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 proteins in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| 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 | ilvG | STM3905 | STM3901 | 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 [...] | Fragment 1; cryptic; similar to E. coli acetolactate synthase II, large subunit, cryptic, interrupted (AAC77488.1); Blastp hit to AAC77488.1 (327 aa), 93% identity in aa 1 - 325. | 0.994 |
| 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 | ilvI | STM3905 | STM0116 | 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 large subunit. (SW:ILVI_SALTY). | 0.979 |
| 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 | 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 | nifJ | STM3905 | STM1651 | 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 oxidoreductase, Fe-S subunit (AAC74460.1); Blastp hit to AAC74460.1 (1174 aa), 92% identity in aa 1 - 1174. | 0.505 |
| 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 |
| ilvB | ilvA | STM3796 | STM3905 | 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. | 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 [...] | 0.969 |
| ilvB | ilvC | STM3796 | STM3909 | 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. | 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. | 0.988 |
| ilvB | ilvG | STM3796 | STM3901 | 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. | Fragment 1; cryptic; similar to E. coli acetolactate synthase II, large subunit, cryptic, interrupted (AAC77488.1); Blastp hit to AAC77488.1 (327 aa), 93% identity in aa 1 - 325. | 0.922 |
| ilvB | ilvH | STM3796 | STM0117 | 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. | Acetolactate synthase isozyme III small subunit. (SW:ILVH_SALTY). | 0.999 |
| ilvB | ilvI | STM3796 | STM0116 | 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. | Acetolactate synthase isozyme III large subunit. (SW:ILVI_SALTY). | 0.940 |
| ilvB | ilvM | STM3796 | STM3902 | 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. | 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. | 0.964 |
| ilvB | ilvN | STM3796 | STM3795 | 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. | 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. | 0.999 |
| ilvB | leuB | STM3796 | STM0112 | 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. | 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. | 0.984 |
| ilvB | nifJ | STM3796 | STM1651 | 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. | Similar to E. coli putative oxidoreductase, Fe-S subunit (AAC74460.1); Blastp hit to AAC74460.1 (1174 aa), 92% identity in aa 1 - 1174. | 0.950 |
| ilvB | tdcB | STM3796 | STM3244 | 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. | 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 [...] | 0.960 |
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