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 | mdeA | CH53_1393 | CH53_4389 | 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. | OAH_OAS_sulfhy: O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase family protein. | 0.807 |
| ilvA | metA | CH53_1393 | CH53_2120 | 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 O-succinyltransferase; Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine; Belongs to the MetA family. | 0.817 |
| ilvA | metB | CH53_1393 | CH53_1907 | 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. | O-succinylhomoserine (thiol)-lyase; Cystathionine gamma-lyase-like protein; O_succ_thio_ly: O-succinylhomoserine (thiol)-lyase. | 0.818 |
| ilvA | metH | CH53_1393 | CH53_2131 | 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. | Methionine synthase; Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate. | 0.890 |
| ilvA | metL | CH53_1393 | CH53_1908 | 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, NAD binding domain protein; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.685 |
| ilvA | tdcB_2 | CH53_1393 | CH53_1718 | 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. | Pyridoxal-phosphate dependent enzyme family protein. | 0.915 |
| ilvA | thrA | CH53_1393 | CH53_1086 | 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. | Asp_kinase: aspartate kinase domain protein; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.685 |
| ilvA | trpB | CH53_1393 | CH53_3895 | 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. | Tryptophan synthase, beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.925 |
| ilvA | uptG | CH53_1393 | CH53_217 | 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. | CBS domain protein. | 0.925 |
| mdeA | ilvA | CH53_4389 | CH53_1393 | OAH_OAS_sulfhy: O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase family protein. | 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. | 0.807 |
| mdeA | metA | CH53_4389 | CH53_2120 | OAH_OAS_sulfhy: O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase family protein. | Homoserine O-succinyltransferase; Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine; Belongs to the MetA family. | 0.984 |
| mdeA | metB | CH53_4389 | CH53_1907 | OAH_OAS_sulfhy: O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase family protein. | O-succinylhomoserine (thiol)-lyase; Cystathionine gamma-lyase-like protein; O_succ_thio_ly: O-succinylhomoserine (thiol)-lyase. | 0.931 |
| mdeA | metH | CH53_4389 | CH53_2131 | OAH_OAS_sulfhy: O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase family protein. | Methionine synthase; Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate. | 0.953 |
| mdeA | metL | CH53_4389 | CH53_1908 | OAH_OAS_sulfhy: O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase family protein. | Homoserine dehydrogenase, NAD binding domain protein; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.912 |
| mdeA | tdcB_2 | CH53_4389 | CH53_1718 | OAH_OAS_sulfhy: O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase family protein. | Pyridoxal-phosphate dependent enzyme family protein. | 0.807 |
| mdeA | thrA | CH53_4389 | CH53_1086 | OAH_OAS_sulfhy: O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase family protein. | Asp_kinase: aspartate kinase domain protein; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.912 |
| mdeA | uptG | CH53_4389 | CH53_217 | OAH_OAS_sulfhy: O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase family protein. | CBS domain protein. | 0.957 |
| metA | ilvA | CH53_2120 | CH53_1393 | Homoserine O-succinyltransferase; Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine; Belongs to the MetA 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. | 0.817 |
| metA | mdeA | CH53_2120 | CH53_4389 | Homoserine O-succinyltransferase; Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine; Belongs to the MetA family. | OAH_OAS_sulfhy: O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase family protein. | 0.984 |
| metA | metB | CH53_2120 | CH53_1907 | Homoserine O-succinyltransferase; Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine; Belongs to the MetA family. | O-succinylhomoserine (thiol)-lyase; Cystathionine gamma-lyase-like protein; O_succ_thio_ly: O-succinylhomoserine (thiol)-lyase. | 0.964 |
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