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 |
| ilvA | ilvB1 | LEPBI_I1590 | LEPBI_I0792 | Threonine dehydratase biosynthetic; 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. | AHAS-I; Acetohydroxy-acid synthase I large subunit; ALS-I; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.950 |
| ilvA | ilvB2 | LEPBI_I1590 | LEPBI_I2362 | Threonine dehydratase biosynthetic; 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. | AHAS; Acetohydroxy-acid synthase large subunit; ALS); Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.951 |
| ilvA | ilvC | LEPBI_I1590 | LEPBI_I0708 | Threonine dehydratase biosynthetic; 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. | Ketol-acid reductoisomerase; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. | 0.796 |
| ilvA | ilvD | LEPBI_I1590 | LEPBI_I3352 | Threonine dehydratase biosynthetic; 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 (DAD); Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the IlvD/Edd family. | 0.925 |
| ilvA | ilvH | LEPBI_I1590 | LEPBI_I2361 | Threonine dehydratase biosynthetic; 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. | AHAS; Acetohydroxy-acid synthase small subunit; ALS); Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.980 |
| ilvA | ilvI | LEPBI_I1590 | LEPBI_I0605 | Threonine dehydratase biosynthetic; 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. | AHAS; Acetohydroxy-acid synthase large subunit; ALS; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.944 |
| ilvB1 | ilvA | LEPBI_I0792 | LEPBI_I1590 | AHAS-I; Acetohydroxy-acid synthase I large subunit; ALS-I; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Threonine dehydratase biosynthetic; 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. | 0.950 |
| ilvB1 | ilvB2 | LEPBI_I0792 | LEPBI_I2362 | AHAS-I; Acetohydroxy-acid synthase I large subunit; ALS-I; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | AHAS; Acetohydroxy-acid synthase large subunit; ALS); Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.911 |
| ilvB1 | ilvC | LEPBI_I0792 | LEPBI_I0708 | AHAS-I; Acetohydroxy-acid synthase I large subunit; ALS-I; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Ketol-acid reductoisomerase; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. | 0.992 |
| ilvB1 | ilvD | LEPBI_I0792 | LEPBI_I3352 | AHAS-I; Acetohydroxy-acid synthase I large subunit; ALS-I; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Dihydroxy-acid dehydratase (DAD); Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the IlvD/Edd family. | 0.938 |
| ilvB1 | ilvH | LEPBI_I0792 | LEPBI_I2361 | AHAS-I; Acetohydroxy-acid synthase I large subunit; ALS-I; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | AHAS; Acetohydroxy-acid synthase small subunit; ALS); Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.998 |
| ilvB1 | ilvI | LEPBI_I0792 | LEPBI_I0605 | AHAS-I; Acetohydroxy-acid synthase I large subunit; ALS-I; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | AHAS; Acetohydroxy-acid synthase large subunit; ALS; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.925 |
| ilvB2 | ilvA | LEPBI_I2362 | LEPBI_I1590 | AHAS; Acetohydroxy-acid synthase large subunit; ALS); Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Threonine dehydratase biosynthetic; 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 |
| ilvB2 | ilvB1 | LEPBI_I2362 | LEPBI_I0792 | AHAS; Acetohydroxy-acid synthase large subunit; ALS); Function of homologous gene experimentally demonstrated in an other organism; enzyme. | AHAS-I; Acetohydroxy-acid synthase I large subunit; ALS-I; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.911 |
| ilvB2 | ilvC | LEPBI_I2362 | LEPBI_I0708 | AHAS; Acetohydroxy-acid synthase large subunit; ALS); Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Ketol-acid reductoisomerase; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. | 0.992 |
| ilvB2 | ilvD | LEPBI_I2362 | LEPBI_I3352 | AHAS; Acetohydroxy-acid synthase large subunit; ALS); Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Dihydroxy-acid dehydratase (DAD); Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the IlvD/Edd family. | 0.955 |
| ilvB2 | ilvH | LEPBI_I2362 | LEPBI_I2361 | AHAS; Acetohydroxy-acid synthase large subunit; ALS); Function of homologous gene experimentally demonstrated in an other organism; enzyme. | AHAS; Acetohydroxy-acid synthase small subunit; ALS); Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.999 |
| ilvB2 | ilvI | LEPBI_I2362 | LEPBI_I0605 | AHAS; Acetohydroxy-acid synthase large subunit; ALS); Function of homologous gene experimentally demonstrated in an other organism; enzyme. | AHAS; Acetohydroxy-acid synthase large subunit; ALS; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.923 |
| ilvC | ilvA | LEPBI_I0708 | LEPBI_I1590 | Ketol-acid reductoisomerase; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. | Threonine dehydratase biosynthetic; 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. | 0.796 |
| ilvC | ilvB1 | LEPBI_I0708 | LEPBI_I0792 | Ketol-acid reductoisomerase; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. | AHAS-I; Acetohydroxy-acid synthase I large subunit; ALS-I; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.992 |
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