ID   CY253_POSPM             Reviewed;         526 AA.
AC   F2ZAF9;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 26.
DE   RecName: Full=Cytochrome P450 monooxygenase 253 {ECO:0000303|PubMed:21938516};
DE            EC=1.-.-.- {ECO:0000305|PubMed:21938516};
GN   Name=CYP253 {ECO:0000303|PubMed:21938516};
GN   Synonyms=CYP5344B1v2 {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-8-ol.
CC       {ECO:0000250|UniProtKB:F1SY62}.
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}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AB623255; BAK20191.1; -; mRNA.
DR   AlphaFoldDB; F2ZAF9; -.
DR   SMR; F2ZAF9; -.
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..526
FT                   /note="Cytochrome P450 monooxygenase 253"
FT                   /id="PRO_0000451351"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        115..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        306..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         451
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   526 AA;  58881 MW;  4F395B3C0764FAE6 CRC64;
     MPASFLASLR AWIASSTIGQ RILLALALGL LLITARVISK SKGTMPPGPR GLPLLGNIFQ
     LPKLPWYRFT EWKEEFGPIF SLNFAGTPVV VLNSHEVVGD LLERKSTIYS DRPRFIMAGE
     ILTGGMLIVF TGYGKVWRKL RRAGQEGLNV RASEKYQPLQ ESEARLLTTN MLREPAEWDA
     HLQRAAASSI ASAVYAWPPL TKSDDGLVHR IDELMRRLVM AGLPGRYLVE IFPIMKHLPT
     WMAKWKREGL EWHRRDTEMF EGFYDNVARF MASGKYKPSL TAGLIERQEK NGLSKKEVSW
     LAGTMIGAGA ETTAASLSVF MLAMTLYPDV MRKAQAEIDA LVGRERMPTF ADRPHLPYVC
     ALVKEVLRWR PVGPVGVPRR TSEDDWYKGY FIPKGTLVIA NVWAMNRDPA IYPDYDEFRP
     DRFLDASGNE IDIAGTHGQG HVTYGFGRRI CIGMHVANQA LFIDIAALLW AFNIEAPTGP
     DGTPILPSRT DFVDEGLVFR PAAFRCKVTP RIDDVATMLA TLEKNA