ID   CY151_POSPM             Reviewed;         497 AA.
AC   F1SYD1;
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 151 {ECO:0000303|PubMed:21938516};
DE            EC=1.-.-.- {ECO:0000269|PubMed:21938516};
GN   Name=CYP151 {ECO:0000303|PubMed:21938516};
GN   Synonyms=CYP512P2 {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 and testosterone as substrates for oxidation,
CC       suggesting that the natural substrate(s) may be structurally related to
CC       steroid compounds. {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; AB573342; BAK09475.1; -; mRNA.
DR   AlphaFoldDB; F1SYD1; -.
DR   SMR; F1SYD1; -.
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   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..497
FT                   /note="Cytochrome P450 monooxygenase 151"
FT                   /id="PRO_0000451362"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         441
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        292
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        397
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   497 AA;  56036 MW;  C17328E1EC79A840 CRC64;
     MTDLVPVYYA FAGVVAALLF YKWQSDPLRA IPTIGPSAPL LSYLGAIRFF KDASGVLQEG
     YDKYNVFKVA MIDRWAVVVS GAKMNEELRS IPDDQMSFMD AADELVQTKY TIAPDVLIHP
     IHITVIKEQL TRNLAPLFHE VVKEVEAAMQ ELIPAKGDDW IEIDGYSTVT QIITRASSRV
     FVGFPLCQNA EYLRIATTYS AEVMKGAMIM SVLPDFLKHI VGPLLPWSRR ALRRAAPFLL
     PIITERRRLL KEYGRDWEDK PNDLLMWIIE EARRVGREDS TDLMVQGIMA SNFTAIHTSS
     LTFTHALYHL AANPEYIQSL REEIEEVIRT DGWTKVSMGS MWKLDSFLKE SHRVNGISGI
     SVMRLALKDV TFSDGTFIPA GTFVAAAATS THHDEENYSD ATVFKPFRFS DMRASESEKN
     KHHYVSTSAE YIGFGHGKHA CPGRFFAANE LKIMLASIVL NYDVKFEDEG KRPANVWFAT
     TVLPAPGAKV MFRKRQT