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 |
| AKC75733.1 | ilvA_1 | ShL2_00867 | ShL2_00861 | Acetolactate synthase 1 regulatory subunit. | Threonine dehydratase biosynthetic, IlvA_1; 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. | 0.990 |
| AKC75733.1 | ilvB | ShL2_00867 | ShL2_00868 | Acetolactate synthase 1 regulatory subunit. | Acetolactate synthase large subunit. | 0.997 |
| AKC75733.1 | ilvC | ShL2_00867 | ShL2_00866 | Acetolactate synthase 1 regulatory subunit. | 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. | 0.996 |
| AKC75733.1 | ilvD | ShL2_00867 | ShL2_00869 | Acetolactate synthase 1 regulatory subunit. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.948 |
| AKC75733.1 | leuA | ShL2_00867 | ShL2_00865 | Acetolactate synthase 1 regulatory subunit. | 2-isopropylmalate synthase; 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. | 0.989 |
| ilvA_1 | AKC75733.1 | ShL2_00861 | ShL2_00867 | Threonine dehydratase biosynthetic, IlvA_1; 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 1 regulatory subunit. | 0.990 |
| ilvA_1 | ilvB | ShL2_00861 | ShL2_00868 | Threonine dehydratase biosynthetic, IlvA_1; 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 large subunit. | 0.994 |
| ilvA_1 | ilvC | ShL2_00861 | ShL2_00866 | Threonine dehydratase biosynthetic, IlvA_1; 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. | 0.967 |
| ilvA_1 | ilvD | ShL2_00861 | ShL2_00869 | Threonine dehydratase biosynthetic, IlvA_1; 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. | 0.995 |
| ilvA_1 | leuA | ShL2_00861 | ShL2_00865 | Threonine dehydratase biosynthetic, IlvA_1; 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; 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. | 0.956 |
| ilvB | AKC75733.1 | ShL2_00868 | ShL2_00867 | Acetolactate synthase large subunit. | Acetolactate synthase 1 regulatory subunit. | 0.997 |
| ilvB | ilvA_1 | ShL2_00868 | ShL2_00861 | Acetolactate synthase large subunit. | Threonine dehydratase biosynthetic, IlvA_1; 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. | 0.994 |
| ilvB | ilvC | ShL2_00868 | ShL2_00866 | Acetolactate synthase large subunit. | 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. | 0.999 |
| ilvB | ilvD | ShL2_00868 | ShL2_00869 | Acetolactate synthase large subunit. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.998 |
| ilvB | leuA | ShL2_00868 | ShL2_00865 | Acetolactate synthase large subunit. | 2-isopropylmalate synthase; 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. | 0.996 |
| ilvC | AKC75733.1 | ShL2_00866 | ShL2_00867 | 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. | Acetolactate synthase 1 regulatory subunit. | 0.996 |
| ilvC | ilvA_1 | ShL2_00866 | ShL2_00861 | 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, IlvA_1; 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. | 0.967 |
| ilvC | ilvB | ShL2_00866 | ShL2_00868 | 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. | Acetolactate synthase large subunit. | 0.999 |
| ilvC | ilvD | ShL2_00866 | ShL2_00869 | 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. | Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. | 0.999 |
| ilvC | leuA | ShL2_00866 | ShL2_00865 | 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. | 2-isopropylmalate synthase; 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. | 0.998 |
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