ID   CY091_POSPM             Reviewed;         542 AA.
AC   F1SY85;
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 91 {ECO:0000303|PubMed:21938516};
DE            EC=1.-.-.- {ECO:0000269|PubMed:21938516};
DE   Flags: Precursor;
GN   Name=CYP091 {ECO:0000303|PubMed:21938516};
GN   Synonyms=CYP5150D12v1 {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
CC       dehydroabietic acid 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   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AB573296; BAK09429.1; -; mRNA.
DR   AlphaFoldDB; F1SY85; -.
DR   SMR; F1SY85; -.
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; 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.
PE   1: Evidence at protein level;
KW   Glycoprotein; Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..542
FT                   /note="Cytochrome P450 monooxygenase 91"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000451365"
FT   BINDING         482
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        299
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        392
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   542 AA;  60202 MW;  7D5AF5B82846EB65 CRC64;
     MLDILRFVLI CGILWILRRV LLRVFIHSPL DKIPGPPPVS FAKGNLPQLY DRNGWDFIKG
     LGEKYGGVVK INGLYGAKML FVFDPAALSS VVVKDQYVYE RSEDATKSTR LMLGDGLLTS
     QGETHRKQRK LMNPVFSINH MRDMMPIFYQ ISRNLRDAIA SRIDNGEKEI DVLDWMARTA
     LELVGQAGLG YSFDPLVQDK ADAYAEAIKA LVPTAFGLRL YRPLLPIALK IGTPAIRRRI
     LKLIPSTRLQ RMREISDAID AHSKRIFEEK KQALARGDEA VLKQVGAGKD ILSRLMQANM
     TASEEDRLPE NELLGQMSTF IFAGMDTTSG ALAHTLQLLA EHPDVQDKMR AEIVAALGGG
     QEIPYDTLVD LPYLDAVCRE TLRLYAPVTT VNRTAQEDIV LPLSEPIRGT DGNLIQEIPV
     PKGTEVIVGI LASNRNPALW GPDAAEWKPE RWLEPLPDTI NTARVPGVYS HLMTFLGGGR
     ACIGFKFSQL EMKVVLAVLL SSFKFSLSSK EIVWNVAGIQ YPTVGASGKP EMPMKIDRVK
     NT