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 |
| STM0458 | cysK | STM0458 | STM2430 | Putative cysteine synthase/cystathionine beta-synthase; Similar to E. coli cysteine synthase B, O-acetylserine sulfhydrolase B (AAC75474.1); Blastp hit to AAC75474.1 (303 aa), 26% identity in aa 6 - 207, 35% identity in aa 198 - 289. | Subunit of cysteine synthase A and O-acetylserine sulfhydrolase A; Two cysteine synthase enzymes are found, this enzyme and CysM; both catalyze the same reaction. Cysteine synthase B (CysM) can also use thiosulfate in place of sulfide to give cysteine thiosulfonate as a product. | 0.914 |
| STM0458 | dpaL | STM0458 | STM1002 | Putative cysteine synthase/cystathionine beta-synthase; Similar to E. coli cysteine synthase B, O-acetylserine sulfhydrolase B (AAC75474.1); Blastp hit to AAC75474.1 (303 aa), 26% identity in aa 6 - 207, 35% identity in aa 198 - 289. | Putatiave diaminopropionate ammonia lyase; Catalyzes the alpha,beta-elimination reaction of both L- and D-alpha,beta-diaminopropionate (DAP) to form pyruvate and ammonia. In vitro L- and D-isomers of serine are also degraded, though slowly; it is the only serine dehydratase which can eliminate an amino group at the beta-carbon position. In vivo L-, D- and a mixure of DL-DAP allow growth. DL-DAP is toxic in the absence of this enzyme, it may inhibit enzymes involved in the synthesis of pyruvate and aspartate, as well as amino acids derived from them. | 0.903 |
| STM0458 | ilvA | STM0458 | STM3905 | Putative cysteine synthase/cystathionine beta-synthase; Similar to E. coli cysteine synthase B, O-acetylserine sulfhydrolase B (AAC75474.1); Blastp hit to AAC75474.1 (303 aa), 26% identity in aa 6 - 207, 35% identity in aa 198 - 289. | 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 [...] | 0.737 |
| STM0458 | tdcB | STM0458 | STM3244 | Putative cysteine synthase/cystathionine beta-synthase; Similar to E. coli cysteine synthase B, O-acetylserine sulfhydrolase B (AAC75474.1); Blastp hit to AAC75474.1 (303 aa), 26% identity in aa 6 - 207, 35% identity in aa 198 - 289. | 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 [...] | 0.499 |
| cysK | STM0458 | STM2430 | STM0458 | Subunit of cysteine synthase A and O-acetylserine sulfhydrolase A; Two cysteine synthase enzymes are found, this enzyme and CysM; both catalyze the same reaction. Cysteine synthase B (CysM) can also use thiosulfate in place of sulfide to give cysteine thiosulfonate as a product. | Putative cysteine synthase/cystathionine beta-synthase; Similar to E. coli cysteine synthase B, O-acetylserine sulfhydrolase B (AAC75474.1); Blastp hit to AAC75474.1 (303 aa), 26% identity in aa 6 - 207, 35% identity in aa 198 - 289. | 0.914 |
| cysK | cysM | STM2430 | STM2440 | Subunit of cysteine synthase A and O-acetylserine sulfhydrolase A; Two cysteine synthase enzymes are found, this enzyme and CysM; both catalyze the same reaction. Cysteine synthase B (CysM) can also use thiosulfate in place of sulfide to give cysteine thiosulfonate as a product. | Cysteine synthase B; Two cysteine synthase enzymes are found. Both catalyze the same reaction. Cysteine synthase B can also use thiosulfate in place of sulfide to give cysteine thiosulfonate as a product. | 0.520 |
| cysK | ilvA | STM2430 | STM3905 | Subunit of cysteine synthase A and O-acetylserine sulfhydrolase A; Two cysteine synthase enzymes are found, this enzyme and CysM; both catalyze the same reaction. Cysteine synthase B (CysM) can also use thiosulfate in place of sulfide to give cysteine thiosulfonate as a product. | 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 [...] | 0.427 |
| cysM | cysK | STM2440 | STM2430 | Cysteine synthase B; Two cysteine synthase enzymes are found. Both catalyze the same reaction. Cysteine synthase B can also use thiosulfate in place of sulfide to give cysteine thiosulfonate as a product. | Subunit of cysteine synthase A and O-acetylserine sulfhydrolase A; Two cysteine synthase enzymes are found, this enzyme and CysM; both catalyze the same reaction. Cysteine synthase B (CysM) can also use thiosulfate in place of sulfide to give cysteine thiosulfonate as a product. | 0.520 |
| dpaL | STM0458 | STM1002 | STM0458 | Putatiave diaminopropionate ammonia lyase; Catalyzes the alpha,beta-elimination reaction of both L- and D-alpha,beta-diaminopropionate (DAP) to form pyruvate and ammonia. In vitro L- and D-isomers of serine are also degraded, though slowly; it is the only serine dehydratase which can eliminate an amino group at the beta-carbon position. In vivo L-, D- and a mixure of DL-DAP allow growth. DL-DAP is toxic in the absence of this enzyme, it may inhibit enzymes involved in the synthesis of pyruvate and aspartate, as well as amino acids derived from them. | Putative cysteine synthase/cystathionine beta-synthase; Similar to E. coli cysteine synthase B, O-acetylserine sulfhydrolase B (AAC75474.1); Blastp hit to AAC75474.1 (303 aa), 26% identity in aa 6 - 207, 35% identity in aa 198 - 289. | 0.903 |
