ID   CY231_POSPM             Reviewed;         567 AA.
AC   F1SYI9;
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 231 {ECO:0000303|PubMed:21938516};
DE            EC=1.-.-.- {ECO:0000305|PubMed:21938516};
GN   Name=CYP231 {ECO:0000303|PubMed:21938516};
GN   Synonyms=CYP5027B1 {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], IDENTIFICATION, FUNCTION, AND CATALYTIC
RP   ACTIVITY.
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 anthracene,
CC       carbazole, pyrene, and phenanthrene as substrates for oxidation
CC       (PubMed:21938516). These multifunctional properties against a series of
CC       polycyclic aromatic hydrocarbons (PAHs) suggest that CYP231 would play
CC       important roles, at least in part, in fungal metabolic systems involved
CC       in xenobiotic detoxification (Probable). {ECO:0000269|PubMed:21938516,
CC       ECO:0000305|PubMed:21938516}.
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; AB573400; BAK09533.1; -; mRNA.
DR   AlphaFoldDB; F1SYI9; -.
DR   SMR; F1SYI9; -.
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   1: Evidence at protein level;
KW   Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..567
FT                   /note="Cytochrome P450 monooxygenase 231"
FT                   /id="PRO_0000451368"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         475
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"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        223
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   567 AA;  64009 MW;  BB1B14E516C4A7F4 CRC64;
     MDVSTNELAI LAIVLLATGV LFYAKGTRRA PLPPGPRGIP FFGNLFQVDA MRPYPQYLKW
     AQKYGPVVSI KLGGQHVIVL NSSEAADELL VTRSKQYSSR ESPHVAFDLV SDQQQMLFMP
     YGREWKIVRK NVHGLLGPGS SKQMRKMQDL ESRVILHDLL CHGETSISED FVEGPHGEVP
     ERHWFSIIRR YTTSLMMTLM YGHRIHRIVD NPELHQVYAV VSNFTHVSQP GRYLVDVFPV
     LRRLPDIMAP WRAEGKKMHE WEMGFWGKLF SDSRTALLDG SGLDGFVQSY LRSRAEAGCE
     DLPGKGVTED AAGWMRDKLV TYTASGIIEA GSDTTSTAMF SFVLLMLSNP DALQRAKEEM
     DAVVGSSRMP GWEDEDRLPW LKACIKETLR RAPPLPLGVP HKTEEDDVYN GRLIPKGSTV
     IGNIWAIHMD PIRYPNPTSF KPERFYHPDE KLDWASGPDT HDRDHYIFGW GRRFCSGKHI
     AEASLFIVLS RLIWGFDLYT GSDAKTGQAR LPDVNDEATF TDGLVAAPKI YPVGFKPRSE
     KHAEMIKASY RDVQNDWQSM GLAGDER