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 |
| bkdA2 | ilvA | SO_2340 | SO_4344 | 3-methyl-2-oxobutanoate dehydrogenase complex E1 component beta subunit BkdA2. | Threonine dehydratase IlvA; 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. | 0.830 |
| bkdA2 | ilvE | SO_2340 | SO_0340 | 3-methyl-2-oxobutanoate dehydrogenase complex E1 component beta subunit BkdA2. | Branched-chain-amino-acid transaminase IlvE. | 0.927 |
| bkdA2 | ldh | SO_2340 | SO_2638 | 3-methyl-2-oxobutanoate dehydrogenase complex E1 component beta subunit BkdA2. | Leucine dehydrogenase Ldh. | 0.959 |
| ilvA | bkdA2 | SO_4344 | SO_2340 | Threonine dehydratase IlvA; 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. | 3-methyl-2-oxobutanoate dehydrogenase complex E1 component beta subunit BkdA2. | 0.830 |
| ilvA | ilvD | SO_4344 | SO_4345 | Threonine dehydratase IlvA; 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 IlvD; Belongs to the IlvD/Edd family. | 0.986 |
| ilvA | ilvE | SO_4344 | SO_0340 | Threonine dehydratase IlvA; 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 transaminase IlvE. | 0.927 |
| ilvA | leuA | SO_4344 | SO_4236 | Threonine dehydratase IlvA; 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. | 2-isopropylmalate synthase LeuA; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily. | 0.469 |
| ilvA | metL | SO_4344 | SO_4055 | Threonine dehydratase IlvA; 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. | Bifunctional aspartokinase II/homoserine dehydrogenase methionine-sensitive MetL; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.803 |
| ilvA | thrA | SO_4344 | SO_3415 | Threonine dehydratase IlvA; 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. | Bifunctional aspartokinase I / homoserine dehydrogenase I ThrA; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.798 |
| ilvA | thrB | SO_4344 | SO_3414 | Threonine dehydratase IlvA; 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 kinase ThrB; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. | 0.599 |
| ilvD | ilvA | SO_4345 | SO_4344 | Dihydroxy-acid dehydratase IlvD; Belongs to the IlvD/Edd family. | Threonine dehydratase IlvA; 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 |
| ilvD | ilvE | SO_4345 | SO_0340 | Dihydroxy-acid dehydratase IlvD; Belongs to the IlvD/Edd family. | Branched-chain-amino-acid transaminase IlvE. | 0.994 |
| ilvD | ldh | SO_4345 | SO_2638 | Dihydroxy-acid dehydratase IlvD; Belongs to the IlvD/Edd family. | Leucine dehydrogenase Ldh. | 0.915 |
| ilvD | leuA | SO_4345 | SO_4236 | Dihydroxy-acid dehydratase IlvD; Belongs to the IlvD/Edd family. | 2-isopropylmalate synthase LeuA; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily. | 0.984 |
| ilvD | metL | SO_4345 | SO_4055 | Dihydroxy-acid dehydratase IlvD; Belongs to the IlvD/Edd family. | Bifunctional aspartokinase II/homoserine dehydrogenase methionine-sensitive MetL; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.687 |
| ilvD | panB | SO_4345 | SO_0870 | Dihydroxy-acid dehydratase IlvD; Belongs to the IlvD/Edd family. | 3-methyl-2-oxobutanoate hydroxymethyltransferase PanB; Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha- ketoisovalerate to form ketopantoate; Belongs to the PanB family. | 0.922 |
| ilvD | thrA | SO_4345 | SO_3415 | Dihydroxy-acid dehydratase IlvD; Belongs to the IlvD/Edd family. | Bifunctional aspartokinase I / homoserine dehydrogenase I ThrA; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.721 |
| ilvD | thrB | SO_4345 | SO_3414 | Dihydroxy-acid dehydratase IlvD; Belongs to the IlvD/Edd family. | Homoserine kinase ThrB; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. | 0.887 |
| ilvD | yfbQ | SO_4345 | SO_2483 | Dihydroxy-acid dehydratase IlvD; Belongs to the IlvD/Edd family. | PLP-dependent aminotransferase YfbQ. | 0.927 |
| ilvE | bkdA2 | SO_0340 | SO_2340 | Branched-chain-amino-acid transaminase IlvE. | 3-methyl-2-oxobutanoate dehydrogenase complex E1 component beta subunit BkdA2. | 0.927 |
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