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 |
| ilvA | ilvB | c4694 | c4596 | 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. | Acetolactate synthase isozyme I large subunit; Escherichia coli K-12 ortholog: b3671; Escherichia coli O157:H7 ortholog: z5165. | 0.977 |
| ilvA | ilvD | c4694 | c4693 | 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; Escherichia coli K-12 ortholog: b3771; Escherichia coli O157:H7 ortholog: z5282. | 0.998 |
| ilvA | ilvE | c4694 | c4692 | 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. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. | 0.988 |
| ilvA | ilvG | c4694 | c4690 | 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. | Acetohydroxy acid synthase II; Escherichia coli O157:H7 ortholog: z5279. | 0.971 |
| ilvA | ilvH | c4694 | c0096 | 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. | Acetolactate synthase isozyme III small subunit; Escherichia coli K-12 ortholog: b0078; Escherichia coli O157:H7 ortholog: z0088. | 0.978 |
| ilvA | ilvI | c4694 | c0095 | 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. | Acetolactate synthase isozyme III large subunit; Escherichia coli K-12 ortholog: b0077; Escherichia coli O157:H7 ortholog: z0087. | 0.952 |
| ilvA | ilvM | c4694 | c4691 | 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. | Acetolactate synthase isozyme II small subunit; Escherichia coli K-12 ortholog: b3769; Escherichia coli O157:H7 ortholog: z5280. | 0.988 |
| ilvA | ilvN | c4694 | c4595 | 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. | Acetolactate synthase isozyme I small subunit; Escherichia coli K-12 ortholog: b3670; Escherichia coli O157:H7 ortholog: z5164; Belongs to the acetolactate synthase small subunit family. | 0.956 |
| ilvA | leuB | c4694 | c0090 | 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. | 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. Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 1 subfamily. | 0.977 |
| ilvA | thrC | c4694 | c0005 | 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. | Threonine synthase; Escherichia coli K-12 ortholog: b0004; Escherichia coli O157:H7 ortholog: z0004. | 0.966 |
| ilvB | ilvA | c4596 | c4694 | Acetolactate synthase isozyme I large subunit; Escherichia coli K-12 ortholog: b3671; Escherichia coli O157:H7 ortholog: z5165. | 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. | 0.977 |
| ilvB | ilvD | c4596 | c4693 | Acetolactate synthase isozyme I large subunit; Escherichia coli K-12 ortholog: b3671; Escherichia coli O157:H7 ortholog: z5165. | Dihydroxy-acid dehydratase; Escherichia coli K-12 ortholog: b3771; Escherichia coli O157:H7 ortholog: z5282. | 0.966 |
| ilvB | ilvE | c4596 | c4692 | Acetolactate synthase isozyme I large subunit; Escherichia coli K-12 ortholog: b3671; Escherichia coli O157:H7 ortholog: z5165. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. | 0.754 |
| ilvB | ilvG | c4596 | c4690 | Acetolactate synthase isozyme I large subunit; Escherichia coli K-12 ortholog: b3671; Escherichia coli O157:H7 ortholog: z5165. | Acetohydroxy acid synthase II; Escherichia coli O157:H7 ortholog: z5279. | 0.907 |
| ilvB | ilvH | c4596 | c0096 | Acetolactate synthase isozyme I large subunit; Escherichia coli K-12 ortholog: b3671; Escherichia coli O157:H7 ortholog: z5165. | Acetolactate synthase isozyme III small subunit; Escherichia coli K-12 ortholog: b0078; Escherichia coli O157:H7 ortholog: z0088. | 0.997 |
| ilvB | ilvI | c4596 | c0095 | Acetolactate synthase isozyme I large subunit; Escherichia coli K-12 ortholog: b3671; Escherichia coli O157:H7 ortholog: z5165. | Acetolactate synthase isozyme III large subunit; Escherichia coli K-12 ortholog: b0077; Escherichia coli O157:H7 ortholog: z0087. | 0.916 |
| ilvB | ilvM | c4596 | c4691 | Acetolactate synthase isozyme I large subunit; Escherichia coli K-12 ortholog: b3671; Escherichia coli O157:H7 ortholog: z5165. | Acetolactate synthase isozyme II small subunit; Escherichia coli K-12 ortholog: b3769; Escherichia coli O157:H7 ortholog: z5280. | 0.973 |
| ilvB | ilvN | c4596 | c4595 | Acetolactate synthase isozyme I large subunit; Escherichia coli K-12 ortholog: b3671; Escherichia coli O157:H7 ortholog: z5165. | Acetolactate synthase isozyme I small subunit; Escherichia coli K-12 ortholog: b3670; Escherichia coli O157:H7 ortholog: z5164; Belongs to the acetolactate synthase small subunit family. | 0.999 |
| ilvB | leuB | c4596 | c0090 | Acetolactate synthase isozyme I large subunit; Escherichia coli K-12 ortholog: b3671; Escherichia coli O157:H7 ortholog: z5165. | 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. Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 1 subfamily. | 0.985 |
| ilvB | thrC | c4596 | c0005 | Acetolactate synthase isozyme I large subunit; Escherichia coli K-12 ortholog: b3671; Escherichia coli O157:H7 ortholog: z5165. | Threonine synthase; Escherichia coli K-12 ortholog: b0004; Escherichia coli O157:H7 ortholog: z0004. | 0.437 |
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