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 |
| ilvA | ilvB | EV102420_29_00220 | EV102420_20_00150 | 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. | Acetolactate synthase I large subunit. | 0.907 |
| ilvA | ilvD | EV102420_29_00220 | EV102420_29_00230 | 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. | 0.978 |
| ilvA | ilvE | EV102420_29_00220 | EV102420_29_00240 | 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; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.954 |
| ilvA | ilvG | EV102420_29_00220 | EV102420_29_00260 | 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. | Acetolactate synthase II large subunit. | 0.962 |
| ilvA | ilvH | EV102420_29_00220 | EV102420_08_02770 | 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. | Acetolactate synthase III small subunit. | 0.974 |
| ilvA | ilvI | EV102420_29_00220 | EV102420_08_02760 | 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. | Acetolactate synthase III large subunit. | 0.908 |
| ilvA | ilvM | EV102420_29_00220 | EV102420_29_00250 | 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. | Acetolactate synthase II small subunit. | 0.957 |
| ilvA | ilvN | EV102420_29_00220 | EV102420_20_00140 | 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. | Acetolactate synthase I small subunit. | 0.967 |
| ilvA | metL | EV102420_29_00220 | EV102420_25_00760 | 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. | Aspartokinase/homoserine dehydrogenase MetL; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.893 |
| ilvA | thrC | EV102420_29_00220 | EV102420_02_03570 | 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. | Threonine synthase. | 0.963 |
| ilvB | ilvA | EV102420_20_00150 | EV102420_29_00220 | Acetolactate synthase I large 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. | 0.907 |
| ilvB | ilvD | EV102420_20_00150 | EV102420_29_00230 | Acetolactate synthase I large subunit. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.916 |
| ilvB | ilvE | EV102420_20_00150 | EV102420_29_00240 | Acetolactate synthase I large subunit. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.739 |
| ilvB | ilvG | EV102420_20_00150 | EV102420_29_00260 | Acetolactate synthase I large subunit. | Acetolactate synthase II large subunit. | 0.702 |
| ilvB | ilvH | EV102420_20_00150 | EV102420_08_02770 | Acetolactate synthase I large subunit. | Acetolactate synthase III small subunit. | 0.996 |
| ilvB | ilvI | EV102420_20_00150 | EV102420_08_02760 | Acetolactate synthase I large subunit. | Acetolactate synthase III large subunit. | 0.710 |
| ilvB | ilvM | EV102420_20_00150 | EV102420_29_00250 | Acetolactate synthase I large subunit. | Acetolactate synthase II small subunit. | 0.833 |
| ilvB | ilvN | EV102420_20_00150 | EV102420_20_00140 | Acetolactate synthase I large subunit. | Acetolactate synthase I small subunit. | 0.999 |
| ilvB | metL | EV102420_20_00150 | EV102420_25_00760 | Acetolactate synthase I large subunit. | Aspartokinase/homoserine dehydrogenase MetL; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.413 |
| ilvB | thrC | EV102420_20_00150 | EV102420_02_03570 | Acetolactate synthase I large subunit. | Threonine synthase. | 0.423 |
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