| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| comS | srfAA | BSU03500 | BSU03480 | Regulator of genetic competence; Required for the development of competence. | 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 |
| comS | srfAB | BSU03500 | BSU03490 | Regulator of genetic competence; Required for the development of competence. | 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. | 0.989 |
| comS | srfAC | BSU03500 | BSU03510 | Regulator of genetic competence; Required for the development of competence. | Surfactin synthetase; Probably activates a leucine. | 0.961 |
| comS | srfAD | BSU03500 | BSU03520 | Regulator of genetic competence; Required for the development of competence. | Surfactin synthetase; Probable thioesterase involved in the biosynthesis of surfactin; Belongs to the thioesterase family. | 0.968 |
| dhbE | dhbF | BSU31980 | BSU31960 | 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. | 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 |
| 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. | 0.877 |
| 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. | 0.875 |
| 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. | 0.598 |
| 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. | 0.964 |
| 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. | 0.902 |
| 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. | 0.927 |
| 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. | 0.982 |
| dhbE | srfAD | BSU31980 | BSU03520 | 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; Probable thioesterase involved in the biosynthesis of surfactin; Belongs to the thioesterase family. | 0.916 |
| dhbF | dhbE | BSU31960 | BSU31980 | Siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin synthetase; Specifically adenylates threonine and glycine, and loads them onto their corresponding peptidyl carrier domains. | 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 |
| 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. | 0.969 |
| 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. | 0.886 |
| 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. | 0.839 |
| 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. | 0.665 |
| 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. | 0.917 |
| 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. | 0.915 |