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 |
| LuPra_03597 | LuPra_06195 | LuPra_03597 | LuPra_06195 | Putative epimerase/dehydratase. | 8-amino-7-oxononanoate synthase/2-amino-3-ketobutyrate coenzyme A ligase. | 0.962 |
| LuPra_03597 | ilvA | LuPra_03597 | LuPra_04592 | Putative epimerase/dehydratase. | L-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. | 0.900 |
| LuPra_03597 | ltaA_1 | LuPra_03597 | LuPra_05446 | Putative epimerase/dehydratase. | L-allo-threonine aldolase. | 0.900 |
| LuPra_03597 | ltaA_2 | LuPra_03597 | LuPra_05703 | Putative epimerase/dehydratase. | L-allo-threonine aldolase. | 0.900 |
| LuPra_03597 | tdcB_1 | LuPra_03597 | LuPra_05890 | Putative epimerase/dehydratase. | L-threonine dehydratase catabolic TdcB. | 0.900 |
| LuPra_03597 | tdcB_2 | LuPra_03597 | LuPra_06028 | Putative epimerase/dehydratase. | L-threonine dehydratase catabolic TdcB. | 0.900 |
| LuPra_03597 | thrC_2 | LuPra_03597 | LuPra_04610 | Putative epimerase/dehydratase. | Threonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. | 0.900 |
| LuPra_06195 | LuPra_03597 | LuPra_06195 | LuPra_03597 | 8-amino-7-oxononanoate synthase/2-amino-3-ketobutyrate coenzyme A ligase. | Putative epimerase/dehydratase. | 0.962 |
| LuPra_06195 | ltaA_1 | LuPra_06195 | LuPra_05446 | 8-amino-7-oxononanoate synthase/2-amino-3-ketobutyrate coenzyme A ligase. | L-allo-threonine aldolase. | 0.917 |
| LuPra_06195 | ltaA_2 | LuPra_06195 | LuPra_05703 | 8-amino-7-oxononanoate synthase/2-amino-3-ketobutyrate coenzyme A ligase. | L-allo-threonine aldolase. | 0.917 |
| LuPra_06195 | pucG | LuPra_06195 | LuPra_02136 | 8-amino-7-oxononanoate synthase/2-amino-3-ketobutyrate coenzyme A ligase. | Purine catabolism protein PucG. | 0.919 |
| LuPra_06195 | soxA | LuPra_06195 | LuPra_05660 | 8-amino-7-oxononanoate synthase/2-amino-3-ketobutyrate coenzyme A ligase. | Monomeric sarcosine oxidase. | 0.914 |
| ilvA | LuPra_03597 | LuPra_04592 | LuPra_03597 | L-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. | Putative epimerase/dehydratase. | 0.900 |
| ilvA | ltaA_1 | LuPra_04592 | LuPra_05446 | L-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. | L-allo-threonine aldolase. | 0.908 |
| ilvA | ltaA_2 | LuPra_04592 | LuPra_05703 | L-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. | L-allo-threonine aldolase. | 0.908 |
| ilvA | metX_1 | LuPra_04592 | LuPra_00060 | L-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. | Homoserine O-acetyltransferase; Belongs to the AB hydrolase superfamily. MetX family. | 0.813 |
| ilvA | metX_2 | LuPra_04592 | LuPra_02943 | L-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. | Homoserine O-acetyltransferase; Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine. | 0.813 |
| ilvA | pucG | LuPra_04592 | LuPra_02136 | L-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. | Purine catabolism protein PucG. | 0.922 |
| ilvA | sdaB_1 | LuPra_04592 | LuPra_02220 | L-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. | L-serine dehydratase 2. | 0.914 |
| ilvA | sdaB_2 | LuPra_04592 | LuPra_03332 | L-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. | L-serine dehydratase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.914 |
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