| dpaL | ilvA | STM1002 | STM3905 | Putatiave diaminopropionate ammonia lyase; Catalyzes the alpha,beta-elimination reaction of both L- and D-alpha,beta-diaminopropionate (DAP) to form pyruvate and ammonia. In vitro L- and D-isomers of serine are also degraded, though slowly; it is the only serine dehydratase which can eliminate an amino group at the beta-carbon position. In vivo L-, D- and a mixure of DL-DAP allow growth. DL-DAP is toxic in the absence of this enzyme, it may inhibit enzymes involved in the synthesis of pyruvate and aspartate, as well as amino acids derived from them. | 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 [...] | 0.426 |
| dpaL | tdcB | STM1002 | STM3244 | Putatiave diaminopropionate ammonia lyase; Catalyzes the alpha,beta-elimination reaction of both L- and D-alpha,beta-diaminopropionate (DAP) to form pyruvate and ammonia. In vitro L- and D-isomers of serine are also degraded, though slowly; it is the only serine dehydratase which can eliminate an amino group at the beta-carbon position. In vivo L-, D- and a mixure of DL-DAP allow growth. DL-DAP is toxic in the absence of this enzyme, it may inhibit enzymes involved in the synthesis of pyruvate and aspartate, as well as amino acids derived from them. | 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 [...] | 0.888 |
| dpaL | thrC | STM1002 | STM0004 | Putatiave diaminopropionate ammonia lyase; Catalyzes the alpha,beta-elimination reaction of both L- and D-alpha,beta-diaminopropionate (DAP) to form pyruvate and ammonia. In vitro L- and D-isomers of serine are also degraded, though slowly; it is the only serine dehydratase which can eliminate an amino group at the beta-carbon position. In vivo L-, D- and a mixure of DL-DAP allow growth. DL-DAP is toxic in the absence of this enzyme, it may inhibit enzymes involved in the synthesis of pyruvate and aspartate, as well as amino acids derived from them. | Similar to E. coli threonine synthase (AAC73115.1); Blastp hit to AAC73115.1 (428 aa), 93% identity in aa 1 - 428. | 0.488 |
| dsdA | ilvA | STM3802 | STM3905 | Similar to E. coli D-serine dehydratase (deaminase) (AAC75425.1); Blastp hit to AAC75425.1 (442 aa), 89% identity in aa 1 - 442. | 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 [...] | 0.919 |
| dsdA | tdcB | STM3802 | STM3244 | Similar to E. coli D-serine dehydratase (deaminase) (AAC75425.1); Blastp hit to AAC75425.1 (442 aa), 89% identity in aa 1 - 442. | 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 [...] | 0.905 |
| ilvA | STM0458 | STM3905 | STM0458 | 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 [...] | Putative cysteine synthase/cystathionine beta-synthase; Similar to E. coli cysteine synthase B, O-acetylserine sulfhydrolase B (AAC75474.1); Blastp hit to AAC75474.1 (303 aa), 26% identity in aa 6 - 207, 35% identity in aa 198 - 289. | 0.737 |
| ilvA | cysK | STM3905 | STM2430 | 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 [...] | Subunit of cysteine synthase A and O-acetylserine sulfhydrolase A; Two cysteine synthase enzymes are found, this enzyme and CysM; both catalyze the same reaction. Cysteine synthase B (CysM) can also use thiosulfate in place of sulfide to give cysteine thiosulfonate as a product. | 0.427 |
| ilvA | dpaL | STM3905 | STM1002 | 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 [...] | Putatiave diaminopropionate ammonia lyase; Catalyzes the alpha,beta-elimination reaction of both L- and D-alpha,beta-diaminopropionate (DAP) to form pyruvate and ammonia. In vitro L- and D-isomers of serine are also degraded, though slowly; it is the only serine dehydratase which can eliminate an amino group at the beta-carbon position. In vivo L-, D- and a mixure of DL-DAP allow growth. DL-DAP is toxic in the absence of this enzyme, it may inhibit enzymes involved in the synthesis of pyruvate and aspartate, as well as amino acids derived from them. | 0.426 |
| ilvA | dsdA | STM3905 | STM3802 | 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 D-serine dehydratase (deaminase) (AAC75425.1); Blastp hit to AAC75425.1 (442 aa), 89% identity in aa 1 - 442. | 0.919 |
| 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 |
| ilvA | thrC | STM3905 | STM0004 | 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 threonine synthase (AAC73115.1); Blastp hit to AAC73115.1 (428 aa), 93% identity in aa 1 - 428. | 0.983 |
page 1 of 2