ID   CY089_POSPM             Reviewed;         568 AA.
AC   F1SY83;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=Cytochrome P450 monooxygenase 89 {ECO:0000303|PubMed:21938516};
DE            EC=1.-.-.- {ECO:0000269|PubMed:21938516};
GN   Name=CYP089 {ECO:0000303|PubMed:21938516};
GN   Synonyms=CYP53D2v2 {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; AB573294; BAK09427.1; -; mRNA.
DR   AlphaFoldDB; F1SY83; -.
DR   SMR; F1SY83; -.
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 89"
FT                   /id="PRO_0000451399"
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;  62454 MW;  5F80759764D791D3 CRC64;
     MDSSTSLLPP LGSIILACEG LTSLVPLILS VLVCLVATVT ISPTLLAYFN DPFELRAYPG
     PFLAKFTSAW ISWIISQNRW SETVDLMHRQ HGPIVRLSPD HVSVASPAAF AAVYGHSSGA
     LKAPFYNAFA NFKTRSIFNT RDRAEHSRKR RVEAHMFSPR SIRALEDTAR VHFQVLVRQW
     DALCAPTGKT GRGSAEGTLG TISWKVHGDR VWFDCMPWFN FWSFDTISDL AFGRPFGMLE
     AAKGSAHVSK SNTKSVQAVS QDTSHSDEAQ SELLEIPAME VLSELLDFTV ALAYLPAWVQ
     PVFGRLPMFR DGYDAAPKLA NLSLTAVANR VASQTDRADM LSELLRGRDE EGKPYGLEEL
     STEAELLIIA GGDTTANTSC ATAYYIARDL QIQAKLQAEL DVALDGVESD VAPYDAVKDL
     PYLDAVINEG LRLHSTIGAG LPRVVPSGGM TVLGQHLKEG TVVSSPIYTL HRNEAVWGKN
     ACEFYPERWL EASADAKKEM MQSFAPFSMG PRACLGRSLA LQQLHILLAT IFHRYSLVLE
     NNAPAQLPLR DGFARKPMKC IVGVQRRK