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 |
| dhbF | pksJ | BSU31960 | BSU17180 | Siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin synthetase; Specifically adenylates threonine and glycine, and loads them onto their corresponding peptidyl carrier domains. | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | 0.999 |
| dhbF | pksL | BSU31960 | BSU17190 | Siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin synthetase; Specifically adenylates threonine and glycine, and loads them onto their corresponding peptidyl carrier domains. | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | 0.970 |
| dhbF | pksM | BSU31960 | BSU17200 | Siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin synthetase; Specifically adenylates threonine and glycine, and loads them onto their corresponding peptidyl carrier domains. | Polyketide synthase; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | 0.999 |
| dhbF | pksN | BSU31960 | BSU17210 | Siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin synthetase; Specifically adenylates threonine and glycine, and loads them onto their corresponding peptidyl carrier domains. | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | 0.999 |
| dhbF | pksR | BSU31960 | BSU17220 | Siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin synthetase; Specifically adenylates threonine and glycine, and loads them onto their corresponding peptidyl carrier domains. | Polyketide synthase; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | 0.987 |
| dhbF | ppsA | BSU31960 | BSU18340 | Siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin synthetase; Specifically adenylates threonine and glycine, and loads them onto their corresponding peptidyl carrier domains. | Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Glu and Orn as part of the biosynthesis of the lipopeptide antibiotic lipastatin. The Orn residue is further epimerized to the D-isomer form. The activation sites for these amino acids consist of individual domains; Belongs to the ATP-dependent AMP-binding enzyme family. | 0.977 |
| dhbF | ppsB | BSU31960 | BSU18330 | Siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin synthetase; Specifically adenylates threonine and glycine, and loads them onto their corresponding peptidyl carrier domains. | Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Tyr and Thr as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The Thr residue is further converted to the D-allo-isomer form. The activation sites for these amino acids consist of individual domains. Belongs to the ATP-dependent AMP-binding enzyme family. | 0.999 |
| dhbF | ppsC | BSU31960 | BSU18320 | Siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin synthetase; Specifically adenylates threonine and glycine, and loads them onto their corresponding peptidyl carrier domains. | Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Glu and Ala/Val as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The Ala/Val residue is further epimerized to the D-isomer form. The activation sites for these amino acids consist of individual domains. Belongs to the ATP-dependent AMP-binding enzyme family. | 0.979 |
| dhbF | ppsD | BSU31960 | BSU18310 | Siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin synthetase; Specifically adenylates threonine and glycine, and loads them onto their corresponding peptidyl carrier domains. | Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Pro, Gln and Tyr as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The Tyr residue is further epimerized to the D-isomer form. The activation sites for these amino acids consist of individual domains. Belongs to the ATP-dependent AMP-binding enzyme family. | 0.978 |
| dhbF | ppsE | BSU31960 | BSU18300 | Siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin synthetase; Specifically adenylates threonine and glycine, and loads them onto their corresponding peptidyl carrier domains. | Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acid Ile as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The activation sites for this amino acid consist of individual domains; Belongs to the ATP-dependent AMP-binding enzyme family. | 0.945 |
| dhbF | srfAA | BSU31960 | BSU03480 | Siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin synthetase; Specifically adenylates threonine and glycine, and loads them onto their corresponding peptidyl carrier domains. | Surfactin synthetase; This protein is a multifunctional enzyme able to activate and polymerize the amino acids Leu, Glu, Asp and Val. Activation sites for these AA consist of individual domains. | 0.999 |
| dhbF | srfAB | BSU31960 | BSU03490 | Siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin synthetase; Specifically adenylates threonine and glycine, and loads them onto their corresponding peptidyl carrier domains. | Surfactin synthetase; This protein is a multifunctional enzyme able to activate and polymerize the amino acids Leu, Glu, Asp and Val. Activation sites for these AA consist of individual domains. | 0.999 |
| dhbF | srfAC | BSU31960 | BSU03510 | Siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin synthetase; Specifically adenylates threonine and glycine, and loads them onto their corresponding peptidyl carrier domains. | Surfactin synthetase; Probably activates a leucine. | 0.999 |
| pksJ | dhbF | BSU17180 | BSU31960 | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | Siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin synthetase; Specifically adenylates threonine and glycine, and loads them onto their corresponding peptidyl carrier domains. | 0.999 |
| pksJ | pksL | BSU17180 | BSU17190 | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | 0.998 |
| pksJ | pksM | BSU17180 | BSU17200 | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | Polyketide synthase; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | 0.999 |
| pksJ | pksN | BSU17180 | BSU17210 | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | 0.999 |
| pksJ | pksR | BSU17180 | BSU17220 | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | Polyketide synthase; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | 0.999 |
| pksJ | ppsA | BSU17180 | BSU18340 | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Glu and Orn as part of the biosynthesis of the lipopeptide antibiotic lipastatin. The Orn residue is further epimerized to the D-isomer form. The activation sites for these amino acids consist of individual domains; Belongs to the ATP-dependent AMP-binding enzyme family. | 0.998 |
| pksJ | ppsB | BSU17180 | BSU18330 | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Tyr and Thr as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The Thr residue is further converted to the D-allo-isomer form. The activation sites for these amino acids consist of individual domains. Belongs to the ATP-dependent AMP-binding enzyme family. | 0.999 |
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