ID   C7D47_PANGI             Reviewed;         363 AA.
AC   H2DH24;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   03-AUG-2022, entry version 26.
DE   RecName: Full=Cytochrome P450 CYP82D47;
DE            EC=1.14.-.-;
OS   Panax ginseng (Korean ginseng).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Araliaceae; Panax.
OX   NCBI_TaxID=4054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX   PubMed=22039120; DOI=10.1093/pcp/pcr150;
RA   Han J.Y., Kim H.J., Kwon Y.S., Choi Y.E.;
RT   "The Cyt P450 enzyme CYP716A47 catalyzes the formation of protopanaxadiol
RT   from dammarenediol-II during ginsenoside biosynthesis in Panax ginseng.";
RL   Plant Cell Physiol. 52:2062-2073(2011).
CC   -!- FUNCTION: Probable heme-thiolate monooxygenase. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- INDUCTION: Down-regulated by methyl jasmonate (MeJA).
CC       {ECO:0000269|PubMed:22039120}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; JN604545; AEY75221.1; -; mRNA.
DR   AlphaFoldDB; H2DH24; -.
DR   SMR; H2DH24; -.
DR   PRIDE; H2DH24; -.
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   2: Evidence at transcript level;
KW   Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..363
FT                   /note="Cytochrome P450 CYP82D47"
FT                   /id="PRO_0000425878"
FT   BINDING         342
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"
SQ   SEQUENCE   363 AA;  41723 MW;  53BE969AACF10E72 CRC64;
     MFAFTPYSSF WVELRKITSL QLLSSRRLEL LKHVRISEME ISMKQLYKIW SKKKDGSGRV
     LVEMKKLFGD LTLNVVLRMV AGKRYFGGGN ANDDEEARRC RRVWREFFRL HGVFVVADSL
     PFLRWLDLGG YEKAMKKTAK EMDNIVSGWL EEHRMKRNSS DEDNTQQDFM DVMLSAVKNV
     DLCGFDADVV IKSTCMVLIA SGTDTVGVEL TWALSLLLNN RHALKKAQEE LDNVVGKQRQ
     VKESDLNNLV YLHAIIKETL RLYPAAQLGV RREFYEDCTV AGYHVPKGTL LAVNLWTLHR
     DPIIWSDPTE FRPERFLNMP KEVDVKGQHF ELIPFGVGRR LCPGIAFGLQ MLHLVLATLL
     HGF