ID   CY105_POSPM             Reviewed;         521 AA.
AC   F1SY96;
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 105 {ECO:0000303|PubMed:21938516};
DE            EC=1.-.-.- {ECO:0000269|PubMed:21938516};
GN   Name=CYP105 {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, pyrene, phenanthrene and trans-stilbene as substrates for
CC       oxidation (PubMed:21938516). These multifunctional properties against a
CC       series of polycyclic aromatic hydrocarbons (PAHs) suggest that CYP105
CC       would play important roles, at least in part, in fungal metabolic
CC       systems involved in xenobiotic detoxification (Probable).
CC       {ECO:0000269|PubMed:21938516, 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; AB573307; BAK09440.1; -; mRNA.
DR   AlphaFoldDB; F1SY96; -.
DR   SMR; F1SY96; -.
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..521
FT                   /note="Cytochrome P450 monooxygenase 105"
FT                   /id="PRO_0000451370"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         449
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        218
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        274
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        317
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   521 AA;  58110 MW;  CE791B98C8076E3A CRC64;
     MQTSGLTLEP PGVASPATLA VAAVTFLTAL VLYELFTYRK RRSMPPGPFR WPFIGNTLQI
     PQVHPWLTYS RWAQVYGDIL HLDALGQHII VINSAKIARE LLDKRSAIYS GRPHLVMAGD
     LAGQDRLLIL QPYGDEFRQQ RRFISQDLSV AAVRRYYDIQ EAAARRLVLG VINDPGSLES
     QIKVNIASII MLVTYGYTVK GTDDPFITRP FEVMDNFNAS MTPGVWIVDM IPQLKYLPLW
     TPGATFLKTA KVWRKHLFTT NWMVYSWSKE SSENGTARVP NLCASVLTEM EGKVTPQLEE
     SLMWAAGTVL GGGLDTNIST ILSFILAMLR FPDVQRKAQV EIDAVVGSER LPEISDRPSL
     PYIRSVVTEV YRWLPAIPLC IPHALTEDDV YNGVFLPKGS VVMPNVWHML HDPTIYPDPD
     AFKPERYGGL DSEMKKVTDL AFGFGRRACP GYQFAQGTIF TIVATMLATC DIVPVVDEHG
     QNSIPDVGYT TGTIIFPVDV KCTFRPRTEQ ARAALVEASV L