ID   C7A10_PANGI             Reviewed;         533 AA.
AC   H2DH22;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   03-AUG-2022, entry version 23.
DE   RecName: Full=Cytochrome P450 CYP73A100;
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- INDUCTION: Up-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; JN604543; AEY75219.1; -; mRNA.
DR   AlphaFoldDB; H2DH22; -.
DR   SMR; H2DH22; -.
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..533
FT                   /note="Cytochrome P450 CYP73A100"
FT                   /id="PRO_0000425877"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         474
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   533 AA;  60571 MW;  47BBA2C7D69323FC CRC64;
     MAKILANSII FTIALFSLAK LLCSPYSINF TPSQLVLPIA IIGILPFILI LLSSISKSNL
     PPGPLSLPIF GNWLQVGNDL NHRLLAAMSK TYGPVFLLKL GSKNLAVVSD PELANQVLHT
     QGVEFGSRPR NVVFDIFTGN GQDMVFTIYG EHWRKMRRIM TLPFFTNKVV HQYSNMWEEE
     MDLVVHDLRN GKAAAREEGI VIRKRLQLML YNIMYRMMFD AKFESQDDPL FIEATRFNSE
     RSRLAQSFDY NYGDFIPLLR PFLRGYLNKC RDLQNRRLAF FNNYYVEKRR KIMAANGEKH
     KIICAMDHII DAQMMGEISD ENVLYIVENI NVAAIETTLW SMEWAIAELV NHPTVQRKIR
     DEISTVLKGS PVTEANLHEL PYLQATVKET LRLHTPIPLL VPHMNLEEAK LAGYTIPKES
     KVVVNAWWLA NNPAWWKNPE EFRPERFTEE EGGAAGRVQV DFRYLPFGVG RRSCPGMILA
     LPILGLVIAK LVMNFEMTVA AAGLGKIDVS EEGGQFSLHI AKHSTVVFNA IME