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 protiens in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Pnap_0111 | Pnap_0539 | Pnap_0111 | Pnap_0539 | L-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. | KEGG: bxe:Bxe_B1555 serine O-acetyltransferase. | 0.805 |
| Pnap_0111 | Pnap_0753 | Pnap_0111 | Pnap_0753 | L-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. | TIGRFAM: CDP-diacylglycerol--serine O-phosphatidyltransferase; PFAM: CDP-alcohol phosphatidyltransferase; KEGG: rfr:Rfer_2496 CDP-diacylglycerol--serine O-phosphatidyltransferase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family. | 0.900 |
| Pnap_0111 | Pnap_1720 | Pnap_0111 | Pnap_1720 | L-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. | KEGG: pol:Bpro_2320 CDP-diacylglycerol--serine O-phosphatidyltransferase; TIGRFAM: CDP-diacylglycerol--serine O-phosphatidyltransferase; PFAM: CDP-alcohol phosphatidyltransferase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family. | 0.900 |
| Pnap_0111 | Pnap_2554 | Pnap_0111 | Pnap_2554 | L-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. | KEGG: pol:Bpro_2720 phosphoserine phosphatase SerB; TIGRFAM: phosphoserine phosphatase SerB; HAD-superfamily hydrolase, subfamily IB (PSPase-like); PFAM: Haloacid dehalogenase domain protein hydrolase; HAD-superfamily hydrolase, subfamily IB hypothetical 1. | 0.905 |
| Pnap_0111 | Pnap_3336 | Pnap_0111 | Pnap_3336 | L-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. | L-threonine ammonia-lyase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: pol:Bpro_0952 pyridoxal-5'-phosphate-dependent enzyme, beta subunit. | 0.927 |
| Pnap_0111 | glyA | Pnap_0111 | Pnap_2907 | L-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. | Serine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. | 0.931 |
| Pnap_0111 | ilvA | Pnap_0111 | Pnap_0644 | L-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. | L-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. | 0.917 |
| Pnap_0111 | trpA | Pnap_0111 | Pnap_3047 | L-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, alpha chain; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.916 |
| Pnap_0111 | trpB | Pnap_0111 | Pnap_3046 | L-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 chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.924 |
| Pnap_0539 | Pnap_0111 | Pnap_0539 | Pnap_0111 | KEGG: bxe:Bxe_B1555 serine O-acetyltransferase. | L-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. | 0.805 |
| Pnap_0539 | Pnap_0753 | Pnap_0539 | Pnap_0753 | KEGG: bxe:Bxe_B1555 serine O-acetyltransferase. | TIGRFAM: CDP-diacylglycerol--serine O-phosphatidyltransferase; PFAM: CDP-alcohol phosphatidyltransferase; KEGG: rfr:Rfer_2496 CDP-diacylglycerol--serine O-phosphatidyltransferase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family. | 0.800 |
| Pnap_0539 | Pnap_1720 | Pnap_0539 | Pnap_1720 | KEGG: bxe:Bxe_B1555 serine O-acetyltransferase. | KEGG: pol:Bpro_2320 CDP-diacylglycerol--serine O-phosphatidyltransferase; TIGRFAM: CDP-diacylglycerol--serine O-phosphatidyltransferase; PFAM: CDP-alcohol phosphatidyltransferase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family. | 0.800 |
| Pnap_0539 | Pnap_2554 | Pnap_0539 | Pnap_2554 | KEGG: bxe:Bxe_B1555 serine O-acetyltransferase. | KEGG: pol:Bpro_2720 phosphoserine phosphatase SerB; TIGRFAM: phosphoserine phosphatase SerB; HAD-superfamily hydrolase, subfamily IB (PSPase-like); PFAM: Haloacid dehalogenase domain protein hydrolase; HAD-superfamily hydrolase, subfamily IB hypothetical 1. | 0.824 |
| Pnap_0539 | Pnap_3336 | Pnap_0539 | Pnap_3336 | KEGG: bxe:Bxe_B1555 serine O-acetyltransferase. | L-threonine ammonia-lyase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: pol:Bpro_0952 pyridoxal-5'-phosphate-dependent enzyme, beta subunit. | 0.802 |
| Pnap_0539 | glyA | Pnap_0539 | Pnap_2907 | KEGG: bxe:Bxe_B1555 serine O-acetyltransferase. | Serine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. | 0.822 |
| Pnap_0539 | ilvA | Pnap_0539 | Pnap_0644 | KEGG: bxe:Bxe_B1555 serine O-acetyltransferase. | L-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. | 0.802 |
| Pnap_0539 | trpA | Pnap_0539 | Pnap_3047 | KEGG: bxe:Bxe_B1555 serine O-acetyltransferase. | Tryptophan synthase, alpha chain; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.808 |
| Pnap_0539 | trpB | Pnap_0539 | Pnap_3046 | KEGG: bxe:Bxe_B1555 serine O-acetyltransferase. | Tryptophan synthase, beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.808 |
| Pnap_0753 | Pnap_0111 | Pnap_0753 | Pnap_0111 | TIGRFAM: CDP-diacylglycerol--serine O-phosphatidyltransferase; PFAM: CDP-alcohol phosphatidyltransferase; KEGG: rfr:Rfer_2496 CDP-diacylglycerol--serine O-phosphatidyltransferase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family. | L-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. | 0.900 |
| Pnap_0753 | Pnap_0539 | Pnap_0753 | Pnap_0539 | TIGRFAM: CDP-diacylglycerol--serine O-phosphatidyltransferase; PFAM: CDP-alcohol phosphatidyltransferase; KEGG: rfr:Rfer_2496 CDP-diacylglycerol--serine O-phosphatidyltransferase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family. | KEGG: bxe:Bxe_B1555 serine O-acetyltransferase. | 0.800 |
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