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 |
| ANL60461.1 | kbl | AMC85_CH03107 | AMC85_CH03109 | GFA family glutathione-dependent formaldehyde-activating protein; Protein involved in carbon-sulfur lyase activity and metabolic process. | 2-amino-3-ketobutyrate coenzyme A ligase; Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA. | 0.454 |
| ANL60461.1 | tdh | AMC85_CH03107 | AMC85_CH03108 | GFA family glutathione-dependent formaldehyde-activating protein; Protein involved in carbon-sulfur lyase activity and metabolic process. | L-threonine 3-dehydrogenase; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate; Belongs to the zinc-containing alcohol dehydrogenase family. | 0.768 |
| ANL61044.1 | ANL61686.1 | AMC85_CH03710 | AMC85_CH04367 | Pyridoxal phosphate-dependent threonine dehydratase protein; Protein involved in catalytic activity, pyridoxal phosphate binding and metabolic process. | Pyridoxal phosphate-dependent serine/threonine dehydratase protein; Protein involved in catalytic activity, pyridoxal phosphate binding and metabolic process. | 0.943 |
| ANL61044.1 | ilvA | AMC85_CH03710 | AMC85_CH01850 | Pyridoxal phosphate-dependent threonine dehydratase protein; Protein involved in catalytic activity, pyridoxal phosphate binding and metabolic process. | 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. | 0.924 |
| ANL61044.1 | ltaE | AMC85_CH03710 | AMC85_CH03743 | Pyridoxal phosphate-dependent threonine dehydratase protein; Protein involved in catalytic activity, pyridoxal phosphate binding and metabolic process. | Low-specificity threonine aldolase; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. | 0.911 |
| ANL61044.1 | tdh | AMC85_CH03710 | AMC85_CH03108 | Pyridoxal phosphate-dependent threonine dehydratase protein; Protein involved in catalytic activity, pyridoxal phosphate binding and metabolic process. | L-threonine 3-dehydrogenase; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate; Belongs to the zinc-containing alcohol dehydrogenase family. | 0.907 |
| ANL61044.1 | thrC | AMC85_CH03710 | AMC85_CH01049 | Pyridoxal phosphate-dependent threonine dehydratase protein; Protein involved in catalytic activity, pyridoxal phosphate binding and metabolic process. | Protein involved in threonine synthase activity, pyridoxal phosphate binding and threonine biosynthetic process. | 0.955 |
| ANL61686.1 | ANL61044.1 | AMC85_CH04367 | AMC85_CH03710 | Pyridoxal phosphate-dependent serine/threonine dehydratase protein; Protein involved in catalytic activity, pyridoxal phosphate binding and metabolic process. | Pyridoxal phosphate-dependent threonine dehydratase protein; Protein involved in catalytic activity, pyridoxal phosphate binding and metabolic process. | 0.943 |
| ANL61686.1 | ilvA | AMC85_CH04367 | AMC85_CH01850 | Pyridoxal phosphate-dependent serine/threonine dehydratase protein; Protein involved in catalytic activity, pyridoxal phosphate binding and metabolic process. | 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. | 0.925 |
| ANL61686.1 | ltaE | AMC85_CH04367 | AMC85_CH03743 | Pyridoxal phosphate-dependent serine/threonine dehydratase protein; Protein involved in catalytic activity, pyridoxal phosphate binding and metabolic process. | Low-specificity threonine aldolase; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. | 0.911 |
| ANL61686.1 | tdh | AMC85_CH04367 | AMC85_CH03108 | Pyridoxal phosphate-dependent serine/threonine dehydratase protein; Protein involved in catalytic activity, pyridoxal phosphate binding and metabolic process. | L-threonine 3-dehydrogenase; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate; Belongs to the zinc-containing alcohol dehydrogenase family. | 0.907 |
| ANL61686.1 | thrC | AMC85_CH04367 | AMC85_CH01049 | Pyridoxal phosphate-dependent serine/threonine dehydratase protein; Protein involved in catalytic activity, pyridoxal phosphate binding and metabolic process. | Protein involved in threonine synthase activity, pyridoxal phosphate binding and threonine biosynthetic process. | 0.965 |
| hemA-1 | kbl | AMC85_CH04104 | AMC85_CH03109 | 5-aminolevulinate synthase 1; Protein involved in catalytic activity, pyridoxal phosphate binding and tetrapyrrole biosynthetic process. | 2-amino-3-ketobutyrate coenzyme A ligase; Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA. | 0.917 |
| hemA-1 | ltaE | AMC85_CH04104 | AMC85_CH03743 | 5-aminolevulinate synthase 1; Protein involved in catalytic activity, pyridoxal phosphate binding and tetrapyrrole biosynthetic process. | Low-specificity threonine aldolase; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. | 0.916 |
| hemA-1 | tdh | AMC85_CH04104 | AMC85_CH03108 | 5-aminolevulinate synthase 1; Protein involved in catalytic activity, pyridoxal phosphate binding and tetrapyrrole biosynthetic process. | L-threonine 3-dehydrogenase; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate; Belongs to the zinc-containing alcohol dehydrogenase family. | 0.668 |
| ilvA | ANL61044.1 | AMC85_CH01850 | AMC85_CH03710 | 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. | Pyridoxal phosphate-dependent threonine dehydratase protein; Protein involved in catalytic activity, pyridoxal phosphate binding and metabolic process. | 0.924 |
| ilvA | ANL61686.1 | AMC85_CH01850 | AMC85_CH04367 | 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. | Pyridoxal phosphate-dependent serine/threonine dehydratase protein; Protein involved in catalytic activity, pyridoxal phosphate binding and metabolic process. | 0.925 |
| ilvA | ltaE | AMC85_CH01850 | AMC85_CH03743 | 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. | Low-specificity threonine aldolase; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. | 0.911 |
| ilvA | tdh | AMC85_CH01850 | AMC85_CH03108 | 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. | L-threonine 3-dehydrogenase; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate; Belongs to the zinc-containing alcohol dehydrogenase family. | 0.907 |
| ilvA | thrC | AMC85_CH01850 | AMC85_CH01049 | 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. | Protein involved in threonine synthase activity, pyridoxal phosphate binding and threonine biosynthetic process. | 0.957 |
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