ID   CY212_POSPM             Reviewed;         545 AA.
AC   F1SYH4;
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 212 {ECO:0000303|PubMed:21938516};
DE            EC=1.-.-.- {ECO:0000305|PubMed:21938516};
DE   Flags: Precursor;
GN   Name=CYP212 {ECO:0000303|PubMed:21938516};
GN   Synonyms=CYP5150D7 {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       and pyrene as 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   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AB573385; BAK09518.1; -; mRNA.
DR   AlphaFoldDB; F1SYH4; -.
DR   SMR; F1SYH4; -.
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   Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase; Signal.
FT   SIGNAL          1..14
FT                   /evidence="ECO:0000255"
FT   CHAIN           15..545
FT                   /note="Cytochrome P450 monooxygenase 212"
FT                   /id="PRO_0000451369"
FT   BINDING         486
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"
SQ   SEQUENCE   545 AA;  61554 MW;  E614D2CCCEF18CF1 CRC64;
     MAAYAWLYCA LALGATWYLQ RYLRQRDAYS VLRNIPGPPS YSWAKGHINQ YFNPRGQAFH
     EEVALNYGSV VKLDGMFGSK LFYVADPKAL HTILIKEENT WEEPDAFLAL NQLMFGDCLV
     GTLGEHHRRQ RKMLNPVFSV NHMRHMLPIF YNVILKLREV ILAKVKAGES EIDVLEWSGR
     AALELIGQGG LGYSFDPLLV NSESRNEYGD ALKSCFPALS KVDILRRYAH YLIKMGPRWF
     RRSVVDMYPN PDVQNIKEVV DTMSAKSYEI FNQKKVALKR GDEAVLRQVG EGKDIMSILI
     KANTAASEDE RLPESELIAQ MSLLVFAATD TTSNTLARIL QLLAEHQEIQ VKLRDEILQS
     SAGGNDISYE ELNRLRLLDA VCRETLRLFP PVTTLRRVPR KDSVLPLSEP IYGVDGRVIN
     EIPVAKGTDV IIGTYGVNVR KQLWGEDSLE WKPERWLSPL PSAVTAAAIP GVYSNIMTFL
     GGKRACIGFK FSEMEMKVVL AVMLSTFTFE RTEKVIQWNI AGVSYPTVEG NSQPQLPLKM
     GLYRP