ID   CY041_POSPM             Reviewed;         568 AA.
AC   F1SY49;
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 41 {ECO:0000303|PubMed:21938516};
DE            EC=1.-.-.- {ECO:0000269|PubMed:21938516};
GN   Name=CYP041 {ECO:0000303|PubMed:21938516};
GN   Synonyms=CYP53D2v1 {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 3,5-
CC       dimethoxy-trans-stilbene and 3,5,4'-trimethoxy-trans-stilbene as
CC       substrates 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; AB573260; BAK09393.1; -; mRNA.
DR   AlphaFoldDB; F1SY49; -.
DR   SMR; F1SY49; -.
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   Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..568
FT                   /note="Cytochrome P450 monooxygenase 41"
FT                   /id="PRO_0000451398"
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         514
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        321
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        377
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   568 AA;  62596 MW;  3FFA72376A287C40 CRC64;
     MDSSTSLLPP LGSIILACEG LTSLVPLILS VMVCLIATVT ISPTLLAYFN DPFELRAYPG
     PFLARFTSAW ISWIISQNRW SETVDLMHRQ HGPIVRLSPD HVSVASPAAF AAVYGHSSGA
     LKAPFYNAFA NFKIRSIFNT RDRAEHSRKR RVEAHMFSPR SIRALEDTAR VHFQVLVRQW
     DALCAPTGKT VRGSAEGTLG TISWKVHGDR VWFDCMPWFN FWSFDTISDL AFGRPFGMLE
     AAKGSAHVSK SNTKSVQAVS QDTSHSNEAQ SELLEIPAME VLSELLDFTV ALAYLPAWVQ
     PVFGRLPMFR DGYDAAPKLA NLSLTAVANR VASQTDRADM LSELLRGRDE EGKPYGLEEL
     STEAELLIIA GGDTTANTSC ATAYYIARDL QIQAKLQAEL DVALDGVESD VAPYDAVKDL
     PYLDAVINEG LRLHSTIGAG LPRVVPSGGM TVLGQHLKEG TVVSSPIYTL HRNEAVWGKN
     AYEFYPERWL EASADAKKEM MQSFAPFSVG PRACLGRSLA LQQLHILLAT IFHRYSLVLE
     NNAPAQLPLR DGFARKPMKC IVGVQRRK