Protein: NVFH_ASPN1
Sequence: MDVTEIAEQTLNTSCLSPACQQQDYAEIEKRYEAERHQQLQTRGKIPDVNIRTNTRFEQFSKDPWLDDSNKRQQIQYHQRRHNGKHHKVLIIGAGYGGLLFAVRIIQTGAFTADDILMVDTSGGFGGTWYWNRYPGLMCDVESYIYMPLLEETGYMPRAKYASGPELRVHAERIADTWKLSNRAMFGVTVKSLDWDEVGKHWSARGLVLDYEKDQSKKASLHLSADFVMLASGIFASPKIPDFTSILEYHGHMFHTSRWDYGCTGGSPENPKLCKLGDKKVGIIGTGATAIQVVPHLAQYSKELHVFQRTPSAVDKRDNHPTDPVWWNKMLQSEGPGWQKRRMENFNAFTGNEQPQPAVDMIADGWTSMPSFSIIGGSPESNATDYLHRMKAFDFPRQERIRARVRETVHNKEVAEALSPWYPGWCKRPCFHDHYLAAFNRPNVRLIDVRQSGIDHFTPKGLVADGREHEIDVFVFSTGYTTSRSSPGGRADIAITGRNGLTMEHKWQNGLATLHGVITRDFPNLFFPGPSQAGTCLNHTYTLDQLATHVAYIISKTLIKIGAADAGYSPRVVIEPTKEAEEDWAVQVLARAATHGALSQCTPGYYNRDGMASAMKSLSMEDKMKLGRMVSWGEGIGSYMDQIVNWRGQGELRGLEIHCVD
What is the function of this protein?
Chermesin D/asnovolin J monooxidase; part of the gene cluster that mediates the biosynthesis of novofumigatonin, a heavily oxygenated meroterpenoid containing a unique orthoester moiety (PubMed:29968715).  The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase nvfA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (PubMed:29968715).  DMOA is then converted to farnesyl-DMOA by the farnesyltransferase nvfB (PubMed:29968715).  Epoxydation by FAD-dependent monooxygenase nvfK, followed by a protonation-initiated cyclization catalyzed by the terpene cyclase nvfL leads to the production of asnavolin H (PubMed:29968715).  The short chain dehydrogenase nvfC then as a 3-OH dehydrogenase of asnovolin H to yield chemesin D (PubMed:29968715).  There are two branches to synthesize asnovolin A from chemesin D (PubMed:29968715).  In one branch, chemesin D undergoes Baeyer-Villiger oxidation by nvfH, methylation by nvfJ, and enoyl reduction by the nvfM D enoylreductase that reduces the double bond between C-5'and C-6', to form respectively asnovolin I, asnovolin K, and asnovolin A (PubMed:29968715).  In the other branch, the methylation precedes the Baeyer-Villiger oxidation and the enoyl reduction to yield asnovolin A via the asnovolin J intermediate (PubMed:29968715).  Asnovolin A is further converted to fumigatonoid A by the Fe(II)/2-oxoglutarate-dependent dioxygenase nvfI that catalyzes an endoperoxidation reaction (PubMed:29968715).  The alpha/beta hydrolase nvfD then acts as an epimerase that converts fumigatonoid A to its C-5' epimer, which then undergoes spontaneous or nvfD-catalyzed lactonization (PubMed:29968715).  The following step utilizes the ketoreductase nvfG to produce fumigatonoid B (PubMed:29968715).  The dioxygenase nvfE further converts fumigatonoid B into fumigatonoid C (PubMed:29968715).  Finally the Fe(II)/2-oxoglutarate-dependent dioxygenase nvfF catalyzes two rounds of oxidation to transform fumigatonoid C into the end product, novofumigatonin A (PubMed:29968715).
What are the official names of this protein?
Chermesin D/asnovolin J monooxidase nvfH, Baeyer-Villiger monooxygenase nvfH, Novofumigatonin biosynthesis cluster protein H.
What is the protein family that this protein belongs to?
Belongs to the FAD-binding monooxygenase family.
What are the subcellular locations of this protein?
Membrane; Single-pass membrane protein.