ID   CY215_POSPM             Reviewed;         547 AA.
AC   F1SYH7;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Cytochrome P450 monooxygenase 215 {ECO:0000303|PubMed:21938516};
DE            EC=1.-.-.- {ECO:0000269|PubMed:21938516};
GN   Name=CYP215 {ECO:0000303|PubMed:21938516};
GN   Synonyms=CYP5139D5v1 {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 7-
CC       ethoxycoumarin, anthracene, phenanthrene and 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; AB573388; BAK09521.1; -; mRNA.
DR   AlphaFoldDB; F1SYH7; -.
DR   SMR; F1SYH7; -.
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; IPR002403; Cyt_P450_E_grp-IV.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..547
FT                   /note="Cytochrome P450 monooxygenase 215"
FT                   /id="PRO_0000451355"
FT   TRANSMEM        9..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         483
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        52
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        336
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        438
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   547 AA;  61551 MW;  4CCA0A392F932A0D CRC64;
     MLTLAVHDIL WAVGAALLAC AAFKIIRVLL LPYTSSLRDL PGPPASSWLL GNVSELMAAE
     DFALHFEWLE KYGPTMKYNV WFKLPELLTI DARAINHVLS HSQDYPKPEE TRVSLVEILG
     NGLVVAEGEL HRRQRRIMNP AFGPAQIREL TEIFVDKAQQ LRDIWRNEVT TCGGTVRIDV
     QSGLTKMTLD AIGLAGFNYN FNALNPDGKA NELNRAFEMM FQRMADLERS YWLIIRSLIP
     ILRYIPDGYT RDTAAAQKVT RRIGMQLIAE KKAAVRQAAQ SGEKNAGSEL RSRDLLTLLI
     KANMSPDIPE DQRLSDDDVL AQVPTFLVAG HETTSNATTW CLYALSQQPN VQHKLREELW
     GVPTDSPSME ELNALPYLDA VIRETMRLFP PIAGTVRIAT KDDEIPLATP YMDAKGRMHD
     SIRIDKGTAF PIPIIGMNRS KALWGEDARE FRPERWGSIP EAAQQIPGVW SNLMTFIGGP
     RACIGYRFSL IEMKALVFTL VRAFEFELAV PVEDITKKIG LVQRPFVRSE MEKGTQMPLI
     IKSHTRE