| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| eno | pps | BSU33900 | BSU18830 | Enolase; Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis; Belongs to the enolase family. | Putative PEP-dependent enzyme; Might catalyze the phosphorylation of pyruvate to phosphoenolpyruvate. | 0.642 |
| eno | ptsI | BSU33900 | BSU13910 | Enolase; Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis; Belongs to the enolase family. | Phosphotransferase system (PTS) enzyme I; General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr). | 0.564 |
| eno | pyk | BSU33900 | BSU29180 | Enolase; Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis; Belongs to the enolase family. | Pyruvate kinase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; In the C-terminal section; belongs to the PEP-utilizing enzyme family. | 0.999 |
| pps | eno | BSU18830 | BSU33900 | Putative PEP-dependent enzyme; Might catalyze the phosphorylation of pyruvate to phosphoenolpyruvate. | Enolase; Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis; Belongs to the enolase family. | 0.642 |
| pps | ppsB | BSU18830 | BSU18330 | Putative PEP-dependent enzyme; Might catalyze the phosphorylation of pyruvate to phosphoenolpyruvate. | 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. | 0.729 |
| pps | ppsC | BSU18830 | BSU18320 | Putative PEP-dependent enzyme; Might catalyze the phosphorylation of pyruvate to phosphoenolpyruvate. | 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. | 0.755 |
| pps | ppsD | BSU18830 | BSU18310 | Putative PEP-dependent enzyme; Might catalyze the phosphorylation of pyruvate to phosphoenolpyruvate. | 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. | 0.719 |
| pps | ppsE | BSU18830 | BSU18300 | Putative PEP-dependent enzyme; Might catalyze the phosphorylation of pyruvate to phosphoenolpyruvate. | 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. | 0.748 |
| pps | ptsI | BSU18830 | BSU13910 | Putative PEP-dependent enzyme; Might catalyze the phosphorylation of pyruvate to phosphoenolpyruvate. | Phosphotransferase system (PTS) enzyme I; General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr). | 0.915 |
| pps | pyk | BSU18830 | BSU29180 | Putative PEP-dependent enzyme; Might catalyze the phosphorylation of pyruvate to phosphoenolpyruvate. | Pyruvate kinase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; In the C-terminal section; belongs to the PEP-utilizing enzyme family. | 0.737 |
| pps | ykoP | BSU18830 | BSU13360 | Putative PEP-dependent enzyme; Might catalyze the phosphorylation of pyruvate to phosphoenolpyruvate. | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. | 0.577 |
| pps | yobA | BSU18830 | BSU18810 | Putative PEP-dependent enzyme; Might catalyze the phosphorylation of pyruvate to phosphoenolpyruvate. | Hypothetical protein; Evidence 5: No homology to any previously reported sequences. | 0.573 |
| pps | yraK | BSU18830 | BSU26910 | Putative PEP-dependent enzyme; Might catalyze the phosphorylation of pyruvate to phosphoenolpyruvate. | Putative hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the AB hydrolase superfamily. | 0.607 |
| ppsB | pps | BSU18330 | BSU18830 | 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. | Putative PEP-dependent enzyme; Might catalyze the phosphorylation of pyruvate to phosphoenolpyruvate. | 0.729 |
| 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. | 0.953 |
| 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. | 0.981 |
| ppsB | ppsE | BSU18330 | BSU18300 | 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 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. | 0.961 |
| ppsC | pps | BSU18320 | BSU18830 | 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. | Putative PEP-dependent enzyme; Might catalyze the phosphorylation of pyruvate to phosphoenolpyruvate. | 0.755 |
| 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. | 0.953 |
| 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 |
