Protein
FAD-dependent monooxygenase DEP2
Organism
Fusarium langsethiae
Function
Part of the gene cluster that mediates the biosynthesis of depudecin, a highly oxidized eleven-carbon linear polyketide that acts as a histone deacetylase (HDAC) inhibitor and makes a small contribution to pathogenesis (PubMed:19737099, PubMed:28460114). The reducing polyketide synthase DEP5 is the central enzyme in depudecin biosynthesis by yielding the backbone polyketide chain (PubMed:19737099). The monooxygenases DEP2 and DEP4, as well as the uncharacterized protein DEP1, then act as tailoring enzymes to modify the intermediate polyketide chain into depudecin (PubMed:19737099).
Similarity
Belongs to the paxM FAD-dependent monooxygenase family.
Sequence
MHDSPPFKVIIVGAGVTGLTLAHCLVKAGIDYALLDKGVVAPGFGTTITLQPHGCRILHQLGCLDAVLAKCDVMGGASCRDPNGKIFTSNDFFGVVRKFAGYDTRTLDRQVFLHELYELLPDKSKVYEKARVEEIIEENSTTRVILADGREFAGDLVVGADGVHSKVREIMWDKANAAHPGMITVEEKRAMVTQYNAIVMASSPVPGISAHDMEVTSNDNYSFLLLCQPDWISIIVHSKLPDDQQCTWPTRRRYTETDMEELVSKIIERPVTGSVVFGELWKRRLKAQMISLEEGVLSHWTFGRIALAGDAVHKVTPNSALGGNTAMEDAVVIANTLHALLAMHPNKKPSDVEVRDAMREKYQNTRVDRARAIVKAGGDLTRQQAYDGWKAYIKQRWLTPIIGLDTLAQKIAGLCVTAPKLAYVDFDERRGILGWQDTLAAEKERESKTQVKVPIKQKKGLSWSTWNGGFEAIVPQILVLWAGLWLAICFFHLVFSGNHVPGFGSEVARFFTVYNETWMHS