04488558_104113 | SAMN04488558_10766 | L-serine dehydratase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Putative intracellular protease/amidase. | 0.595 |
| SEQ08329.1 | SEP70506.1 | SAMN04488558_10523 | SAMN04488558_101395 | Aldo/keto reductase. | 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. | 0.567 |
| SEQ08329.1 | SEQ17911.1 | SAMN04488558_10523 | SAMN04488558_10631 | Aldo/keto reductase. | Lactoylglutathione lyase. | 0.701 |
| SEQ08329.1 | SEQ25179.1 | SAMN04488558_10523 | SAMN04488558_10738 | Aldo/keto reductase. | Lactate dehydrogenase; Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. | 0.648 |
| SEQ08329.1 | SEQ26264.1 | SAMN04488558_10523 | SAMN04488558_10766 | Aldo/keto reductase. | Putative intracellular protease/amidase. | 0.420 |
| SEQ08329.1 | SEQ33769.1 | SAMN04488558_10523 | SAMN04488558_10895 | Aldo/keto reductase. | Putative quinone oxidoreductase, YhdH/YhfP family. | 0.797 |
| SEQ17757.1 | SEQ17797.1 | SAMN04488558_10629 | SAMN04488558_10630 | Glutaredoxin-related protein. | Cytidine deaminase; This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis; Belongs to the cytidine and deoxycytidylate deaminase family. | 0.743 |
| SEQ17757.1 | SEQ17911.1 | SAMN04488558_10629 | SAMN04488558_10631 | Glutaredoxin-related protein. | Lactoylglutathione lyase. | 0.630 |
| SEQ17797.1 | SEQ17757.1 | SAMN04488558_10630 | SAMN04488558_10629 | Cytidine deaminase; This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis; Belongs to the cytidine and deoxycytidylate deaminase family. | Glutaredoxin-related protein. | 0.743 |
| SEQ17797.1 | SEQ17911.1 | SAMN04488558_10630 | SAMN04488558_10631 | Cytidine deaminase; This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis; Belongs to the cytidine and deoxycytidylate deaminase family. | Lactoylglutathione lyase. | 0.591 |
| SEQ17911.1 | SEP70506.1 | SAMN04488558_10631 | SAMN04488558_101395 | Lactoylglutathione lyase. | 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. | 0.928 |
| SEQ17911.1 | SEQ03537.1 | SAMN04488558_10631 | SAMN04488558_104113 | Lactoylglutathione lyase. | L-serine dehydratase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.894 |
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