UGT13_PANGI
ID UGT13_PANGI Reviewed; 472 AA.
AC A0A0K0PVL3;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 11-NOV-2015, sequence version 1.
DT 03-AUG-2022, entry version 25.
DE RecName: Full=UDP-glucosyltransferase 103 {ECO:0000303|PubMed:26032089};
DE Short=UGTPg103 {ECO:0000303|PubMed:26032089};
DE EC=2.4.1.366 {ECO:0000305|PubMed:26032089};
GN Name=UGT103 {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 MUTAGENESIS OF THR-142; SER-186
RP AND ARG-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).
CC -!- FUNCTION: Probable component of the triterpene saponins (e.g.
CC ginsenosides) biosynthetic pathway (PubMed:26032089). No detectable
CC activity toward protopanaxatriol (PPT) (PubMed:26032089).
CC {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:0000305|PubMed:26032089};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58009;
CC Evidence={ECO:0000305|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; KP795116; AKQ76391.1; -; mRNA.
DR AlphaFoldDB; A0A0K0PVL3; -.
DR SMR; A0A0K0PVL3; -.
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..472
FT /note="UDP-glucosyltransferase 103"
FT /id="PRO_0000446968"
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 MUTAGEN 142
FT /note="T->A: Gained ability to transfer a glucose residue
FT to the C6-OH of protopanaxatriol (PPT); when associated
FT with L-186 and G-338."
FT /evidence="ECO:0000269|PubMed:26032089"
FT MUTAGEN 186
FT /note="S->L: Gained ability to transfer a glucose residue
FT to the C6-OH of protopanaxatriol (PPT); when associated
FT with T-142 and G-338."
FT /evidence="ECO:0000269|PubMed:26032089"
FT MUTAGEN 338
FT /note="R->G: Gained ability to transfer a glucose residue
FT to the C6-OH of protopanaxatriol (PPT); when associated
FT with T-142 and L-186."
FT /evidence="ECO:0000269|PubMed:26032089"
SQ SEQUENCE 472 AA; 53204 MW; C80409971D6C54D3 CRC64;
MKSELIFLPV PAFGHLVGMV EMAKLFISRH ENLSVTVLIS KFFIDTGIDN YNKSLLAKPT
PRLTIINLPE IDPQKYLLKP RCAIFPSLIE NQKTHVRDVM SRMTQSESTR IVGLLADILF
VDIFDIADEF NVPTYVYSPA GTGFLGLAFH LQTLNDDKKQ DVTEFRNSDT ELLVPSFANP
VPAEFSPSIF LEKDGRHDVL LSLYRRCREA KGIIVNTFEE LEPYAINSLR MDSMIPPIYP
VGPILNLNGE GQNSDEAAVI LGWLDDQPPS SVVFLCFGSF GSFPENQVKE IAMGLERSGH
RFLWSLRPCI SEGETTLQLK YSNLELPAGF LDRTSCVRKV IGWAPQMAVL AHEAVGGFVS
HCGWNSVLES VWYGMPVATW PMYGEQQLNA FEMVKELGLA VEIEVDYRNE YNKSDFIVKA
DEIETKIKKL MMDGKNSKIR KKVKEMKEKS RVAMSENGSS YTSLAKLFEE IM