ID   C7D13_PANGI             Reviewed;         505 AA.
AC   H2DH20;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   03-AUG-2022, entry version 21.
DE   RecName: Full=Cytochrome P450 CYP71D313;
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}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; JN604541; AEY75217.1; -; mRNA.
DR   AlphaFoldDB; H2DH20; -.
DR   SMR; H2DH20; -.
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..505
FT                   /note="Cytochrome P450 CYP71D313"
FT                   /id="PRO_0000425874"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        442..462
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         441
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   505 AA;  56756 MW;  D628F1BCCB95CB5C CRC64;
     MELQFPLFSI FFVTILFFFL FKKSSKTTKN LPPGPRKLPI IGNILELAGE VQHRVLAELS
     QKHGPIMHLQ LAEISAIVVS SSKVAKEVLK THDLAFSDRA QLQLSKIILK GCKDVVFNDY
     DDYWRQMRKI CTVELLTANK VNSFRAIRED EAWNLVESIK TSLDSPVNLT HKFTSLTNAI
     TCRAAIGERS KYQDELVHLI ELMAALGGGF DIADLFPSYK FLHFLSGLRS KLEKVRKRLD
     DIFYNILKEH EEKRAKTKNS DGRVAGEEDL VDVLLRVQEK GGLQFPISSN NIQGIICDML
     TAGTDTASTA LDWAMSELVR YPSVLHKAQA EVREAFKGKT KIHEDDVQGL SYLKLVIKET
     LRLHPPAPLL LPKECREQCV IEGYTIPVRT KLIVNAWAIG RDPEYWVNAE SFDPERFSNK
     SIDYNGTNLN YIPFGAGRRS CPGIAFGIAT IELPLALLLY HFNWGMPGGI KPSALDMNEV
     LGATLKRKTN LLLSATSYTP NEDSS