ID   BRAC_ANNTR              Reviewed;         504 AA.
AC   P9WER2; A0A866WL53;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   29-SEP-2021, sequence version 1.
DT   03-AUG-2022, entry version 4.
DE   RecName: Full=Cytochrome P450 monooxygenase braC {ECO:0000303|PubMed:32936132};
DE            EC=1.-.-.- {ECO:0000269|PubMed:32936132};
DE   AltName: Full=Brasilane terpene glycosides biosynthesis cluster protein C {ECO:0000303|PubMed:32936132};
GN   Name=braC {ECO:0000303|PubMed:32936132};
OS   Annulohypoxylon truncatum (Hypoxylon truncatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Hypoxylaceae; Annulohypoxylon.
OX   NCBI_TaxID=327061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   PATHWAY.
RC   STRAIN=DSM 103480 / CBS 140778;
RX   PubMed=32936132; DOI=10.1039/d0cc03950k;
RA   Feng J., Surup F., Hauser M., Miller A., Wennrich J.P., Stadler M.,
RA   Cox R.J., Kuhnert E.;
RT   "Biosynthesis of oxygenated brasilane terpene glycosides involves a
RT   promiscuous N-acetylglucosamine transferase.";
RL   Chem. Commun. (Camb.) 56:12419-12422(2020).
CC   -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of the brasilane terpene glycosides brasilane
CC       D and E (PubMed:32936132). The biosynthesis starts with the activity of
CC       the terpene cyclase braA that converts farnesyl pyrophosphate into the
CC       sesquiterpene alcohol trichobrasilenol (PubMed:32936132). Subsequently,
CC       trichobrasilenol is glycosylated by the O-glycosyltransferase braB
CC       putatively using UDP-GlcNAc as sugar donor to yield brasilane A
CC       (PubMed:32936132). The latter then undergoes two rounds of oxidation
CC       performed by the cytochrome P450 monooxygenase braC (PubMed:32936132).
CC       In the first round braC hydroxylates C-12 forming brasilane D, which
CC       serves as substrate in the second round to establish the epoxide at the
CC       bond between C-5 and C-10 and oxidize the alcohol at C-12 to an
CC       aldehyde leading to the final product brasilane E (PubMed:32936132).
CC       {ECO:0000269|PubMed:32936132}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:32936132}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; MT383109; QOE88885.1; -; Genomic_DNA.
DR   SMR; P9WER2; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..504
FT                   /note="Cytochrome P450 monooxygenase braC"
FT                   /id="PRO_0000453906"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         448
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P04798"
SQ   SEQUENCE   504 AA;  57587 MW;  BF192ADE7EF5BEA5 CRC64;
     MASLYLPTIW ASTLTAATIF IVAVLSKWLR KPRSFDVPIV GAESGDLNVL KARYVQEADA
     LLREGYEKFK DAIFQVITPD GPRVFLPRKY AHDLKDYSRH EASGMKALAD RHIGHYTTID
     HESDIMLGAI KIDLNRNLGT FVGDVEHEVA FCFETQFPAC DDWTPIDLHD KLLRVVAQAS
     ARIFVGYPMC RNEEWLECST KFALDVMTGG EKLKQWHPYL RPIAQYFVPE MTRIRGDHQR
     ALELLLPELN RRLAEPADPD SSPHNDMIQW MQDRARKTGD NSFDNKELAN LQMLTATAAI
     HTTRLAIIHA LYDLAARPEY VEPLRKEILE ATKDSNGVLQ KQHLTQMKML DSFMKESQRH
     SPPSVATYQR KAMIPITLSN GFHIPAGTIV QCNTNILDET PPDWGDPHAF DGFRFYKLRN
     RTPDDINKFQ FASPTYDSMQ FGFGKDACPG RFFASNQIKI ILAYILSHYD IKFEDSVVGR
     PKNFMFEVNV LADPTKMVLF KKIR