Your Input: | |||||
srfAA | 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. (3587 aa) | ||||
srfAB | 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. (3583 aa) | ||||
comS | Regulator of genetic competence; Required for the development of competence. (46 aa) | ||||
srfAC | Surfactin synthetase; Probably activates a leucine. (1275 aa) | ||||
srfAD | Surfactin synthetase; Probable thioesterase involved in the biosynthesis of surfactin; Belongs to the thioesterase family. (242 aa) | ||||
pksB | Putative hydrolase; Probably involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism; Belongs to the metallo-beta-lactamase superfamily. (225 aa) | ||||
pksC | malonyl-CoA-acyltransferase involved in polyketide synthesis; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. It catalyzes the transfer of the malonyl-CoA group to the acyl-carrier-protein AcpK (Mal-AcpK); Belongs to the FabD family. (288 aa) | ||||
pksD | Enzyme involved in polyketide synthesis; Probably involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. (324 aa) | ||||
pksE | Enzyme involved in polyketide synthesis; Probably involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. Probably has an acyl transferase activity and could also have a flavin mononucleotide-dependent oxidoreductase activity; In the N-terminal section; belongs to the FabD family. (767 aa) | ||||
acpK | Acyl-carrier protein; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. (82 aa) | ||||
pksF | Decarboxylase converting malonyl-S-AcpK to acetyl-S-AcpK for polyketide synthesis; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. It decarboxylates selectively the malonyl group attached on the acyl-carrier-protein AcpK (Mal-AcpK); Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. (415 aa) | ||||
pksG | acetyl-S-AcpK beta-ketothioester polyketide intermediate transferase; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. It catalyzes the aldol condensation between the acetyl group attached to the acyl-carrier-protein AcpK (Ac-AcpK) and a beta- ketothioester polyketide intermediate linked to one of the consecutive thiolation domains of PksL; Belongs to the thiolase-like superfamily. HMG-CoA synthase family. (420 aa) | ||||
pksH | Dehydratase for polyketide biosynthesis; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. Probably catalyzes the dehydration of the (S)-3-hydroxy-3- methylglutaryl group attached to PksL. (259 aa) | ||||
pksI | Decarboxylase involved in polyketide synthesis; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. May have a role in the decarboxylation of the (S)-3- methylglutaryl group attached to PksL. (249 aa) | ||||
pksJ | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. (5043 aa) | ||||
pksL | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. (4538 aa) | ||||
pksM | Polyketide synthase; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. (4262 aa) | ||||
pksN | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. (5488 aa) | ||||
pksR | Polyketide synthase; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. (2543 aa) | ||||
pksS | Cytochrome P450 of bacillaene metabolism; Involved in the metabolism of the antibiotic polyketide bacillaene which is involved in secondary metabolism. The substrate is dihydrobacillaene. (405 aa) | ||||
ppsE | 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. (1279 aa) | ||||
ppsD | 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. (3603 aa) | ||||
ppsC | 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. (2555 aa) | ||||
ppsB | 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. (2560 aa) | ||||
ppsA | 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. (2561 aa) | ||||
ybdZ | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 11112781. (69 aa) | ||||
dhbB | Isochorismatase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. (312 aa) |