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 |
| ANP63727.1 | ANP67263.1 | BAU10_01450 | BAU10_20150 | Threonine synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Low-specificity L-threonine aldolase; Low- specificity; catalyzes the formation of acetaldehyde and glycine from L-threonine; acts on L-threonine, L-allo-threonine, L-threo-phenylserine, and L-erythro-phenylserine; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.927 |
| ANP63727.1 | ilvA | BAU10_01450 | BAU10_15045 | Threonine synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | PLP-dependent 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. | 0.973 |
| ANP63727.1 | ilvC | BAU10_01450 | BAU10_15320 | Threonine synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.855 |
| ANP63727.1 | leuD | BAU10_01450 | BAU10_00725 | Threonine synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 3-isopropylmalate dehydratase small subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily. | 0.913 |
| ANP63727.1 | metL | BAU10_01450 | BAU10_13695 | Threonine synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Bifunctional aspartate kinase/homoserine dehydrogenase II; Derived by automated computational analysis using gene prediction method: Protein Homology; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.966 |
| ANP63727.1 | pdxA | BAU10_01450 | BAU10_00695 | Threonine synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 4-hydroxythreonine-4-phosphate dehydrogenase PdxA; Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L- threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP). | 0.906 |
| ANP63727.1 | serC | BAU10_01450 | BAU10_05530 | Threonine synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Phosphoserine transaminase; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily. | 0.946 |
| ANP63727.1 | tdh | BAU10_01450 | BAU10_22370 | Threonine synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.903 |
| ANP63727.1 | thrA | BAU10_01450 | BAU10_01440 | Threonine synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Bifunctional aspartate kinase/homoserine dehydrogenase I; Derived by automated computational analysis using gene prediction method: Protein Homology; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.994 |
| ANP63727.1 | thrB | BAU10_01450 | BAU10_01445 | Threonine synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Homoserine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. | 0.999 |
| ANP67263.1 | ANP63727.1 | BAU10_20150 | BAU10_01450 | Low-specificity L-threonine aldolase; Low- specificity; catalyzes the formation of acetaldehyde and glycine from L-threonine; acts on L-threonine, L-allo-threonine, L-threo-phenylserine, and L-erythro-phenylserine; Derived by automated computational analysis using gene prediction method: Protein Homology. | Threonine synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.927 |
| ANP67263.1 | ilvA | BAU10_20150 | BAU10_15045 | Low-specificity L-threonine aldolase; Low- specificity; catalyzes the formation of acetaldehyde and glycine from L-threonine; acts on L-threonine, L-allo-threonine, L-threo-phenylserine, and L-erythro-phenylserine; Derived by automated computational analysis using gene prediction method: Protein Homology. | PLP-dependent 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. | 0.920 |
| ANP67263.1 | tdh | BAU10_20150 | BAU10_22370 | Low-specificity L-threonine aldolase; Low- specificity; catalyzes the formation of acetaldehyde and glycine from L-threonine; acts on L-threonine, L-allo-threonine, L-threo-phenylserine, and L-erythro-phenylserine; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.900 |
| ilvA | ANP63727.1 | BAU10_15045 | BAU10_01450 | PLP-dependent 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. | Threonine synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.973 |
| ilvA | ANP67263.1 | BAU10_15045 | BAU10_20150 | PLP-dependent 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 L-threonine aldolase; Low- specificity; catalyzes the formation of acetaldehyde and glycine from L-threonine; acts on L-threonine, L-allo-threonine, L-threo-phenylserine, and L-erythro-phenylserine; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.920 |
| ilvA | ilvC | BAU10_15045 | BAU10_15320 | PLP-dependent 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. | 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. | 0.776 |
| ilvA | leuD | BAU10_15045 | BAU10_00725 | PLP-dependent 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. | 3-isopropylmalate dehydratase small subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily. | 0.733 |
| ilvA | metL | BAU10_15045 | BAU10_13695 | PLP-dependent 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. | Bifunctional aspartate kinase/homoserine dehydrogenase II; Derived by automated computational analysis using gene prediction method: Protein Homology; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.795 |
| ilvA | tdh | BAU10_15045 | BAU10_22370 | PLP-dependent 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. | 0.914 |
| ilvA | thrA | BAU10_15045 | BAU10_01440 | PLP-dependent 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. | Bifunctional aspartate kinase/homoserine dehydrogenase I; Derived by automated computational analysis using gene prediction method: Protein Homology; In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.795 |
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