ID   C7D31_PANGI             Reviewed;         460 AA.
AC   H2DH19;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=Cytochrome P450 CYP71D312;
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   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; JN604540; AEY75216.1; -; mRNA.
DR   AlphaFoldDB; H2DH19; -.
DR   SMR; H2DH19; -.
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..460
FT                   /note="Cytochrome P450 CYP71D312"
FT                   /id="PRO_0000425872"
FT   BINDING         398
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   460 AA;  51812 MW;  11BD932519DC9551 CRC64;
     MLHLAGTLQI THGLRDLALK HGPLMHLQLG EISAVVVSSA RVAKEVLKTH DIAFADRPKL
     VSTKILLRNE KDLVMSIYGD YWRQMRKLCT VELLNTNKVS FFRSIREEEV WRLVQSIQSS
     LESPINLSKR FSAFTNAVTC IATIGKRSQL QDELVQVIED IASLAGGFDV SDLFPSIKLL
     HVLSGMRPKL QTIRKKLDNI FDNIILEHKE NRNRTNKGYG LTGEEDLVDV LLSVQERGGF
     EFPVTTDDIY GLILNMLIGG TDTSATALEW TMSELIRNPR VLEKVQAEVR QALKGKTTIH
     ENDIQGLSYL KLVIKETLRL HPPLALLLPR LCRDERQIDG YQIPIDTKLI INAWAIGRDP
     GYWVDAESFE PERFDNISAD FNGVNLNYIP FGSGRRMCPG ISFGVATVEL PLALLLYHFN
     WKLPFGMKPE SLDMSETFGA TLKRKNNLCL IATSCIPSNN