UGT10_PANGI
ID UGT10_PANGI Reviewed; 472 AA.
AC A0A0K0PVW1;
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 100 {ECO:0000303|PubMed:26032089};
DE Short=UGTPg100 {ECO:0000303|PubMed:26032089, ECO:0000303|PubMed:29509695};
DE EC=2.4.1.367 {ECO:0000269|PubMed:26032089};
GN Name=UGT100 {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, CATALYTIC ACTIVITY, AND MUTAGENESIS
RP OF CYS-82; ALA-142; PHE-144; LEU-186; TRP-205 AND GLY-338.
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 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 [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).
CC -!- FUNCTION: Component of the dammarane-type triterpene saponins (e.g.
CC PPT-type ginsenosides or panaxosides) biosynthetic pathway
CC (PubMed:26032089, PubMed:27746309, PubMed:29378087).
CC Glycosyltransferase that catalyzes the biosynthesis of ginsenoside Rh1
CC from protopanaxatriol (PPT) and the conversion of ginsenoside F1 to
CC ginsenoside Rg1 (PubMed:26032089, PubMed:27746309).
CC {ECO:0000269|PubMed:26032089, ECO:0000269|PubMed:27746309,
CC ECO:0000303|PubMed:29378087}.
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;
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)-protopanaxatriol + UDP-alpha-D-glucose = (20S)-
CC ginsenoside Rh1 + H(+) + UDP; Xref=Rhea:RHEA:58952,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:75951, ChEBI:CHEBI:142487; EC=2.4.1.367;
CC Evidence={ECO:0000269|PubMed:26032089};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58953;
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=2.4.1.367;
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 -!- INDUCTION: Induced by A.niger mycelium-derived elicitor, thus improving
CC ginsenosides production in adventitious roots culture.
CC {ECO:0000269|PubMed:27746309}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; KP795113; AKQ76388.1; -; mRNA.
DR AlphaFoldDB; A0A0K0PVW1; -.
DR SMR; A0A0K0PVW1; -.
DR KEGG; ag:AKQ76388; -.
DR BioCyc; MetaCyc:MON-20535; -.
DR BRENDA; 2.4.1.367; 7895.
DR UniPathway; UPA00213; -.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
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 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; Hydrolase; Isoprene biosynthesis; Transferase.
FT CHAIN 1..472
FT /note="UDP-glycosyltransferase 100"
FT /id="PRO_0000446966"
FT BINDING 279
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q9M156"
FT BINDING 343..344
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q9M156"
FT BINDING 361..369
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q9M156"
FT BINDING 383..386
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q9M156"
FT SITE 142
FT /note="Essential for the glycosylation activity toward the
FT C6-OH of protopanaxatriol (PPT)"
FT /evidence="ECO:0000269|PubMed:26032089"
FT SITE 186
FT /note="Essential for the glycosylation activity toward the
FT C6-OH of protopanaxatriol (PPT)"
FT /evidence="ECO:0000269|PubMed:26032089"
FT SITE 338
FT /note="Essential for the glycosylation activity toward the
FT C6-OH of protopanaxatriol (PPT)"
FT /evidence="ECO:0000269|PubMed:26032089"
FT MUTAGEN 82
FT /note="C->H: Loss of glycosylase activity toward
FT protopanaxatriol (PPT)."
FT /evidence="ECO:0000269|PubMed:26032089"
FT MUTAGEN 142
FT /note="A->T: Loss of glycosylase activity toward
FT protopanaxatriol (PPT)."
FT /evidence="ECO:0000269|PubMed:26032089"
FT MUTAGEN 144
FT /note="F->Y,H: Loss of glycosylase activity toward
FT protopanaxatriol (PPT)."
FT /evidence="ECO:0000269|PubMed:26032089"
FT MUTAGEN 186
FT /note="L->S: Loss of glycosylase activity toward
FT protopanaxatriol (PPT)."
FT /evidence="ECO:0000269|PubMed:26032089"
FT MUTAGEN 205
FT /note="W->R: Normal ability to transfer a glucose residue
FT to the C6-OH of protopanaxatriol (PPT)."
FT /evidence="ECO:0000269|PubMed:26032089"
FT MUTAGEN 338
FT /note="G->R: Loss of glycosylase activity toward
FT protopanaxatriol (PPT)."
FT /evidence="ECO:0000269|PubMed:26032089"
SQ SEQUENCE 472 AA; 53131 MW; FCE00FBCBC06A7A5 CRC64;
MKSELIFLPV PAFGHLVGMV EMAKLFISRH ENLSVTVLIS KFFIDTGIDN YNKSLLAKPT
PRLTIINLPE IDPQKYLLKP RCAIFPSLIE NQKTHVRDVM SRMTQSESTR VVGLLADILF
VDIFDIADEF NVPTYVYSPA GAGFLGLAFH LQTLNDDKKQ DVTEFRNSDT ELLVPSFANP
VPAEFLPSIF LEKDGRHDVL LSLYWRCREA KGIIVNTFEE LEPYAINSLR MDSMIPPIYP
VGPILNLNGE GQNSDEAAVI LGWLDDQPPS SVVFLCFGSF GSFPENQVKE IAMGLERSGH
RFLWSLRPCI SEGETTLQLK YSNLELPAGF LDRTSCVGKV IGWAPQMAIL AHEAVGGFVS
HCGWNSVLES VWYGMPVATW PMYGEQQLNA FEMVKELGLA VEIEVDYRNE YNKSDFIVKA
DEIETKIKKL MMDGKNSKIR KKVKEMKEKS RVAMSENGSS YTSLAKLFEE IM
