node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
dhbB | dhbE | BSU31970 | BSU31980 | Isochorismatase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | 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 |
dhbB | pksJ | BSU31970 | BSU17180 | Isochorismatase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | 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 |
dhbB | pksM | BSU31970 | BSU17200 | Isochorismatase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | Polyketide synthase; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | 0.850 |
dhbB | pksN | BSU31970 | BSU17210 | Isochorismatase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | 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 |
dhbB | pksR | BSU31970 | BSU17220 | Isochorismatase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | Polyketide synthase; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | 0.694 |
dhbB | ppsB | BSU31970 | BSU18330 | Isochorismatase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | 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. | 0.931 |
dhbB | ppsE | BSU31970 | BSU18300 | Isochorismatase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | 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. | 0.999 |
dhbB | srfAA | BSU31970 | BSU03480 | Isochorismatase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | 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. | 0.953 |
dhbB | srfAB | BSU31970 | BSU03490 | Isochorismatase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | 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. | 0.984 |
dhbB | ybdZ | BSU31970 | BSU31959 | Isochorismatase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 11112781. | 0.999 |
dhbE | dhbB | BSU31980 | BSU31970 | 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. | Isochorismatase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | 0.999 |
dhbE | pksJ | BSU31980 | BSU17180 | 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. | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | 0.899 |
dhbE | pksM | BSU31980 | BSU17200 | 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. | Polyketide synthase; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | 0.715 |
dhbE | pksN | BSU31980 | BSU17210 | 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. | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | 0.901 |
dhbE | pksR | BSU31980 | BSU17220 | 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. | Polyketide synthase; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | 0.624 |
dhbE | ppsB | BSU31980 | BSU18330 | 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 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. | 0.990 |
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 | srfAA | BSU31980 | BSU03480 | 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; 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. | 0.992 |
dhbE | srfAB | BSU31980 | BSU03490 | 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; 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. | 0.993 |
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 |