ID   CY176_POSPM             Reviewed;         520 AA.
AC   F1SYF1;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=Cytochrome P450 monooxygenase 176 {ECO:0000303|PubMed:21938516};
DE            EC=1.-.-.- {ECO:0000269|PubMed:21938516, ECO:0000269|PubMed:30105900};
GN   Name=CYP176 {ECO:0000303|PubMed:21938516};
GN   Synonyms=CYP5348J3 {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).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 44394 / Madison 698-R;
RX   PubMed=30105900; DOI=10.1111/1751-7915.13304;
RA   Ichinose H., Kitaoka T.;
RT   "Insight into metabolic diversity of the brown-rot basidiomycete Postia
RT   placenta responsible for sesquiterpene biosynthesis: semi-comprehensive
RT   screening of cytochrome P450 monooxygenase involved in protoilludene
RT   metabolism.";
RL   Microb. Biotechnol. 11:952-965(2018).
CC   -!- FUNCTION: Cytochrome P450 monooxygenase that is able to use delta(6)-
CC       protoilludene as a substrate to produce delta(6)-protoilludene-5-ol and
CC       an unidentified hydroxyprotoilludene (PubMed:30105900). Is also able to
CC       use phenanthrene as a substrate for oxidation (PubMed:21938516).
CC       {ECO:0000269|PubMed:21938516, ECO:0000269|PubMed:30105900}.
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; AB573362; BAK09495.1; -; mRNA.
DR   AlphaFoldDB; F1SYF1; -.
DR   SMR; F1SYF1; -.
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   PRINTS; PR00385; P450.
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..520
FT                   /note="Cytochrome P450 monooxygenase 176"
FT                   /id="PRO_0000451347"
FT   TRANSMEM        10..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         445
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        6
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        141
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        270
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        517
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   520 AA;  59160 MW;  7BBB812FB2695256 CRC64;
     MSLVLNRTDL LVVAGALFLT FLTTRFIRAA QRYHLPPGPT RIPLLGNLHQ VPLHDQQKTF
     AEWVKKYGDI IYIQLLSKPF VIVSSVRAAQ DLMEKRAVKY SDRPYFLLLC EFVMTRPLMI
     FMQHGDRWRR LRRWYQGSLE NKSVLEGYRP VLRREIGRLL SSLAEAPQDF MSHIKRYNGA
     VMLDIAYGHR VTSAEDEFMV FADKTISTVT SLGSFAATLV DFFPILRYFP AWTPGSGFKK
     QALMAKEMWD EMEDIPYRKL RHEMGSDAVN RSFTTFMIGE VSHDGKLGAD DEIDIKGSAT
     LMYVAGSDTT MTTMTTFVLA MTLYPEVARK AQAEIDHVVG LSRLPGLDDK DSLPYLECII
     KELYRWNPPV PLGVPHRLCV DDNYRGYDIP GGSMIVPNVW AMSRDPSLYP DTKTFRPERF
     EGLDAQAMKF RDPRKYIFGF GRRICPGRYL ADSNVWLFLA SVLASMDIGR AHDAAGHEII
     PTPSFKDGII SHVEPFQCTI RPRSERAAQL IRESTGNTSA