ID   CY098_POSPM             Reviewed;         520 AA.
AC   F1SY91;
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 98 {ECO:0000303|PubMed:21938516};
DE            EC=1.-.-.- {ECO:0000269|PubMed:21938516};
GN   Name=CYP098 {ECO:0000303|PubMed:21938516};
GN   Synonyms=CYP5144K1v1 {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 pyrene,
CC       phenanthrene, 3,5-dimethoxy-trans-stilbene and 3,5,4'-trimethoxy-trans-
CC       stilbene as 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; AB573302; BAK09435.1; -; mRNA.
DR   AlphaFoldDB; F1SY91; -.
DR   SMR; F1SY91; -.
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..520
FT                   /note="Cytochrome P450 monooxygenase 98"
FT                   /id="PRO_0000451395"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         445
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   520 AA;  57665 MW;  8E79BA6C2F450677 CRC64;
     MPTTLRMLNN NLLIVIGTFA VCVYIVLQRS KARLPLPPGP RKWPLIGNLL DMPGGRAWLK
     YAEWSREYGS DIIHLSAAGT SILVLNSAEL VNELMEKRSA IYSSRAQLTM LHELMGWKDA
     FSFAPTNPTW RAQRKIFMQA LNPNNAALFH GKQLRATHEL LWRLHKGPAN LFHELHHWAA
     ILIMDITYGI RGDAADPYIE TAVEALDSMA IAGAPGAFLV DAVPLLRHMP EWTPGAGFKR
     QAREWNVLRQ KMANRPFIAA KQQITSGSYT PSLVSNALEA VDKNQDLAEQ EELIKGAAVT
     SYGGGSDTVV AAVSAFVLAI LQHPEIQAKA QRQLDEVLGH GELPSFQDVQ SLPYITALVK
     EVLRHNPVTP LAIPHLLSED DTWDGYWLPK GSIVMANAWA ILHDENTYPD PMPFNPDRFL
     RPDGKLDETV KDPATASFGF GRRLCPGRHI ALSSIWISVA SILACYVIRK EVDAAGREVV
     PDGEWYGGPT LFNRPLPFKC RFTPRSKAAE AIIVSLENTV