ID   PR450_PENRF             Reviewed;         461 AA.
AC   W6Q9B3;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=Conidiogenone synthase PrP450 {ECO:0000303|PubMed:30343633};
DE            EC=1.-.-.- {ECO:0000269|PubMed:30343633};
DE   AltName: Full=Conidiogenone biosynthesis cluster protein PrP450 {ECO:0000303|PubMed:30343633};
DE   AltName: Full=Cytochrome P450 monooxygenase PrP450 {ECO:0000303|PubMed:30343633};
GN   Name=PrP450 {ECO:0000303|PubMed:30343633}; ORFNames=PROQFM164_S02g003151;
OS   Penicillium roqueforti (strain FM164).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1365484;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FM164;
RX   PubMed=24407037; DOI=10.1038/ncomms3876;
RA   Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA   Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA   Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT   "Multiple recent horizontal transfers of a large genomic region in cheese
RT   making fungi.";
RL   Nat. Commun. 5:2876-2876(2014).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=30343633; DOI=10.1080/09168451.2018.1536518;
RA   Shiina T., Nakagawa K., Fujisaki Y., Ozaki T., Liu C., Toyomasu T.,
RA   Hashimoto M., Koshino H., Minami A., Kawaide H., Oikawa H.;
RT   "Biosynthetic study of conidiation-inducing factor conidiogenone:
RT   heterologous production and cyclization mechanism of a key bifunctional
RT   diterpene synthase.";
RL   Biosci. Biotechnol. Biochem. 83:192-201(2019).
CC   -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of conidiogenone, a diterpene known to induce
CC       the conidiation (PubMed:30343633). The bifunctional terpene synthase
CC       PrDS converts isopentenyl diphosphate (IPP) and dimethylallyl
CC       diphosphate (DMAPP) into deoxyconidiogenol (PubMed:30343633). The C-
CC       terminal prenyltransferase (PT) domain of PrDS catalyzes formation of
CC       GGPP, whereas the N-terminal terpene cyclase (TC) domain catalyzes the
CC       cyclization of GGPP into deoxyconidiogenol (PubMed:30343633). The
CC       cytochrome P450 monooxygenase PrP450 then catalyzes two rounds of
CC       oxidation to furnish conidiogenone (PubMed:30343633).
CC       {ECO:0000269|PubMed:30343633}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000269|PubMed:30343633}.
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; HG792016; CDM33000.1; -; Genomic_DNA.
DR   SMR; W6Q9B3; -.
DR   STRING; 1365484.W6Q9B3; -.
DR   EnsemblFungi; CDM33000; CDM33000; PROQFM164_S02g003151.
DR   OrthoDB; 1247045at2759; -.
DR   UniPathway; UPA00213; -.
DR   Proteomes; UP000030686; Unassembled WGS sequence.
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   1: Evidence at protein level;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..461
FT                   /note="Conidiogenone synthase PrP450"
FT                   /id="PRO_0000453714"
FT   TRANSMEM        2..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         400
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   461 AA;  52242 MW;  2947AA2F305E00B4 CRC64;
     MLLLWFGFFS FIFGVVIYRL YFHPLSKFPG PKLAALTSLY EFYYNVVLGG RYLWEIERMH
     EKYGPIVRIT PHELHVADPN FYTEIYAGPT RRRDKDPRLV RLAGQPTSMF ATVDHGLHSS
     RRAILNSYFS KKSIAGLEDM IQGKVQKLVK RLSMACDQGT VVKLDAASSA LTADIISEYA
     HGFFPFLLDL SKFIPDKVLE KLWFHAANIL RLQKLVRAQA DVALQNGGKV DGQATMFGAL
     CDPSLPVQER TLDRLQDEGF SLIGGGTETT TGTLKIVMFH LLNEKALLLK LREELEQYPS
     STWADLEKLP YMRGTINEGL RLSGVITRLP RRAPDEALVY KQWTIPPNSL MSTSSHFVHT
     NSDLFPNPLA FDPERWIRAE AAGQRLEHMI VTFSKGSRQC MGNHLALAEL YLVISTLVRR
     FDMDLYGVTA DNIVTHREYG FGVPKERGEG LRVSITRVRD P