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 |
| dhbA | dhbE | BSU32000 | BSU31980 | 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the short-chain dehydrogenases/reductases (SDR) family. | 2,3-dihydroxybenzoate-AMP ligase; Involved in the biosynthesis of the catecholic siderophore bacillibactin. Catalyzes the activation of the carboxylate group of 2,3-dihydroxy-benzoate (DHB), via ATP-dependent PPi exchange reactions, to the acyladenylate. | 0.999 |
| dhbA | ppsA | BSU32000 | BSU18340 | 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the short-chain dehydrogenases/reductases (SDR) 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. | 0.593 |
| dhbA | ppsE | BSU32000 | BSU18300 | 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the short-chain dehydrogenases/reductases (SDR) family. | 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. | 0.762 |
| dhbA | srfAC | BSU32000 | BSU03510 | 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the short-chain dehydrogenases/reductases (SDR) family. | Surfactin synthetase; Probably activates a leucine. | 0.871 |
| dhbA | ybdZ | BSU32000 | BSU31959 | 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the short-chain dehydrogenases/reductases (SDR) family. | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 11112781. | 0.939 |
| dhbE | dhbA | BSU31980 | BSU32000 | 2,3-dihydroxybenzoate-AMP ligase; Involved in the biosynthesis of the catecholic siderophore bacillibactin. Catalyzes the activation of the carboxylate group of 2,3-dihydroxy-benzoate (DHB), via ATP-dependent PPi exchange reactions, to the acyladenylate. | 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the short-chain dehydrogenases/reductases (SDR) family. | 0.999 |
| dhbE | ppsA | BSU31980 | BSU18340 | 2,3-dihydroxybenzoate-AMP ligase; Involved in the biosynthesis of the catecholic siderophore bacillibactin. Catalyzes the activation of the carboxylate group of 2,3-dihydroxy-benzoate (DHB), via ATP-dependent PPi exchange reactions, to the acyladenylate. | 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. | 0.761 |
| dhbE | ppsE | BSU31980 | BSU18300 | 2,3-dihydroxybenzoate-AMP ligase; Involved in the biosynthesis of the catecholic siderophore bacillibactin. Catalyzes the activation of the carboxylate group of 2,3-dihydroxy-benzoate (DHB), via ATP-dependent PPi exchange reactions, to the acyladenylate. | 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. | 0.992 |
| dhbE | srfAC | BSU31980 | BSU03510 | 2,3-dihydroxybenzoate-AMP ligase; Involved in the biosynthesis of the catecholic siderophore bacillibactin. Catalyzes the activation of the carboxylate group of 2,3-dihydroxy-benzoate (DHB), via ATP-dependent PPi exchange reactions, to the acyladenylate. | Surfactin synthetase; Probably activates a leucine. | 0.996 |
| dhbE | ybdZ | BSU31980 | BSU31959 | 2,3-dihydroxybenzoate-AMP ligase; Involved in the biosynthesis of the catecholic siderophore bacillibactin. Catalyzes the activation of the carboxylate group of 2,3-dihydroxy-benzoate (DHB), via ATP-dependent PPi exchange reactions, to the acyladenylate. | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 11112781. | 0.997 |
| ppsA | dhbA | BSU18340 | BSU32000 | 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. | 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the short-chain dehydrogenases/reductases (SDR) family. | 0.593 |
| ppsA | dhbE | BSU18340 | BSU31980 | 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. | 2,3-dihydroxybenzoate-AMP ligase; Involved in the biosynthesis of the catecholic siderophore bacillibactin. Catalyzes the activation of the carboxylate group of 2,3-dihydroxy-benzoate (DHB), via ATP-dependent PPi exchange reactions, to the acyladenylate. | 0.761 |
| ppsA | ppsE | BSU18340 | BSU18300 | 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 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. | 0.974 |
| ppsA | srfAC | BSU18340 | BSU03510 | 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; Probably activates a leucine. | 0.980 |
| ppsA | ybdZ | BSU18340 | BSU31959 | 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. | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 11112781. | 0.965 |
| ppsE | dhbA | BSU18300 | BSU32000 | 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. | 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the short-chain dehydrogenases/reductases (SDR) family. | 0.762 |
| ppsE | dhbE | BSU18300 | BSU31980 | 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. | 2,3-dihydroxybenzoate-AMP ligase; Involved in the biosynthesis of the catecholic siderophore bacillibactin. Catalyzes the activation of the carboxylate group of 2,3-dihydroxy-benzoate (DHB), via ATP-dependent PPi exchange reactions, to the acyladenylate. | 0.992 |
| ppsE | ppsA | BSU18300 | BSU18340 | 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. | 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. | 0.974 |
| ppsE | srfAC | BSU18300 | BSU03510 | 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. | Surfactin synthetase; Probably activates a leucine. | 0.924 |
| ppsE | ybdZ | BSU18300 | BSU31959 | 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. | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 11112781. | 0.999 |
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