ID   C7A22_PANGI             Reviewed;         524 AA.
AC   H2DH17;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   03-AUG-2022, entry version 26.
DE   RecName: Full=Cytochrome P450 CYP749A22;
DE            EC=1.14.-.-;
DE   AltName: Full=Cytochrome P450 CYP749A20;
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}; Single-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}.
CC   -!- CAUTION: Reported as CYP749A22 in the publication but submitted as
CC       CYP749A20. {ECO:0000305|PubMed:22039120}.
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DR   EMBL; JN604538; AEY75214.1; -; mRNA.
DR   AlphaFoldDB; H2DH17; -.
DR   SMR; H2DH17; -.
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..524
FT                   /note="Cytochrome P450 CYP749A22"
FT                   /id="PRO_0000425873"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         472
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   524 AA;  60118 MW;  047718CB3C719CF8 CRC64;
     MSWNNIGVVE MTPILFQFLL SSLCVFLLFV FIRFLNDIWW TPIRLQRVFR QQGIRGPSYG
     FLYGNTKEIL NMRKESMSRP MDYLSHNIFP RLQPHLYSWL NIYGKNFLNW YGPRAQFVVT
     QVDFVKETMI KDQAYPKMDP EWFAKKLLGD GIVTSKGKKW AKHRRLANHA FHAESLKSMT
     PAMIASVEMM LKRWKQHEGR EIDVFQEFKI LTSEVISRTA FGSSYLDGKD IFDRLTQLGI
     IITRNSYKVK LPGISLFYKS NDEIEAEKLD QGLYDSILRI MEKREKESTM SGEVGSFGTD
     FLGLLMKAMN DADEKNRITA QDVVDECKTF YVAGQETTTT LLAWVIFLLG IHTDWQEKAR
     QEVLNLFGQE IPNSDGLAKL KTVNMIINET LRLYPPVIFL TRKVKEETKF GKLTLPANVH
     IVVPTLALHH DEQIWGDDAL LFKPERFSQG VAKATNNNAA AFFPFGLGPR SCVGLNFATN
     EAKIALAMIL QCYSFALSPT YIHSPVQILT VRPQHGLQVM LQPL