ID   CY226_POSPM             Reviewed;         526 AA.
AC   F1SYI7;
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 226 {ECO:0000303|PubMed:21938516};
DE            EC=1.-.-.- {ECO:0000269|PubMed:21938516};
GN   Name=CYP226 {ECO:0000303|PubMed:21938516};
GN   Synonyms=CYP5350B9 {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 anthracene,
CC       carbazole and phenanthrene as substrates for oxidation
CC       (PubMed:21938516). These multifunctional properties against a series of
CC       polycyclic aromatic hydrocarbons (PAHs) suggest that CYP226 would play
CC       important roles, at least in part, in fungal metabolic systems involved
CC       in xenobiotic 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   -!- 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; AB573398; BAK09531.1; -; mRNA.
DR   AlphaFoldDB; F1SYI7; -.
DR   SMR; F1SYI7; -.
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..526
FT                   /note="Cytochrome P450 monooxygenase 226"
FT                   /id="PRO_0000451371"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         452
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        219
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        277
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        320
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   526 AA;  58243 MW;  979DCE66EFAAA4CF CRC64;
     MQASDPIPPQ LGVPFATSYA ALTVAAVTLL AALLVHELSA YSKRRSMPPG PFRWPLIGNA
     LQMPQIHPWL TFSRWARVYG DIFYLDALGQ HIVVINSATV ARELLDRRSS IYSGRPHLTM
     VGDLAGYDRM IVMQPYGDEL RQQRRLISQT LSTSTIGQYY DIQEAAARRL VLGVIDDPSS
     LEGQIKMNIA SIIMLVTYGY TVKGTEDVFF GRAIEIMDNL TLAARPGVWL ADMIPQLKYF
     PSWMPGLSSL KAAEAWRKLL HTTNGMVYQW CKENSENGTA HLPNLCASVL AQAEGKATLQ
     LEESLMWAAL TVLSGGLDTN ISTILSFILA MLHYPDVQKK AQAEIDAVVG SGRLPQISDK
     SSLPYIRSVI AESYRWLPAT PLSVPHALDE DDIYDGSFLP KGSIIMPNVW HMLHDPKIYP
     EPDAFKPERY GGSDIEMKKV TDIAFGFGRR ACPGFYFAEG TIFSIVVTVL ATCDIVPVVN
     DHGQEIIPDI RYSTNVVLCP EDVKCTFRPR SEQAKSALID SMTGVL