C7A53_PANGI
ID C7A53_PANGI Reviewed; 469 AA.
AC I7CT85;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Protopanaxadiol 6-hydroxylase {ECO:0000303|PubMed:22875608};
DE Short=P6H {ECO:0000303|PubMed:22875608};
DE EC=1.14.14.121 {ECO:0000269|PubMed:22875608};
DE AltName: Full=Cytochrome P450 CYP716A53v2 {ECO:0000303|PubMed:22875608};
DE AltName: Full=Protopanaxatriol synthase {ECO:0000303|PubMed:22875608};
DE Short=PgPPTS {ECO:0000303|PubMed:22875608};
GN Name=CYP716A53v2 {ECO:0000303|PubMed:22875608,
GN ECO:0000303|PubMed:30577538};
GN Synonyms=PPTS {ECO:0000303|PubMed:22875608, ECO:0000303|PubMed:30577538};
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], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND LACK OF INDUCTION BY MEJA.
RX PubMed=22875608; DOI=10.1093/pcp/pcs106;
RA Han J.Y., Hwang H.S., Choi S.W., Kim H.J., Choi Y.E.;
RT "Cytochrome P450 CYP716A53v2 catalyzes the formation of protopanaxatriol
RT from protopanaxadiol during ginsenoside biosynthesis in Panax ginseng.";
RL Plant Cell Physiol. 53:1535-1545(2012).
RN [2]
RP IDENTIFICATION.
RX PubMed=18351680; DOI=10.1002/bit.21829;
RA Yue C.J., Zhou X., Zhong J.J.;
RT "Protopanaxadiol 6-hydroxylase and its role in regulating the ginsenoside
RT heterogeneity in Panax notoginseng cells.";
RL Biotechnol. Bioeng. 100:933-940(2008).
RN [3]
RP ACTIVITY REGULATION.
RX PubMed=23467002; DOI=10.1016/j.jbiotec.2013.02.012;
RA Huang C., Qian Z.-G., Zhong J.-J.;
RT "Enhancement of ginsenoside biosynthesis in cell cultures of Panax ginseng
RT by N,N'-dicyclohexylcarbodiimide elicitation.";
RL J. Biotechnol. 165:30-36(2013).
RN [4]
RP INDUCTION BY TWEEN 80.
RX PubMed=24889095; DOI=10.1002/bab.1256;
RA Liang Y., Wu J., Li Y., Li J., Ouyang Y., He Z., Zhao S.;
RT "Enhancement of ginsenoside biosynthesis and secretion by Tween 80 in Panax
RT ginseng hairy roots.";
RL Biotechnol. Appl. Biochem. 62:193-199(2015).
RN [5]
RP FUNCTION, AND INDUCTION BY ASPERGILLUS NIGER.
RX PubMed=27746309; DOI=10.1016/j.jbiotec.2016.10.011;
RA Li J., Liu S., Wang J., Li J., Liu D., Li J., Gao W.;
RT "Fungal elicitors enhance ginsenosides biosynthesis, expression of
RT functional genes as well as signal molecules accumulation in adventitious
RT roots of Panax ginseng C. A. Mey.";
RL J. Biotechnol. 239:106-114(2016).
RN [6]
RP REVIEW.
RX PubMed=29378087; DOI=10.1002/bab.1649;
RA Lu J., Li J., Wang S., Yao L., Liang W., Wang J., Gao W.;
RT "Advances in ginsenoside biosynthesis and metabolic regulation.";
RL Biotechnol. Appl. Biochem. 65:514-522(2018).
RN [7]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=29509695; DOI=10.3390/molecules23030589;
RA Yang J.-L., Hu Z.-F., Zhang T.-T., Gu A.-D., Gong T., Zhu P.;
RT "Progress on the studies of the key enzymes of ginsenoside biosynthesis.";
RL Molecules 23:0-0(2018).
RN [8]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION BY ABIOTIC FACTORS.
RX PubMed=30577538; DOI=10.3390/molecules24010014;
RA Zhang T., Han M., Yang L., Han Z., Cheng L., Sun Z., Yang L.;
RT "The effects of environmental factors on ginsenoside biosynthetic enzyme
RT gene expression and saponin abundance.";
RL Molecules 24:0-0(2018).
