ID   C7A52_PANGI             Reviewed;         481 AA.
AC   I7C6E8;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Beta-amyrin 28-monooxygenase {ECO:0000305};
DE            EC=1.14.14.126 {ECO:0000269|PubMed:24092881};
DE   AltName: Full=Beta-amyrin 28-oxidase {ECO:0000303|PubMed:24092881};
DE   AltName: Full=Cytochrome P450 CYP716A52v2 {ECO:0000303|PubMed:22875608};
DE   AltName: Full=Oleanic acid synthase {ECO:0000303|PubMed:29509695};
DE            Short=PgOAS {ECO:0000305};
GN   Name=CYP716A52v2 {ECO:0000303|PubMed:22875608,
GN   ECO:0000303|PubMed:30577538};
GN   Synonyms=OAS {ECO:0000303|PubMed:29509695, 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], TISSUE SPECIFICITY, CATALYTIC ACTIVITY, AND
RP   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   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=24092881; DOI=10.1093/pcp/pct141;
RA   Han J.Y., Kim M.J., Ban Y.W., Hwang H.S., Choi Y.E.;
RT   "The involvement of beta-amyrin 28-oxidase (CYP716A52v2) in oleanane-type
RT   ginsenoside biosynthesis in Panax ginseng.";
RL   Plant Cell Physiol. 54:2034-2046(2013).
RN   [3]
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   [4]
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   [5]
RP   DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, 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 oleanane-type triterpene saponins (e.g.
CC       ginsenosides or panaxosides) biosynthetic pathway (PubMed:29378087).
CC       Catalyzes the carboxylation of beta-amyrin at the C-28 position to form
CC       oleanolic acid during ginsenoside biosynthesis, a class of tetracyclic
CC       triterpenoid saponins. {ECO:0000269|PubMed:24092881,
CC       ECO:0000303|PubMed:29378087}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-amyrin + 3 O2 + 3 reduced [NADPH--hemoprotein reductase]
CC         = 4 H(+) + 4 H2O + oleanolate + 3 oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:43068, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:10352, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:82828; EC=1.14.14.126;
CC         Evidence={ECO:0000269|PubMed:24092881};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:Q96242};
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: Mostly expressed in roots, and, to a lower extent,
CC       in stems and leaves (PubMed:30577538). Accumulates only in the rhizome
CC       of plants (PubMed:22875608). {ECO:0000269|PubMed:22875608,
CC       ECO:0000269|PubMed:30577538}.
CC   -!- DEVELOPMENTAL STAGE: Progressive increase in roots from the leaf opened
CC       stage to the green fruit, red fruit and root growth stages,
CC       respectively. {ECO:0000269|PubMed:30577538}.
CC   -!- INDUCTION: Expression is not affected by methyl jasmonate (MeJA)
CC       treatment (PubMed:22875608). Influenced in roots and leaves by relative
CC       humidity and soil water potential (PubMed:30577538).
CC       {ECO:0000269|PubMed:22875608, ECO:0000269|PubMed:30577538}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; JX036032; AFO63032.1; -; mRNA.
DR   AlphaFoldDB; I7C6E8; -.
DR   SMR; I7C6E8; -.
DR   PRIDE; I7C6E8; -.
DR   KEGG; ag:AFO63032; -.
DR   BioCyc; MetaCyc:MON-20537; -.
DR   BRENDA; 1.14.14.121; 7895.
DR   BRENDA; 1.14.14.126; 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:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IDA:UniProtKB.
DR   GO; GO:0102374; F:ursolic aldehyde 28-monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102373; F:uvaol dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019742; P:pentacyclic triterpenoid metabolic process; IDA: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..481
FT                   /note="Beta-amyrin 28-monooxygenase"
FT                   /id="PRO_0000425881"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         428
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   481 AA;  53955 MW;  728979F41FD9244F CRC64;
     MELFYVPLLS LFVLFISLSF HFLFYKSKPS SSGGFPLPPG KTGWPIIGES YEFLSTGWKG
     YPEKFIFDRM TKYSSNVFKT SIFGEPAAVF CGAACNKFLF SNENKLVQAW WPDSVNKVFP
     SSTQTSSKEE AIKMRKMLPN FFKPEALQRY IGLMDQIAAN HFESGWENKN EVVVFPLAKS
     YTFWIACKVF VSVEEPAQVA ELLEPFSAIA SGIISVPIDL PGTPFNSAIK SSKIVRRKLV
     GIIKQRKIDL GEGKASATQD ILSHMLLTSD ESGKFMGEGD IADKILGLLI GGHDTASSAC
     TFVVKFLAEL PQIYEGVYQE QMEIVKSKKA GELLKWEDIQ KMKYSWNVAC EVLRLAPPLQ
     GAFREALSDF TYNGFSIPKG WKLYWSANST HINSEVFPEP LKFDPSRFDG AGPPPFSFVP
     FGGGPRMCPG KEYARLEILV FMHHLVKRFK WEKVIPDEKI VVNPMPIPAN GLPVRLFPHK
     A