ID   C7A29_PANGI             Reviewed;         518 AA.
AC   H2DH21;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=Cytochrome P450 CYP72A219;
DE            EC=1.14.-.-;
DE   AltName: Full=Cytochrome P450 CYP72A129;
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].
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   -!- CAUTION: Reported as CYP72A219 in the publication but submitted as
CC       CYP72A129. {ECO:0000305|PubMed:22039120}.
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DR   EMBL; JN604542; AEY75218.1; -; mRNA.
DR   AlphaFoldDB; H2DH21; -.
DR   SMR; H2DH21; -.
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   2: Evidence at transcript level;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..518
FT                   /note="Cytochrome P450 CYP72A219"
FT                   /id="PRO_0000425876"
FT   TRANSMEM        2..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         465
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   518 AA;  59736 MW;  12DC77027BDC2380 CRC64;
     MELVLKLISS FCAIVVVILL GWRIFNWVWL RPRKLEKYLR NQGFNGNSYR LFFGDVKEMI
     VMLKEAKSKP INLYDDIIPR IIPLNQKIIT NYGKNSFLWL GPKPMVHIMN PDHIKDVLSK
     FYQFQKPRHN PLTKLLATGV ADAEGDRWAK HRKLINPAFH LEKLKNMLPA IYLSSSEIVT
     KWEEMVSTKG QFELDVLPYL ETLTSDVISR TAFGSSYEEG RKIFQLQREQ AELIIQASQT
     IYLPGMRFLP TKRNKRMKEI AKEVKIALKS IINKRLKAME AGERSSHDDL LGILLESNSK
     EIKQHGNTNF GLTVDEVIEE CKLFFFAGQE TTSNLLVWTM ILLSQHQDWQ KRAKEEVLRT
     FGNNKPDFDG LNHLKVVNMI LLEVLRLYPP ILSLDRTIYE EIKLGEISLP AGVILLLPII
     LLHYDQEIWG DDAKEFNPER FSEGVLKATK GRVTYFPFSW GPRICIGQNF AMLEAKMAMA
     MILQRFSFVL SPSYAHAPHA IITLQPQYGA HLILHSLI