CC -!- FUNCTION: Component of the dammarane-type triterpene saponins (e.g.
CC PPT-type ginsenosides or panaxosides) biosynthetic pathway
CC (PubMed:27746309, PubMed:29378087). Catalyzes the formation of
CC protopanaxatriol from protopanaxadiol during ginsenoside biosynthesis,
CC a class of tetracyclic triterpenoid saponins.
CC {ECO:0000269|PubMed:22875608, ECO:0000269|PubMed:27746309,
CC ECO:0000303|PubMed:29378087}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(20S)-protopanaxadiol + O2 + reduced [NADPH--hemoprotein
CC reductase] = (20S)-protopanaxatriol + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:22272, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:75950, ChEBI:CHEBI:75951; EC=1.14.14.121;
CC Evidence={ECO:0000269|PubMed:22875608};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q96242};
CC -!- ACTIVITY REGULATION: Activated by N,N'-dicyclohexylcarbodiimide (DCCD)
CC thus leading to increased ginsenosides accumulation.
CC {ECO:0000269|PubMed:23467002}.
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Accumulates ubiquitously in all organs of plants,
CC including roots, stems and leaves. {ECO:0000269|PubMed:22875608,
CC ECO:0000269|PubMed:30577538}.
CC -!- DEVELOPMENTAL STAGE: Accumulates strongly from the leaf opened to the
CC green fruit stage (PubMed:30577538). High levels are maintained until
CC the red fruit stage, but decrease drastically during the root growth
CC stage (PubMed:30577538). {ECO:0000269|PubMed:30577538}.
CC -!- INDUCTION: Expression is not affected by methyl jasmonate (MeJA)
CC treatment (PubMed:22875608). Induced by A.niger mycelium-derived
CC elicitor, thus improving ginsenosides production in adventitious roots
CC culture (PubMed:27746309). Slightly induced by Tween 80
CC (PubMed:24889095). Influenced in roots by relative humidity and
CC photosynthetically active radiation (PAR), and in leaves by temperature
CC and rain (PubMed:30577538). {ECO:0000269|PubMed:22875608,
CC ECO:0000269|PubMed:24889095, ECO:0000269|PubMed:27746309,
CC ECO:0000269|PubMed:30577538}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; JX036031; AFO63031.1; -; mRNA.
DR AlphaFoldDB; I7CT85; -.
DR SMR; I7CT85; -.
DR KEGG; ag:AFO63031; -.
DR BioCyc; MetaCyc:MON-18262; -.
DR BRENDA; 1.14.13.184; 7895.
DR BRENDA; 1.14.14.121; 7895.
DR UniPathway; UPA00213; -.
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:0102557; F:protopanaxadiol 6-hydroxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0002238; P:response to molecule of fungal origin; IEP:UniProtKB.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
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 1: Evidence at protein level;
KW Heme; Iron; Isoprene biosynthesis; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN 1..469
FT /note="Protopanaxadiol 6-hydroxylase"
FT /id="PRO_0000425880"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 416
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|UniProtKB:Q96242"
SQ SEQUENCE 469 AA; 53297 MW; ECA30E88DF990759 CRC64;
MDLFISSQLL LLLVFCLFLF WNFKPSSQNK LPPGKTGWPI IGETLEFISC GQKGNPEKFV
TQRMNKYSPD VFTTSLAGEK MVVFCGASGN KFIFSNENKL VVSWWPPAIS KILTATIPSV
EKSKALRSLI VEFLKPEALH KFISVMDRTT RQHFEDKWNG STEVKAFAMS ESLTFELACW
LLFSINDPVQ VQKLSHLFEK VKAGLLSLPL NFPGTAFNRG IKAANLIRKE LSVVIKQRRS
DKLQTRKDLL SHVMLSNGEG EKFFSEMDIA DVVLNLLIAS HDTTSSAMGS VVYFLADHPH
IYAKVLTEQM EIAKSKGAEE LLSWEDIKRM KYSRNVINEA MRLVPPSQGG FKVVTSKFSY
ANFIIPKGWK IFWSVYSTHK DPKYFKNPEE FDPSRFEGDG PMPFTFIPFG GGPRMCPGSE
FARLEVLIFM HHLVTNFKWE KVFPNEKIIY TPFPFPENGL PIRLSPCTL
