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 | HMPREF0766_11218 | HMPREF0766_11209 | 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. | Acetolactate synthase, large subunit, biosynthetic type; COG: COG0028; Pfam: PF02776,PF00205,PF02775; InterPro: IPR012846. | 0.992 |
| ilvA | ilvD | HMPREF0766_11218 | HMPREF0766_11208 | 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. | Dihydroxy-acid dehydratase; COG: COG0129; Pfam: PF00920; InterPro: IPR000581; Belongs to the IlvD/Edd family. | 0.934 |
| ilvA | ilvE | HMPREF0766_11218 | HMPREF0766_11113 | 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 transaminase; COG: COG0115; Pfam: PF01063; InterPro: IPR001544. | 0.959 |
| ilvA | ilvE-2 | HMPREF0766_11218 | HMPREF0766_11207 | 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 transaminase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.939 |
| ilvA | ilvN | HMPREF0766_11218 | HMPREF0766_11210 | 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. | Acetolactate synthase, small subunit; COG: COG0440; Pfam: PF01842; InterPro: IPR004789. | 0.996 |
| ilvA | leuA | HMPREF0766_11218 | HMPREF0766_11217 | 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. | HMGL-like protein; COG: COG0119; Pfam: PF00682; InterPro: IPR013785; Belongs to the alpha-IPM synthase/homocitrate synthase family. | 0.804 |
| ilvA | thrA | HMPREF0766_11218 | HMPREF0766_12530 | 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. | Homoserine dehydrogenase; COG: COG0527; Pfam: PF00696,PF01842,PF03447,PF00742; InterPro: IPR001341. | 0.907 |
| ilvA | tktA2 | HMPREF0766_11218 | HMPREF0766_12833 | 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. | Transketolase, C-terminal domain protein; COG: COG0022; Pfam: PF00676,PF02779,PF02780; InterPro: IPR001017. | 0.956 |
| ilvB | ilvA | HMPREF0766_11209 | HMPREF0766_11218 | Acetolactate synthase, large subunit, biosynthetic type; COG: COG0028; Pfam: PF02776,PF00205,PF02775; InterPro: IPR012846. | 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. | 0.992 |
| ilvB | ilvD | HMPREF0766_11209 | HMPREF0766_11208 | Acetolactate synthase, large subunit, biosynthetic type; COG: COG0028; Pfam: PF02776,PF00205,PF02775; InterPro: IPR012846. | Dihydroxy-acid dehydratase; COG: COG0129; Pfam: PF00920; InterPro: IPR000581; Belongs to the IlvD/Edd family. | 0.994 |
| ilvB | ilvE | HMPREF0766_11209 | HMPREF0766_11113 | Acetolactate synthase, large subunit, biosynthetic type; COG: COG0028; Pfam: PF02776,PF00205,PF02775; InterPro: IPR012846. | Branched-chain-amino-acid transaminase; COG: COG0115; Pfam: PF01063; InterPro: IPR001544. | 0.567 |
| ilvB | ilvE-2 | HMPREF0766_11209 | HMPREF0766_11207 | Acetolactate synthase, large subunit, biosynthetic type; COG: COG0028; Pfam: PF02776,PF00205,PF02775; InterPro: IPR012846. | Branched-chain-amino-acid transaminase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.907 |
| ilvB | ilvN | HMPREF0766_11209 | HMPREF0766_11210 | Acetolactate synthase, large subunit, biosynthetic type; COG: COG0028; Pfam: PF02776,PF00205,PF02775; InterPro: IPR012846. | Acetolactate synthase, small subunit; COG: COG0440; Pfam: PF01842; InterPro: IPR004789. | 0.999 |
| ilvB | leuA | HMPREF0766_11209 | HMPREF0766_11217 | Acetolactate synthase, large subunit, biosynthetic type; COG: COG0028; Pfam: PF02776,PF00205,PF02775; InterPro: IPR012846. | HMGL-like protein; COG: COG0119; Pfam: PF00682; InterPro: IPR013785; Belongs to the alpha-IPM synthase/homocitrate synthase family. | 0.981 |
| ilvB | thrA | HMPREF0766_11209 | HMPREF0766_12530 | Acetolactate synthase, large subunit, biosynthetic type; COG: COG0028; Pfam: PF02776,PF00205,PF02775; InterPro: IPR012846. | Homoserine dehydrogenase; COG: COG0527; Pfam: PF00696,PF01842,PF03447,PF00742; InterPro: IPR001341. | 0.782 |
| ilvB | tktA2 | HMPREF0766_11209 | HMPREF0766_12833 | Acetolactate synthase, large subunit, biosynthetic type; COG: COG0028; Pfam: PF02776,PF00205,PF02775; InterPro: IPR012846. | Transketolase, C-terminal domain protein; COG: COG0022; Pfam: PF00676,PF02779,PF02780; InterPro: IPR001017. | 0.758 |
| ilvD | ilvA | HMPREF0766_11208 | HMPREF0766_11218 | Dihydroxy-acid dehydratase; COG: COG0129; Pfam: PF00920; InterPro: IPR000581; Belongs to the IlvD/Edd 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. | 0.934 |
| ilvD | ilvB | HMPREF0766_11208 | HMPREF0766_11209 | Dihydroxy-acid dehydratase; COG: COG0129; Pfam: PF00920; InterPro: IPR000581; Belongs to the IlvD/Edd family. | Acetolactate synthase, large subunit, biosynthetic type; COG: COG0028; Pfam: PF02776,PF00205,PF02775; InterPro: IPR012846. | 0.994 |
| ilvD | ilvE | HMPREF0766_11208 | HMPREF0766_11113 | Dihydroxy-acid dehydratase; COG: COG0129; Pfam: PF00920; InterPro: IPR000581; Belongs to the IlvD/Edd family. | Branched-chain-amino-acid transaminase; COG: COG0115; Pfam: PF01063; InterPro: IPR001544. | 0.994 |
| ilvD | ilvE-2 | HMPREF0766_11208 | HMPREF0766_11207 | Dihydroxy-acid dehydratase; COG: COG0129; Pfam: PF00920; InterPro: IPR000581; Belongs to the IlvD/Edd family. | Branched-chain-amino-acid transaminase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. | 0.999 |
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