UGT11_PANGI
ID UGT11_PANGI Reviewed; 475 AA.
AC A0A0K0PVM5;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 11-NOV-2015, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=UDP-glycosyltransferase 101 {ECO:0000303|PubMed:26032089};
DE Short=UGTPg101 {ECO:0000303|PubMed:26032089, ECO:0000303|PubMed:29509695};
DE EC=2.4.1.363 {ECO:0000269|PubMed:26032089};
DE EC=2.4.1.366 {ECO:0000269|PubMed:26032089};
GN Name=UGT101 {ECO:0000303|PubMed:26032089};
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, AND CATALYTIC ACTIVITY.
RX PubMed=26032089; DOI=10.1016/j.molp.2015.05.010;
RA Wei W., Wang P., Wei Y., Liu Q., Yang C., Zhao G., Yue J., Yan X., Zhou Z.;
RT "Characterization of Panax ginseng UDP-glycosyltransferases catalyzing
RT protopanaxatriol and biosyntheses of bioactive ginsenosides F1 and Rh1 in
RT metabolically engineered yeasts.";
RL Mol. Plant 8:1412-1424(2015).
RN [2]
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).
CC -!- FUNCTION: Component of the dammarane-type triterpene saponins (e.g.
CC ginsenosides or panaxosides) biosynthetic pathway (PubMed:26032089).
CC Glycosyltransferase that catalyzes the biosynthesis of ginsenoside F1
CC from protopanaxatriol (PPT) and the conversion of ginsenoside F1 to
CC ginsenoside Rg1 (PubMed:26032089). Triggers C20-OH glycosylation of
CC ginsenoside Rg3 to produce ginsenoside Rd (PubMed:26032089). Mediates
CC the conversion of protopanaxadiol (PPD) to the ginsenoside compound K
CC (PubMed:26032089). {ECO:0000269|PubMed:26032089}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(20S)-protopanaxadiol + UDP-alpha-D-glucose = (20S)-
CC ginsenoside C-K + H(+) + UDP; Xref=Rhea:RHEA:57976,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:75950, ChEBI:CHEBI:77146; EC=2.4.1.363;
CC Evidence={ECO:0000269|PubMed:26032089};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57977;
CC Evidence={ECO:0000269|PubMed:26032089};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(20S)-ginsenoside Rg3 + UDP-alpha-D-glucose = (20S)-
CC ginsenoside Rd + H(+) + UDP; Xref=Rhea:RHEA:57984, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:67988,
CC ChEBI:CHEBI:67991; EC=2.4.1.363;
CC Evidence={ECO:0000269|PubMed:26032089};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57985;
CC Evidence={ECO:0000269|PubMed:26032089};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(20S)-protopanaxatriol + UDP-alpha-D-glucose = (20S)-
CC ginsenoside F1 + H(+) + UDP; Xref=Rhea:RHEA:57980, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:75951,
CC ChEBI:CHEBI:77150; EC=2.4.1.363;
CC Evidence={ECO:0000269|PubMed:26032089};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57981;
CC Evidence={ECO:0000269|PubMed:26032089};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(20S)-ginsenoside F1 + UDP-alpha-D-glucose = (20S)-ginsenoside
CC Rg1 + H(+) + UDP; Xref=Rhea:RHEA:58008, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:67987,
CC ChEBI:CHEBI:77150; EC=2.4.1.366;
CC Evidence={ECO:0000269|PubMed:26032089};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58009;
CC Evidence={ECO:0000269|PubMed:26032089};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; KP795114; AKQ76389.1; -; mRNA.
DR AlphaFoldDB; A0A0K0PVM5; -.
DR SMR; A0A0K0PVM5; -.
DR KEGG; ag:AKQ76389; -.
DR BioCyc; MetaCyc:MON-20536; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03784; GT1_Gtf-like; 1.
DR InterPro; IPR002213; UDP_glucos_trans.
DR InterPro; IPR035595; UDP_glycos_trans_CS.
DR Pfam; PF00201; UDPGT; 1.
DR PROSITE; PS00375; UDPGT; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Isoprene biosynthesis; Transferase.
FT CHAIN 1..475
FT /note="UDP-glycosyltransferase 101"
FT /id="PRO_0000446965"
FT BINDING 278
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q9M156"
FT BINDING 344..345
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q9M156"
FT BINDING 362..370
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q9M156"
FT BINDING 384..387
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q9M156"
SQ SEQUENCE 475 AA; 53443 MW; D18C9D7F29887735 CRC64;
MKSELIFLPA PAIGHLVGMV EMAKLFISRH ENLSVTVLIA KFYMDTGVDN YNKSLLTNPT
PRLTIVNLPE TDPQNYMLKP RHAIFPSVIE TQKTHVRDII SGMTQSESTR VVGLLADLLF
INIMDIANEF NVPTYVYSPA GAGHLGLAFH LQTLNDKKQD VTEFRNSDTE LLVPSFANPV
PAEVLPSMYV DKEGGYDYLF SLFRRCRESK AIIINTFEEL EPYAINSLRM DSMIPPIYPV
GPILNLNGDG QNSDEAAVIL GWLDDQPPSS VVFLCFGSYG TFQENQVKEI AMGLERSGHR
FLWSLRPSIP KGETKLQLKY SNLEEILPVG FLDRTSCVGK VIGWAPQVAV LGHEAVGGFL
SHCGWNSTLE SVWCGVPVAT WPMYGEQQLN AFEMVKELGI AVEIEVDYKN EYFNMNNDFI
VRAEEIETKI KKLMMDEKNS EIRKKVKEMK EKSRLAMSEN GSSYNSLAKL FEEIM
