ID   BTCC_NEOBT              Reviewed;         510 AA.
AC   A0A2Z6FZ20;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2018, sequence version 1.
DT   03-AUG-2022, entry version 7.
DE   RecName: Full=Cytochrome P450 monooxygenase btcC {ECO:0000303|Ref.2};
DE            EC=1.-.-.- {ECO:0000305|Ref.2};
DE   AltName: Full=Betaestacins biosynthesis cluster protein C {ECO:0000303|Ref.2};
GN   Name=btcC {ECO:0000303|PubMed:29185768};
OS   Neocamarosporium betae (Beet black rot fungus) (Pleospora betae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Neocamarosporium.
OX   NCBI_TaxID=1979465;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PS-13;
RX   PubMed=29185768; DOI=10.1021/acs.orglett.7b03418;
RA   Narita K., Sato H., Minami A., Kudo K., Gao L., Liu C., Ozaki T.,
RA   Kodama M., Lei X., Taniguchi T., Monde K., Yamazaki M., Uchiyama M.,
RA   Oikawa H.;
RT   "Focused genome mining of structurally related sesterterpenes: enzymatic
RT   formation of enantiomeric and diastereomeric products.";
RL   Org. Lett. 19:6696-6699(2017).
RN   [2]
RP   FUNCTION, AND PATHWAY.
RX   DOI=10.1016/j.tetlet.2018.02.022;
RA   Gao L., Narita K., Ozaki T., Kamukara N., Gan P., Minami A., Liu C.,
RA   Lei X., Shirasu K., Oikawa H.;
RT   "Identification of novel sesterterpenes by genome mining of phytopathogenic
RT   fungi Phoma and Colletotrichum sp.";
RL   Tetrahedron Lett. 59:1136-1139(2018).
CC   -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of betaestacins (PubMed:29185768, Ref.2). The
CC       bifunctional terpene synthase btcA converts isopentenyl diphosphate
CC       (IPP) and dimethylallyl diphosphate (DMAPP) into the sesterterpene
CC       betaestacin I (PubMed:29185768, Ref.2). The C-terminal
CC       prenyltransferase (PT) domain of btcA catalyzes formation of GFPP,
CC       whereas the N-terminal terpene cyclase (TC) domain catalyzes the
CC       cyclization of GFPP into betaestacin I (PubMed:29185768, Ref.2). The
CC       cytochrome P450 monooxygenase btcB is then responsible for the six-step
CC       oxidation of betaestacin I to yield betaestacin II (Ref.2). The roles
CC       of the cytochrome P450 monooxygenase btcC and the alpha-ketoglutarate-
CC       dependent dioxygenase btcD have not been identified yet (Probable).
CC       {ECO:0000269|PubMed:29185768, ECO:0000269|Ref.2, ECO:0000305|Ref.2}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000305|Ref.2}.
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; LC274619; BBE36500.1; -; Genomic_DNA.
DR   SMR; A0A2Z6FZ20; -.
DR   UniPathway; UPA00213; -.
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   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..510
FT                   /note="Cytochrome P450 monooxygenase btcC"
FT                   /id="PRO_0000453710"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         446
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   510 AA;  57030 MW;  AF96FE93CB1CD81F CRC64;
     MSFPGVIFVV SFFPLLMGIA VYRLLWHPLA SFKGPKLAAV TDWWFCKKWL NGRYHQTLEK
     LQLQYGDVIR IAPNELVFAT PEAARDIYTR CNPDQDLQFI KQPPFYKQSE GFPTLVTETD
     PAAHRTLRKP LERGFSPSSL KDYGRVIERV ADDLTAQLEK ASEHSNAVDV KAWAARFTFD
     VITEVTFGKS SGTVAQGKNT VWLDLLTGNI AAAAVGVAIR RQPHAVKTLL RSIFAKLSKT
     AKLRAQYLSV CRKMCEERLR DPPKAANLFD HVLATCPPVE KDADNHGYLV FLQGQAAALV
     SGGTETSSTL LSSLIYNLLA HPAHLARLQY EVRNAFSQSG EIDIESTKQL KYLQAVIDES
     LRIFPPVGFG LPRVCPGAMI GGVYVPKGTV VQAPDILMVR NSRYFVRPYE FLPERWLPKD
     HEFYDEQFSG DRKEASKPFS LGPRQCIGMS LAYAEWRIVL AKLVLKFDWE IIGETQDLMD
     VARLKLLWEM PPILVSFKPV GGLAAASPGA