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
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| IlvG | gltB | DR97_5812 | DR97_2391 | Thiamine pyrophosphate enzyme, central domain protein; Belongs to the TPP enzyme family | annotation not available | 0.713 |
| IlvG | ilvA1 | DR97_5812 | DR97_3296 | Thiamine pyrophosphate enzyme, central domain protein; Belongs to the TPP enzyme family | 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 | 0.913 |
| IlvG | ilvA2 | DR97_5812 | DR97_468 | Thiamine pyrophosphate enzyme, central domain protein; Belongs to the TPP enzyme family | 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 | 0.913 |
| IlvG | ilvB | DR97_5812 | DR97_2038 | Thiamine pyrophosphate enzyme, central domain protein; Belongs to the TPP enzyme family | Acolac_lg: acetolactate synthase, large subunit, biosynthetic type | 0.851 |
| IlvG | ilvC | DR97_5812 | DR97_2036 | Thiamine pyrophosphate enzyme, central domain protein; Belongs to the TPP enzyme family | 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 | 0.980 |
| IlvG | ilvN | DR97_5812 | DR97_2037 | Thiamine pyrophosphate enzyme, central domain protein; Belongs to the TPP enzyme family | Acetolactate synthase 3 regulatory subunit; Acolac_sm: acetolactate synthase, small subunit | 0.997 |
| IlvG | leuA | DR97_5812 | DR97_4077 | Thiamine pyrophosphate enzyme, central domain protein; Belongs to the TPP enzyme family | 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) | 0.894 |
| IlvG | leuB | DR97_5812 | DR97_4815 | Thiamine pyrophosphate enzyme, central domain protein; Belongs to the TPP enzyme family | 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 | 0.969 |
| IlvG | leuC | DR97_5812 | DR97_4812 | Thiamine pyrophosphate enzyme, central domain protein; Belongs to the TPP enzyme family | 3-isopropylmalate/(R)-2-methylmalate dehydratase large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate | 0.668 |
| IlvG | leuD | DR97_5812 | DR97_4813 | Thiamine pyrophosphate enzyme, central domain protein; Belongs to the TPP enzyme family | 3-isopropylmalate/(R)-2-methylmalate dehydratase small subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate | 0.561 |
| gltB | IlvG | DR97_2391 | DR97_5812 | annotation not available | Thiamine pyrophosphate enzyme, central domain protein; Belongs to the TPP enzyme family | 0.713 |
| gltB | ilvA1 | DR97_2391 | DR97_3296 | annotation not available | 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 | 0.514 |
| gltB | ilvA2 | DR97_2391 | DR97_468 | annotation not available | 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 | 0.520 |
| gltB | ilvB | DR97_2391 | DR97_2038 | annotation not available | Acolac_lg: acetolactate synthase, large subunit, biosynthetic type | 0.750 |
| gltB | ilvC | DR97_2391 | DR97_2036 | annotation not available | 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 | 0.810 |
| gltB | ilvN | DR97_2391 | DR97_2037 | annotation not available | Acetolactate synthase 3 regulatory subunit; Acolac_sm: acetolactate synthase, small subunit | 0.891 |
| gltB | leuA | DR97_2391 | DR97_4077 | annotation not available | 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) | 0.507 |
| gltB | leuB | DR97_2391 | DR97_4815 | annotation not available | 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 | 0.964 |
| gltB | leuC | DR97_2391 | DR97_4812 | annotation not available | 3-isopropylmalate/(R)-2-methylmalate dehydratase large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate | 0.918 |
| gltB | leuD | DR97_2391 | DR97_4813 | annotation not available | 3-isopropylmalate/(R)-2-methylmalate dehydratase small subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate | 0.846 |
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