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 | Z5283 | Z5165 | Threonine deaminase (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. | Acetolactate synthase I,valine-sensitive, large subunit; Residues 1 to 562 of 562 are 98.57 pct identical to residues 1 to 562 of 562 from Escherichia coli K-12 Strain MG1655: B3671. | 0.972 |
| ilvA | ilvC | Z5283 | Z5285 | Threonine deaminase (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. | 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. | 0.888 |
| ilvA | ilvG | Z5283 | Z5279 | Threonine deaminase (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. | Acetohydroxy acid synthase II; Residues 1 to 326 of 548 are 99.38 pct identical to residues 1 to 326 of 327 from Escherichia coli K-12 Strain MG1655: B3767. | 0.978 |
| ilvA | ilvI | Z5283 | Z0087 | Threonine deaminase (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. | Acetolactate synthase III, valine sensitive, large subunit; Residues 1 to 602 of 602 are 99.33 pct identical to residues 3 to 604 of 604 from Escherichia coli K-12 Strain MG1655: B0077. | 0.954 |
| ilvA | ilvM | Z5283 | Z5280 | Threonine deaminase (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. | Acetolactate synthase II, valine insensitive, small subunit; Residues 1 to 87 of 87 are 100.00 pct identical to residues 1 to 87 of 87 from Escherichia coli K-12 Strain MG1655: B3769. | 0.987 |
| ilvA | ilvN | Z5283 | Z5164 | Threonine deaminase (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. | Acetolactate synthase I, valine sensitive, small subunit; Residues 1 to 96 of 96 are 100.00 pct identical to residues 1 to 96 of 96 from Escherichia coli K-12 Strain MG1655: B3670; Belongs to the acetolactate synthase small subunit family. | 0.957 |
| ilvA | leuB | Z5283 | Z0082 | Threonine deaminase (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. | 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. | 0.973 |
| ilvA | tdcB | Z5283 | Z4469 | Threonine deaminase (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. | Threonine dehydratase, catabolic; 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. TdcB also dehydrates serine to [...] | 0.917 |
| ilvB | ilvA | Z5165 | Z5283 | Acetolactate synthase I,valine-sensitive, large subunit; Residues 1 to 562 of 562 are 98.57 pct identical to residues 1 to 562 of 562 from Escherichia coli K-12 Strain MG1655: B3671. | Threonine deaminase (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. | 0.972 |
| ilvB | ilvC | Z5165 | Z5285 | Acetolactate synthase I,valine-sensitive, large subunit; Residues 1 to 562 of 562 are 98.57 pct identical to residues 1 to 562 of 562 from Escherichia coli K-12 Strain MG1655: B3671. | 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. | 0.995 |
| ilvB | ilvG | Z5165 | Z5279 | Acetolactate synthase I,valine-sensitive, large subunit; Residues 1 to 562 of 562 are 98.57 pct identical to residues 1 to 562 of 562 from Escherichia coli K-12 Strain MG1655: B3671. | Acetohydroxy acid synthase II; Residues 1 to 326 of 548 are 99.38 pct identical to residues 1 to 326 of 327 from Escherichia coli K-12 Strain MG1655: B3767. | 0.907 |
| ilvB | ilvI | Z5165 | Z0087 | Acetolactate synthase I,valine-sensitive, large subunit; Residues 1 to 562 of 562 are 98.57 pct identical to residues 1 to 562 of 562 from Escherichia coli K-12 Strain MG1655: B3671. | Acetolactate synthase III, valine sensitive, large subunit; Residues 1 to 602 of 602 are 99.33 pct identical to residues 3 to 604 of 604 from Escherichia coli K-12 Strain MG1655: B0077. | 0.916 |
| ilvB | ilvM | Z5165 | Z5280 | Acetolactate synthase I,valine-sensitive, large subunit; Residues 1 to 562 of 562 are 98.57 pct identical to residues 1 to 562 of 562 from Escherichia coli K-12 Strain MG1655: B3671. | Acetolactate synthase II, valine insensitive, small subunit; Residues 1 to 87 of 87 are 100.00 pct identical to residues 1 to 87 of 87 from Escherichia coli K-12 Strain MG1655: B3769. | 0.969 |
| ilvB | ilvN | Z5165 | Z5164 | Acetolactate synthase I,valine-sensitive, large subunit; Residues 1 to 562 of 562 are 98.57 pct identical to residues 1 to 562 of 562 from Escherichia coli K-12 Strain MG1655: B3671. | Acetolactate synthase I, valine sensitive, small subunit; Residues 1 to 96 of 96 are 100.00 pct identical to residues 1 to 96 of 96 from Escherichia coli K-12 Strain MG1655: B3670; Belongs to the acetolactate synthase small subunit family. | 0.999 |
| ilvB | leuB | Z5165 | Z0082 | Acetolactate synthase I,valine-sensitive, large subunit; Residues 1 to 562 of 562 are 98.57 pct identical to residues 1 to 562 of 562 from Escherichia coli K-12 Strain MG1655: B3671. | 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 | poxB | Z5165 | Z1105 | Acetolactate synthase I,valine-sensitive, large subunit; Residues 1 to 562 of 562 are 98.57 pct identical to residues 1 to 562 of 562 from Escherichia coli K-12 Strain MG1655: B3671. | Pyruvate oxidase; Residues 1 to 572 of 572 are 99.47 pct identical to residues 1 to 572 of 572 from Escherichia coli K-12 Strain MG1655: B0871; Belongs to the TPP enzyme family. | 0.846 |
| ilvB | tdcB | Z5165 | Z4469 | Acetolactate synthase I,valine-sensitive, large subunit; Residues 1 to 562 of 562 are 98.57 pct identical to residues 1 to 562 of 562 from Escherichia coli K-12 Strain MG1655: B3671. | Threonine dehydratase, catabolic; 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. TdcB also dehydrates serine to [...] | 0.935 |
| ilvB | yeaU | Z5165 | Z2843 | Acetolactate synthase I,valine-sensitive, large subunit; Residues 1 to 562 of 562 are 98.57 pct identical to residues 1 to 562 of 562 from Escherichia coli K-12 Strain MG1655: B3671. | Putative tartrate dehydrogenase; Residues 1 to 361 of 361 are 99.72 pct identical to residues 1 to 361 of 361 from Escherichia coli K-12 Strain MG1655: B1800. | 0.954 |
| ilvC | ilvA | Z5285 | Z5283 | 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 deaminase (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. | 0.888 |
| ilvC | ilvB | Z5285 | Z5165 | 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 I,valine-sensitive, large subunit; Residues 1 to 562 of 562 are 98.57 pct identical to residues 1 to 562 of 562 from Escherichia coli K-12 Strain MG1655: B3671. | 0.995 |
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