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 |
| EHY68849.1 | ilvA | SEHO0A_03345 | SEHO0A_03967 | Threonine ammonia-lyase; 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 ammonia-lyase; 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. | 0.994 |
| EHY68849.1 | ilvE | SEHO0A_03345 | SEHO0A_03965 | Threonine ammonia-lyase; 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. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.989 |
| EHY68849.1 | pheA | SEHO0A_03345 | SEHO0A_02780 | Threonine ammonia-lyase; 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. | Chorismate mutase; KEGG: seg:SG2645 1.3e-199 pheA; bifunctional chorismate mutase/prephenate dehydratase; K04093 chorismate mutase K04518; Psort location: Cytoplasmic, score: 9.97; locus tag in AE006468 is STM2667; pheA. | 0.407 |
| EHY68849.1 | ridA | SEHO0A_03345 | SEHO0A_04541 | Threonine ammonia-lyase; 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. | Putative endoribonuclease L-PSP; Locus tag in AE006468 is STM4458; yjgF. | 0.958 |
| fba | ridA | SEHO0A_03124 | SEHO0A_04541 | Fructose-bisphosphate aldolase, class II; Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis; Belongs to the class II fructose-bisphosphate aldolase family. | Putative endoribonuclease L-PSP; Locus tag in AE006468 is STM4458; yjgF. | 0.579 |
| ilvA | EHY68849.1 | SEHO0A_03967 | SEHO0A_03345 | Threonine ammonia-lyase; 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 ammonia-lyase; 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. | 0.994 |
| ilvA | ilvE | SEHO0A_03967 | SEHO0A_03965 | Threonine ammonia-lyase; 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. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.989 |
| ilvA | pheA | SEHO0A_03967 | SEHO0A_02780 | Threonine ammonia-lyase; 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. | Chorismate mutase; KEGG: seg:SG2645 1.3e-199 pheA; bifunctional chorismate mutase/prephenate dehydratase; K04093 chorismate mutase K04518; Psort location: Cytoplasmic, score: 9.97; locus tag in AE006468 is STM2667; pheA. | 0.407 |
| ilvA | ridA | SEHO0A_03967 | SEHO0A_04541 | Threonine ammonia-lyase; 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. | Putative endoribonuclease L-PSP; Locus tag in AE006468 is STM4458; yjgF. | 0.868 |
| ilvE | EHY68849.1 | SEHO0A_03965 | SEHO0A_03345 | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | Threonine ammonia-lyase; 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. | 0.989 |
| ilvE | ilvA | SEHO0A_03965 | SEHO0A_03967 | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | Threonine ammonia-lyase; 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. | 0.989 |
| ilvE | pheA | SEHO0A_03965 | SEHO0A_02780 | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | Chorismate mutase; KEGG: seg:SG2645 1.3e-199 pheA; bifunctional chorismate mutase/prephenate dehydratase; K04093 chorismate mutase K04518; Psort location: Cytoplasmic, score: 9.97; locus tag in AE006468 is STM2667; pheA. | 0.807 |
| ilvE | ridA | SEHO0A_03965 | SEHO0A_04541 | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | Putative endoribonuclease L-PSP; Locus tag in AE006468 is STM4458; yjgF. | 0.866 |
| ilvE | trpD | SEHO0A_03965 | SEHO0A_01711 | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | Anthranilate phosphoribosyltransferase; Catalyzes the transfer of the phosphoribosyl group of 5- phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'- phosphoribosyl)-anthranilate (PRA). | 0.804 |
| ilvE | tyrA | SEHO0A_03965 | SEHO0A_02782 | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | Chorismate mutase; KEGG: spq:SPAB_03380 6.0e-193 tyrA; bifunctional chorismate mutase/prephenate dehydrogenase; K04092 chorismate mutase K04517; Psort location: Cytoplasmic, score: 9.97; locus tag in AE006468 is STM2669; tyrA. | 0.774 |
| pheA | EHY68849.1 | SEHO0A_02780 | SEHO0A_03345 | Chorismate mutase; KEGG: seg:SG2645 1.3e-199 pheA; bifunctional chorismate mutase/prephenate dehydratase; K04093 chorismate mutase K04518; Psort location: Cytoplasmic, score: 9.97; locus tag in AE006468 is STM2667; pheA. | Threonine ammonia-lyase; 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. | 0.407 |
| pheA | ilvA | SEHO0A_02780 | SEHO0A_03967 | Chorismate mutase; KEGG: seg:SG2645 1.3e-199 pheA; bifunctional chorismate mutase/prephenate dehydratase; K04093 chorismate mutase K04518; Psort location: Cytoplasmic, score: 9.97; locus tag in AE006468 is STM2667; pheA. | Threonine ammonia-lyase; 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. | 0.407 |
| pheA | ilvE | SEHO0A_02780 | SEHO0A_03965 | Chorismate mutase; KEGG: seg:SG2645 1.3e-199 pheA; bifunctional chorismate mutase/prephenate dehydratase; K04093 chorismate mutase K04518; Psort location: Cytoplasmic, score: 9.97; locus tag in AE006468 is STM2667; pheA. | Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.807 |
| pheA | pyrB | SEHO0A_02780 | SEHO0A_04543 | Chorismate mutase; KEGG: seg:SG2645 1.3e-199 pheA; bifunctional chorismate mutase/prephenate dehydratase; K04093 chorismate mutase K04518; Psort location: Cytoplasmic, score: 9.97; locus tag in AE006468 is STM2667; pheA. | Aspartate carbamoyltransferase; Locus tag in AE006468 is STM4460; pyrB; Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family. | 0.466 |
| pheA | ridA | SEHO0A_02780 | SEHO0A_04541 | Chorismate mutase; KEGG: seg:SG2645 1.3e-199 pheA; bifunctional chorismate mutase/prephenate dehydratase; K04093 chorismate mutase K04518; Psort location: Cytoplasmic, score: 9.97; locus tag in AE006468 is STM2667; pheA. | Putative endoribonuclease L-PSP; Locus tag in AE006468 is STM4458; yjgF. | 0.632 |
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