ID   CY208_POSPM             Reviewed;         512 AA.
AC   F1SYH1;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=Cytochrome P450 monooxygenase 208 {ECO:0000303|PubMed:21938516};
DE            EC=1.-.-.- {ECO:0000269|PubMed:21938516};
GN   Name=CYP208 {ECO:0000303|PubMed:21938516};
GN   Synonyms=CYP5037B5v2 {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 7-
CC       ethoxycoumarin as a substrate for oxidation.
CC       {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; AB573382; BAK09515.1; -; mRNA.
DR   AlphaFoldDB; F1SYH1; -.
DR   SMR; F1SYH1; -.
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..512
FT                   /note="Cytochrome P450 monooxygenase 208"
FT                   /id="PRO_0000451352"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         438
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   512 AA;  57396 MW;  7AE2DA89734F073C CRC64;
     MSRLFLVLDT GAAVLLVALL FVVYRGRQSA RGPLPPGPRG WPLVGNVFDM PSTNEWNTYM
     SWGEKWGDIV SVTLFGQHIV ILNSVQHAYD MFEKKSNIYS DRPVITMAGE MVGWDRTLAV
     LRYGKRFRET RKLFSQLIGT RNHAERFSHH LEHEVHQFLR RVLREPTSLL KEVRKTTGAV
     ILKMAYGYEV QEGDDPLVDL VDRAVEEFSI STRPGAFLVD TLPVLRHVPA WIPGAGWKKK
     AQVWADDLEM TCNVPYAFTQ QQMSAGTAIP SFTSAHLESN PDPEQEILIK NAAASLYSAG
     ADTTVSAVST FFLAMTCYPE AQRKAQAEID AVIGNDRLPT LADRDKLPYV TALCWEVLRW
     QPVVPLGFPH CPVKDDIHAG YLIPKGTLVS PNIWKFLHDP DTYANPFDFE PERFIASPGK
     TAEKDPRQIV FGFGRRICPG MYLADASLFI SCAMSLAVFD ISKVVRDGKV IEPVIDYTSG
     TISHPRPFEC SIKPRSANAE VLITAMHETR EK