ID   CY124_POSPM             Reviewed;         517 AA.
AC   F1SYB2;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 27.
DE   RecName: Full=Cytochrome P450 monooxygenase 124 {ECO:0000303|PubMed:21938516};
DE            EC=1.-.-.- {ECO:0000269|PubMed:21938516};
GN   Name=CYP124 {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 trans-
CC       stilbene as a substrate for oxidation. {ECO:0000269|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; AB573323; BAK09456.1; -; mRNA.
DR   AlphaFoldDB; F1SYB2; -.
DR   SMR; F1SYB2; -.
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; 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..517
FT                   /note="Cytochrome P450 monooxygenase 124"
FT                   /id="PRO_0000451396"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         453
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   517 AA;  59130 MW;  14EF542097CEF09E CRC64;
     MHSLLVLFVS LLALGALKKH LDFRAAVDKI HNYPGLRFIF GVQSFIFGKR IPYFAAGGLS
     LWDTKHQDFV DHDADIISSV NIFPTCATYM IADAQAIKEI TTNRARFPKP LQQYKILTFF
     GSNIVVTEAD EWKRHRKISA PSFSERNNRL VWDETINIVK ELSDDVWRGK NEVTMDNIVD
     LTVPIALFVI GVAGFGRRMS WVEDFTVPAG HSMPFKDALH LVSNHLWMKV LLPAWFLRSA
     PIPRVRKFHT AYEDLEKYMI EMIQARKTAE KKEERYDLFS SLLDANEEET DGNTKLSDSE
     LMGNIFIYLI AGHETTAHTL AFTFILLALY QDEQEKLYQH IKSVVPDDRL PAYEEMGKLT
     YCYAMLLETL RMFPPVNLIP KQAAEDTTLH TSNMAGEPVA VPCLAGTALA IHTPGLHYNP
     RYWEDPFAFK PARFLGDWPR DAFLPFSAGP RSCLGRRFSE TEAVAVLTYI VARWRIDVKE
     EPQFAGETFE QRKARLLDSK SAITLYPVRA PLVFKRR