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 |
| AIL72030.1 | ilvA | VV93_v1c29620 | VV93_v1c29660 | Acetolactate synthase 2 catalytic 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. | 0.986 |
| AIL72030.1 | ilvD | VV93_v1c29620 | VV93_v1c29650 | Acetolactate synthase 2 catalytic subunit. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.981 |
| AIL72030.1 | ilvE | VV93_v1c29620 | VV93_v1c29640 | Acetolactate synthase 2 catalytic subunit. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.927 |
| AIL72030.1 | ilvM | VV93_v1c29620 | VV93_v1c29630 | Acetolactate synthase 2 catalytic subunit. | Acetolactate synthase 2 regulatory subunit. | 0.984 |
| ilvA | AIL72030.1 | VV93_v1c29660 | VV93_v1c29620 | 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 2 catalytic subunit. | 0.986 |
| ilvA | ilvD | VV93_v1c29660 | VV93_v1c29650 | 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. | 0.951 |
| ilvA | ilvE | VV93_v1c29660 | VV93_v1c29640 | 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. | 0.977 |
| ilvA | ilvM | VV93_v1c29660 | VV93_v1c29630 | 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 2 regulatory subunit. | 0.982 |
| ilvD | AIL72030.1 | VV93_v1c29650 | VV93_v1c29620 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | Acetolactate synthase 2 catalytic subunit. | 0.981 |
| ilvD | ilvA | VV93_v1c29650 | VV93_v1c29660 | 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. | 0.951 |
| ilvD | ilvE | VV93_v1c29650 | VV93_v1c29640 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.995 |
| ilvD | ilvM | VV93_v1c29650 | VV93_v1c29630 | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | Acetolactate synthase 2 regulatory subunit. | 0.945 |
| ilvE | AIL72030.1 | VV93_v1c29640 | VV93_v1c29620 | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | Acetolactate synthase 2 catalytic subunit. | 0.927 |
| ilvE | ilvA | VV93_v1c29640 | VV93_v1c29660 | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase 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. | 0.977 |
| ilvE | ilvD | VV93_v1c29640 | VV93_v1c29650 | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.995 |
| ilvE | ilvM | VV93_v1c29640 | VV93_v1c29630 | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | Acetolactate synthase 2 regulatory subunit. | 0.921 |
| ilvM | AIL72030.1 | VV93_v1c29630 | VV93_v1c29620 | Acetolactate synthase 2 regulatory subunit. | Acetolactate synthase 2 catalytic subunit. | 0.984 |
| ilvM | ilvA | VV93_v1c29630 | VV93_v1c29660 | Acetolactate synthase 2 regulatory 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. | 0.982 |
| ilvM | ilvD | VV93_v1c29630 | VV93_v1c29650 | Acetolactate synthase 2 regulatory subunit. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.945 |
| ilvM | ilvE | VV93_v1c29630 | VV93_v1c29640 | Acetolactate synthase 2 regulatory subunit. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.921 |