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 |
| ppsA | ppsB | BSU18340 | BSU18330 | 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. | 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. | 0.968 |
| ppsA | ppsC | BSU18340 | BSU18320 | 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. | 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. | 0.867 |
| ppsA | ppsD | BSU18340 | BSU18310 | 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. | 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. | 0.798 |
| ppsA | srfAA | BSU18340 | BSU03480 | 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. | 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. | 0.831 |
| ppsA | srfAB | BSU18340 | BSU03490 | 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. | 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. | 0.970 |
| ppsB | ppsA | BSU18330 | BSU18340 | 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. | 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. | 0.968 |
| ppsB | ppsC | BSU18330 | BSU18320 | 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. | 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. | 0.947 |
| ppsB | ppsD | BSU18330 | BSU18310 | 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. | 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. | 0.964 |
| ppsB | srfAA | BSU18330 | BSU03480 | 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. | 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. | 0.913 |
| ppsB | srfAB | BSU18330 | BSU03490 | 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. | 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 |
| ppsC | ppsA | BSU18320 | BSU18340 | 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. | 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. | 0.867 |
| ppsC | ppsB | BSU18320 | BSU18330 | 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. | 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. | 0.947 |
| ppsC | ppsD | BSU18320 | BSU18310 | 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. | 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. | 0.825 |
| ppsC | srfAA | BSU18320 | BSU03480 | 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. | 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. | 0.904 |
| ppsC | srfAB | BSU18320 | BSU03490 | 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. | 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. | 0.976 |
| ppsD | ppsA | BSU18310 | BSU18340 | 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. | 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. | 0.798 |
| ppsD | ppsB | BSU18310 | BSU18330 | 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. | 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. | 0.964 |
| ppsD | ppsC | BSU18310 | BSU18320 | 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. | 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. | 0.825 |
| ppsD | srfAA | BSU18310 | BSU03480 | 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. | 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. | 0.821 |
| ppsD | srfAB | BSU18310 | BSU03490 | 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. | 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. | 0.967 |
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