ID   UGT12_PANGI             Reviewed;         475 AA.
AC   A0A0K0PVL0;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   11-NOV-2015, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=UDP-glucosyltransferase 102 {ECO:0000303|PubMed:26032089};
DE            Short=UGTPg102 {ECO:0000303|PubMed:26032089};
DE            EC=2.4.1.- {ECO:0000305};
GN   Name=UGT102;
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 TYR-144.
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   -!- 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; KP795115; AKQ76390.1; -; mRNA.
DR   AlphaFoldDB; A0A0K0PVL0; -.
DR   SMR; A0A0K0PVL0; -.
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-glucosyltransferase 102"
FT                   /id="PRO_0000446967"
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"
FT   MUTAGEN         144
FT                   /note="Y->H: Gained ability to transfer a glucose residue
FT                   to the C20-OH of protopanaxatriol (PPT)."
FT                   /evidence="ECO:0000269|PubMed:26032089"
SQ   SEQUENCE   475 AA;  53556 MW;  799CCC4BCE1EE7E5 CRC64;
     MKSELIFLPA PAIGHLVGMV EMAKLFISRH ENLSVTVFIS KFYMDTGVDN YNKSLLTNPT
     PRLTIVNLPE TDPQNYMLKP RHAILPSVIE TQKTHVRDII SGMTQSESTR VVGLLADLLF
     INIMDIANEF NVPIYVYSPA GAGYLGLAFH LQTLYDKKQD VTEFRNSDTE LLVPGFANPV
     PAEVLPSMYV DKEGGYDYLF SLFRRCRESK AIIINTFEEL EPYAINSLRM DSMIPPIYPV
     GPILNLNGDG QNSDEAAVIL GWLDDQPPSS VVFLCFGSYG TFQENQVKEI AMGLERSGHR
     FLWALRPSIP KGETKLQLKY SNLEEILPVG FLDRTSCVGK VIGWAPQVAV LGHEAVAGFM
     SHCGWNSTLE SVWFGVPVAT WPMYGEQHLN AFEMVKELGL AVEIEVDYKN EYFNTKNDFI
     VRAEEIETKI KKLMMDEKNS EIRKKVKEMK EKSRVAMSEN GSSYNSLAKL FEEIM