ID   C7A12_PANGI             Reviewed;         500 AA.
AC   H2DH18;
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 CYP736A12;
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].
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}.
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DR   EMBL; JN604539; AEY75215.1; -; mRNA.
DR   AlphaFoldDB; H2DH18; -.
DR   SMR; H2DH18; -.
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..500
FT                   /note="Cytochrome P450 CYP736A12"
FT                   /id="PRO_0000425879"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         442
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   500 AA;  56042 MW;  B5A8AC9A6002378B CRC64;
     MFPLAYPLLF VLLGALSWWI LPIISPLKRH HKLPPGPRGL PIIGSLHTLG ALPHRTLQTL
     AKKYGPIMSM RLGSVPTIVV SSPQAAELFL KTHDNIFASR PKLQAAEYMS YGTMGMSFTA
     YGPHWRNIRK FVVLELLTPA KINSFVGMRR EELGTVVKSI KEASAANEVV DLSAKVANII
     ENMTYRLLLG RTKDDRYDLK GIMNEALTLA GRFNIADFVP FLGPLDIQGL TRQFKDTGKR
     LDKILEFIID EHEQNSSNGN ASGDFIDDML SLKNKPSNTH DELSKVIDRS VIKAIMIDII
     SAAIDTSDTS IEWILTELIK HPRAMKKCQE EIDAVVGVDR MVEETDLPNL EYVYMVVKEG
     LRLHPVAPLL GPHESMEDIT INGYFIPKQS RVIVNSWALG RDPNVWSENA EEFLPERFEG
     SNVDVRGRDF QLLPFGSGRR GCPGMQLGLI TVQLVVARLV HCFDWNLPNG TTPDNLDMTE
     KFGLTTPRVK HLLAVPKYRL