ID   CY219_POSPM             Reviewed;         546 AA.
AC   F1SYI1;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 26.
DE   RecName: Full=Cytochrome P450 monooxygenase 219 {ECO:0000303|PubMed:21938516};
DE            EC=1.-.-.- {ECO:0000305|PubMed:21938516};
DE   Flags: Precursor;
GN   Name=CYP219 {ECO:0000303|PubMed:21938516};
GN   Synonyms=CYP5150D1 {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       testosterone, anthracene, carbazole, pyrene, phenanthrene and trans-
CC       stilbene as substrates for oxidation (PubMed:21938516). These
CC       multifunctional properties against a series of polycyclic aromatic
CC       hydrocarbons (PAHs) suggest that CYP219 would play important roles, at
CC       least in part, in fungal metabolic systems involved in xenobiotic
CC       detoxification (Probable). {ECO:0000269|PubMed:21938516,
CC       ECO:0000305|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; AB573392; BAK09525.1; -; mRNA.
DR   AlphaFoldDB; F1SYI1; -.
DR   SMR; F1SYI1; -.
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..546
FT                   /note="Cytochrome P450 monooxygenase 219"
FT                   /id="PRO_0000451367"
FT   BINDING         487
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        367
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        441
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   546 AA;  61248 MW;  7481599354BE84EA CRC64;
     MATLIVLLYG LLAFGTVWLV RRQSKNHDAH RVMRNIPGPP SRSWMKGNIM QYFTRHGRAF
     QRDVALNYGP VVRLQGPLGR KILYVSDPKA LHTIIIKEEN VFEEPESTLI TFNLLFGDCL
     VGSLGENHRR QRKLLNPVFS VNHMRHMLPM FYNVIFKLRE VVMAKVRGGE KEIDVLEWTG
     RAALELIGQG GLGYSFDPLV SDKEARNEYG DALKAMLPAL MNIESLRQIL PHLVKMGPKW
     FRRLATDIFP NAHVQTVKHV VDTMSKRSQE IFREKKAALK SGDEAVLRQV GEGKDIMSIL
     LRANTAASDA DKLPESQMVA QMSLLVFAAT DTTSNTLAHI LQLLAEHSNV QSKLREELLQ
     SGAGTGNTSY DELMKLPLLD AVCRETLRVH PPATLLVRVP RKDSILPLSE PVIGLDGTII
     KDVPVPEGTE IVIGVFGSNV NKSLWGEDAL EWKPERWLSP LPRAVNDASI PGVYSNLMTF
     LGGKRACIGF KFSEMEMKVV LAVMVSNFVF ELEKEIEWNV AGVDYPTVVW DGDRPQLPLK
     VRVYKS