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 |
| IlvM | ilvA | HMPREF0621_0776 | HMPREF0621_0780 | Hypothetical protein; COG: COG3978; 2.2.1.6. | Threonine ammonia-lyase, biosynthetic; 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. | 0.945 |
| IlvM | ilvB | HMPREF0621_0776 | HMPREF0621_0775 | Hypothetical protein; COG: COG3978; 2.2.1.6. | Acetolactate synthase, large subunit, biosynthetic type; COG: COG0028; Pfam: PF02776,PF00205,PF02775; InterPro: IPR012846. | 0.970 |
| IlvM | ilvB-2 | HMPREF0621_0776 | HMPREF0621_1661 | Hypothetical protein; COG: COG3978; 2.2.1.6. | Acetolactate synthase, large subunit, biosynthetic type; COG: COG0028; Pfam: PF02776,PF00205,PF02775; InterPro: IPR012846; overlaps another CDS with the same product name. | 0.920 |
| IlvM | ilvC | HMPREF0621_0776 | HMPREF0621_0723 | Hypothetical protein; COG: COG3978; 2.2.1.6. | Ketol-acid reductoisomerase; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. | 0.956 |
| IlvM | ilvD | HMPREF0621_0776 | HMPREF0621_0779 | Hypothetical protein; COG: COG3978; 2.2.1.6. | Dihydroxy-acid dehydratase; COG: COG0129; Pfam: PF00920; InterPro: IPR004404; Belongs to the IlvD/Edd family. | 0.862 |
| IlvM | ilvE | HMPREF0621_0776 | HMPREF0621_1513 | Hypothetical protein; COG: COG3978; 2.2.1.6. | Branched-chain-amino-acid transaminase; COG: COG0115; Pfam: PF01063; InterPro: IPR001544. | 0.670 |
| IlvM | leuA | HMPREF0621_0776 | HMPREF0621_0234 | Hypothetical protein; COG: COG3978; 2.2.1.6. | 2-isopropylmalate synthase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily. | 0.820 |
| IlvM | leuB | HMPREF0621_0776 | HMPREF0621_0233 | Hypothetical protein; COG: COG3978; 2.2.1.6. | 3-isopropylmalate dehydrogenase; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. | 0.912 |
| aspC2 | ilvD | HMPREF0621_1127 | HMPREF0621_0779 | Aminotransferase AlaT; COG: COG0436; Pfam: PF00155; InterPro: IPR004839. | Dihydroxy-acid dehydratase; COG: COG0129; Pfam: PF00920; InterPro: IPR004404; Belongs to the IlvD/Edd family. | 0.924 |
| aspC2 | ilvE | HMPREF0621_1127 | HMPREF0621_1513 | Aminotransferase AlaT; COG: COG0436; Pfam: PF00155; InterPro: IPR004839. | Branched-chain-amino-acid transaminase; COG: COG0115; Pfam: PF01063; InterPro: IPR001544. | 0.915 |
| aspC2 | leuA | HMPREF0621_1127 | HMPREF0621_0234 | Aminotransferase AlaT; COG: COG0436; Pfam: PF00155; InterPro: IPR004839. | 2-isopropylmalate synthase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily. | 0.918 |
| ilvA | IlvM | HMPREF0621_0780 | HMPREF0621_0776 | Threonine ammonia-lyase, biosynthetic; 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. | Hypothetical protein; COG: COG3978; 2.2.1.6. | 0.945 |
| ilvA | ilvB | HMPREF0621_0780 | HMPREF0621_0775 | Threonine ammonia-lyase, biosynthetic; 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. | 0.943 |
| ilvA | ilvB-2 | HMPREF0621_0780 | HMPREF0621_1661 | Threonine ammonia-lyase, biosynthetic; 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; overlaps another CDS with the same product name. | 0.926 |
| ilvA | ilvC | HMPREF0621_0780 | HMPREF0621_0723 | Threonine ammonia-lyase, biosynthetic; 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. | Ketol-acid reductoisomerase; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. | 0.619 |
| ilvA | ilvD | HMPREF0621_0780 | HMPREF0621_0779 | Threonine ammonia-lyase, biosynthetic; 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: IPR004404; Belongs to the IlvD/Edd family. | 0.864 |
| ilvA | ilvE | HMPREF0621_0780 | HMPREF0621_1513 | Threonine ammonia-lyase, biosynthetic; 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. | 0.899 |
| ilvA | leuB | HMPREF0621_0780 | HMPREF0621_0233 | Threonine ammonia-lyase, biosynthetic; 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. | 3-isopropylmalate dehydrogenase; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. | 0.947 |
| ilvA | leuC | HMPREF0621_0780 | HMPREF0621_0232 | Threonine ammonia-lyase, biosynthetic; 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. | 3-isopropylmalate dehydratase, large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. | 0.533 |
| ilvB | IlvM | HMPREF0621_0775 | HMPREF0621_0776 | Acetolactate synthase, large subunit, biosynthetic type; COG: COG0028; Pfam: PF02776,PF00205,PF02775; InterPro: IPR012846. | Hypothetical protein; COG: COG3978; 2.2.1.6. | 0.970 |
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