Export your current network:
... as a bitmap image:
file format is 'PNG': portable network graphic
... as a high-resolution bitmap:
same PNG format, but resolution at 400 dpi
... as a vector graphic:
SVG: scalable vector graphic - can be opened and edited in Illustrator, CorelDraw, Dia, etc
... as simple tabular text output:
TSV: tab separated values - can be opened in Excel
... as an XML summary:
structured XML interaction data, according to the 'PSI-MI' data standard
... 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 annotated functions of the network proteins
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| DR97_5812 | DR97_606 | DR97_5812 | DR97_606 | annotation not available | annotation not available | 0.841 |
| DR97_5812 | ilvA1 | DR97_5812 | DR97_3296 | annotation not available | 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 | 0.823 |
| DR97_5812 | ilvA3 | DR97_5812 | DR97_468 | annotation not available | 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 | 0.835 |
| DR97_5812 | ilvB | DR97_5812 | DR97_2038 | annotation not available | Acolac_lg- acetolactate synthase, large subunit, biosynthetic type | 0.841 |
| DR97_5812 | ilvC | DR97_5812 | DR97_2036 | annotation not available | Ketol-acid reductoisomerase (NADP(+)); 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; Belongs to the ketol-acid reductoisomerase family | 0.975 |
| DR97_5812 | ilvN | DR97_5812 | DR97_2037 | annotation not available | Acolac_sm- acetolactate synthase, small subunit | 0.971 |
| DR97_5812 | leuA | DR97_5812 | DR97_4077 | annotation not available | leuA_yeast- 2-isopropylmalate synthase; Belongs to the alpha-IPM synthase/homocitrate synthase family | 0.858 |
| DR97_5812 | leuB | DR97_5812 | DR97_4815 | annotation not available | 3-isopropylmalate dehydrogenase; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate | 0.968 |
| DR97_5812 | leuC | DR97_5812 | DR97_4812 | annotation not available | 3-isopropylmalate dehydratase large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate; Belongs to the aconitase/IPM isomerase family. LeuC type 1 subfamily | 0.641 |
| DR97_5812 | leuD | DR97_5812 | DR97_4813 | annotation not available | 3-isopropylmalate dehydratase small subunit; Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate; Belongs to the LeuD family. LeuD type 1 subfamily | 0.520 |
| DR97_606 | DR97_5812 | DR97_606 | DR97_5812 | annotation not available | annotation not available | 0.841 |
| DR97_606 | ilvA1 | DR97_606 | DR97_3296 | annotation not available | 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 | 0.819 |
| DR97_606 | ilvA3 | DR97_606 | DR97_468 | annotation not available | 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 | 0.832 |
| DR97_606 | ilvB | DR97_606 | DR97_2038 | annotation not available | Acolac_lg- acetolactate synthase, large subunit, biosynthetic type | 0.847 |
| DR97_606 | ilvC | DR97_606 | DR97_2036 | annotation not available | Ketol-acid reductoisomerase (NADP(+)); 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; Belongs to the ketol-acid reductoisomerase family | 0.975 |
| DR97_606 | ilvN | DR97_606 | DR97_2037 | annotation not available | Acolac_sm- acetolactate synthase, small subunit | 0.967 |
| DR97_606 | leuA | DR97_606 | DR97_4077 | annotation not available | leuA_yeast- 2-isopropylmalate synthase; Belongs to the alpha-IPM synthase/homocitrate synthase family | 0.857 |
| DR97_606 | leuB | DR97_606 | DR97_4815 | annotation not available | 3-isopropylmalate dehydrogenase; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate | 0.959 |
| DR97_606 | leuC | DR97_606 | DR97_4812 | annotation not available | 3-isopropylmalate dehydratase large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate; Belongs to the aconitase/IPM isomerase family. LeuC type 1 subfamily | 0.512 |
| ilvA1 | DR97_5812 | DR97_3296 | DR97_5812 | 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 | annotation not available | 0.823 |
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