ID   CY067_POSPM             Reviewed;         515 AA.
AC   F1SY68;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 26.
DE   RecName: Full=Cytochrome P450 monooxygenase 67 {ECO:0000303|PubMed:21938516};
DE            EC=1.-.-.- {ECO:0000269|PubMed:21938516};
GN   Name=CYP067 {ECO:0000303|PubMed:21938516};
GN   Synonyms=CYP5348E1v2 {ECO:0000303|PubMed:21938516};
OS   Postia placenta (strain ATCC 44394 / Madison 698-R) (Brown rot fungus)
OS   (Poria monticola).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Dacryobolaceae; Postia.
OX   NCBI_TaxID=561896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION.
RC   STRAIN=ATCC 44394 / Madison 698-R;
RX   PubMed=21938516; DOI=10.1007/s00203-011-0753-2;
RA   Ide M., Ichinose H., Wariishi H.;
RT   "Molecular identification and functional characterization of cytochrome
RT   P450 monooxygenases from the brown-rot basidiomycete Postia placenta.";
RL   Arch. Microbiol. 194:243-253(2012).
CC   -!- FUNCTION: Cytochrome P450 monooxygenase that is able to use delta(6)-
CC       protoilludene as a substrate to produce delta(6)-protoilludene-5-ol.
CC       {ECO:0000250|UniProtKB:F1SYC2}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Secondary metabolite biosynthesis. {ECO:0000305}.
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; AB573279; BAK09412.1; -; mRNA.
DR   AlphaFoldDB; F1SY68; -.
DR   SMR; F1SY68; -.
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; 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.
PE   2: Evidence at transcript level;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..515
FT                   /note="Cytochrome P450 monooxygenase 67"
FT                   /id="PRO_0000451349"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         447
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   515 AA;  58007 MW;  BCFDA733E209793D CRC64;
     MQLPVQLSPP LALAVLSIAA CQIALVWWFQ RKRTNPLPPG PSALPFLGNA HQIPLQYPER
     IFSQWARTYG GVMYLRLFKK SVLILDSVKA AQDLMDKRGA KFSDRPQLTL ITDVFAFKPM
     MFTMPYGDLW RRHRKWYQAS LESKAALDTY NAVQETETCT LLSALVSEPE HFADQVKRFT
     GAILLEIVYG HAVTSVKDDL IRLSDEMMTQ AVSAGSLVAT LLDFFPFLMH IPEWFPGGGF
     KREGARVRHL MRQLLDVPFN EVQQAMLEGS GKACLTTYML EEQAEHGDLT PDDVDNIKGA
     ATLLFIAGTD TTITSLLTFF LAMVLHPEVV HKAQAEIDRV VGRTRLPGLM DRDALPYLDQ
     VLKEVYRWNP PVPLGIPHQV RDDDVYNGRH IPGGSMVVSN IWSMSRDPDT YEDADRFWPE
     RYEGKSPDEL ARSDPRRIVY GFGRRLCPGR FLADSSIWLA VARVIATLDI RKVRDAEGKE
     ITPSAEFISG AVSHPKPFSL DIRPRDEVAA KLIAQ