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 |
| STM3531 | ilvA | STM3531 | STM3905 | Similar to E. coli putative dehydratase (AAC73372.1); Blastp hit to AAC73372.1 (655 aa), 39% identity in aa 86 - 578; Belongs to the IlvD/Edd family. | Threonine deaminase; 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 (By similarity). Belongs to the serine/threon [...] | 0.723 |
| STM3531 | ilvB | STM3531 | STM3796 | Similar to E. coli putative dehydratase (AAC73372.1); Blastp hit to AAC73372.1 (655 aa), 39% identity in aa 86 - 578; Belongs to the IlvD/Edd family. | Valine sensitive; similar to E. coli acetolactate synthase I,valine-sensitive, large subunit (AAC76694.1); Blastp hit to AAC76694.1 (562 aa), 91% identity in aa 1 - 562. | 0.959 |
| STM3531 | ilvC | STM3531 | STM3909 | Similar to E. coli putative dehydratase (AAC73372.1); Blastp hit to AAC73372.1 (655 aa), 39% identity in aa 86 - 578; Belongs to the IlvD/Edd family. | 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 |
| STM3531 | ilvD | STM3531 | STM3904 | Similar to E. coli putative dehydratase (AAC73372.1); Blastp hit to AAC73372.1 (655 aa), 39% identity in aa 86 - 578; Belongs to the IlvD/Edd family. | Dihydroxy-acid dehydratase. (SW:ILVD_SALTY); Belongs to the IlvD/Edd family. | 0.919 |
| STM3531 | ilvH | STM3531 | STM0117 | Similar to E. coli putative dehydratase (AAC73372.1); Blastp hit to AAC73372.1 (655 aa), 39% identity in aa 86 - 578; Belongs to the IlvD/Edd family. | Acetolactate synthase isozyme III small subunit. (SW:ILVH_SALTY). | 0.883 |
| STM3531 | ilvM | STM3531 | STM3902 | Similar to E. coli putative dehydratase (AAC73372.1); Blastp hit to AAC73372.1 (655 aa), 39% identity in aa 86 - 578; Belongs to the IlvD/Edd family. | Similar to E. coli acetolactate synthase II, valine insensitive, small subunit (AAC77489.1); Blastp hit to AAC77489.1 (87 aa), 93% identity in aa 2 - 87. | 0.707 |
| STM3531 | ilvN | STM3531 | STM3795 | Similar to E. coli putative dehydratase (AAC73372.1); Blastp hit to AAC73372.1 (655 aa), 39% identity in aa 86 - 578; Belongs to the IlvD/Edd family. | Similar to E. coli acetolactate synthase I, valine sensitive, small subunit (AAC76693.1); Blastp hit to AAC76693.1 (96 aa), 90% identity in aa 1 - 96. | 0.859 |
| STM3531 | leuA | STM3531 | STM0113 | Similar to E. coli putative dehydratase (AAC73372.1); Blastp hit to AAC73372.1 (655 aa), 39% identity in aa 86 - 578; Belongs to the IlvD/Edd family. | 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 |
| STM3531 | leuB | STM3531 | STM0112 | Similar to E. coli putative dehydratase (AAC73372.1); Blastp hit to AAC73372.1 (655 aa), 39% identity in aa 86 - 578; Belongs to the IlvD/Edd family. | 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. | 0.935 |
| STM3531 | tdcB | STM3531 | STM3244 | Similar to E. coli putative dehydratase (AAC73372.1); Blastp hit to AAC73372.1 (655 aa), 39% identity in aa 86 - 578; Belongs to the IlvD/Edd family. | 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. TdcB also dehydrates serine to yield pyruv [...] | 0.757 |
| ilvA | STM3531 | STM3905 | STM3531 | Threonine deaminase; 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 (By similarity). Belongs to the serine/threon [...] | Similar to E. coli putative dehydratase (AAC73372.1); Blastp hit to AAC73372.1 (655 aa), 39% identity in aa 86 - 578; Belongs to the IlvD/Edd family. | 0.723 |
| ilvA | ilvB | STM3905 | STM3796 | Threonine deaminase; 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 (By similarity). Belongs to the serine/threon [...] | Valine sensitive; similar to E. coli acetolactate synthase I,valine-sensitive, large subunit (AAC76694.1); Blastp hit to AAC76694.1 (562 aa), 91% identity in aa 1 - 562. | 0.969 |
| ilvA | ilvC | STM3905 | STM3909 | Threonine deaminase; 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 (By similarity). Belongs to the serine/threon [...] | 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. | 0.917 |
| ilvA | ilvD | STM3905 | STM3904 | Threonine deaminase; 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 (By similarity). Belongs to the serine/threon [...] | Dihydroxy-acid dehydratase. (SW:ILVD_SALTY); Belongs to the IlvD/Edd family. | 0.998 |
| ilvA | ilvH | STM3905 | STM0117 | Threonine deaminase; 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 (By similarity). Belongs to the serine/threon [...] | Acetolactate synthase isozyme III small subunit. (SW:ILVH_SALTY). | 0.986 |
| ilvA | ilvM | STM3905 | STM3902 | Threonine deaminase; 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 (By similarity). Belongs to the serine/threon [...] | Similar to E. coli acetolactate synthase II, valine insensitive, small subunit (AAC77489.1); Blastp hit to AAC77489.1 (87 aa), 93% identity in aa 2 - 87. | 0.944 |
| ilvA | ilvN | STM3905 | STM3795 | Threonine deaminase; 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 (By similarity). Belongs to the serine/threon [...] | Similar to E. coli acetolactate synthase I, valine sensitive, small subunit (AAC76693.1); Blastp hit to AAC76693.1 (96 aa), 90% identity in aa 1 - 96. | 0.965 |
| ilvA | leuA | STM3905 | STM0113 | Threonine deaminase; 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 (By similarity). Belongs to the serine/threon [...] | 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. | 0.870 |
| ilvA | leuB | STM3905 | STM0112 | Threonine deaminase; 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 (By similarity). Belongs to the serine/threon [...] | 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 | STM3905 | STM3244 | Threonine deaminase; 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 (By similarity). Belongs to the serine/threon [...] | 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. TdcB also dehydrates serine to yield pyruv [...] | 0.925 |
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