ID   UGT45_PANGI             Reviewed;         457 AA.
AC   A0A0D5ZDC8;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2015, sequence version 1.
DT   03-AUG-2022, entry version 15.
DE   RecName: Full=UDP-glucosyltransferase 45 {ECO:0000303|PubMed:25769286};
DE            Short=UGTPg45 {ECO:0000303|PubMed:25769286, ECO:0000303|PubMed:29509695};
DE            EC=2.4.1.- {ECO:0000269|PubMed:25769286};
GN   Name=UGT45 {ECO:0000303|PubMed:25769286};
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
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=25769286; DOI=10.1016/j.ymben.2015.03.003;
RA   Wang P., Wei Y., Fan Y., Liu Q., Wei W., Yang C., Zhang L., Zhao G.,
RA   Yue J., Yan X., Zhou Z.;
RT   "Production of bioactive ginsenosides Rh2 and Rg3 by metabolically
RT   engineered yeasts.";
RL   Metab. Eng. 29:97-105(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 triterpene saponins (e.g. PPD-type
CC       ginsenosides) biosynthetic pathway (PubMed:25769286).
CC       Glycosyltransferase that catalyzes the biosynthesis of ginsenoside Rh2
CC       from protopanaxadiol (PPD) (PubMed:25769286).
CC       {ECO:0000269|PubMed:25769286}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(20S)-protopanaxadiol + UDP-alpha-D-glucose = (20S)-
CC         ginsenoside Rh2 + H(+) + UDP; Xref=Rhea:RHEA:57996,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC         ChEBI:CHEBI:75950, ChEBI:CHEBI:77147;
CC         Evidence={ECO:0000269|PubMed:25769286};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57997;
CC         Evidence={ECO:0000269|PubMed:25769286};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=209 uM for protopanaxadiol (at pH 8 and 40 degrees Celsius)
CC         {ECO:0000269|PubMed:25769286};
CC         Vmax=80 nmol/min/mg enzyme with protopanaxadiol as substrate (at pH 8
CC         and 40 degrees Celsius) {ECO:0000269|PubMed:25769286};
CC         Note=kcat is 0.384 sec(-1) with protopanaxadiol as substrate (at pH 8
CC         and 40 degrees Celsius). {ECO:0000269|PubMed:25769286};
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; KM401918; AKA44586.1; -; mRNA.
DR   AlphaFoldDB; A0A0D5ZDC8; -.
DR   SMR; A0A0D5ZDC8; -.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0016135; P:saponin biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0046246; P:terpene biosynthetic process; IDA: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   Pfam; PF00201; UDPGT; 1.
PE   1: Evidence at protein level;
KW   Isoprene biosynthesis; Transferase.
FT   CHAIN           1..457
FT                   /note="UDP-glucosyltransferase 45"
FT                   /id="PRO_0000446963"
FT   BINDING         278
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         333..334
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         351..359
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         373..376
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
SQ   SEQUENCE   457 AA;  51153 MW;  848FB428D705BE1C CRC64;
     MEREMLSKTH IMFIPFPAQG HMSPMMQFAK RLAWKGLRIT IVLPAQIRDF MQITNPLINT
     ECISFDFDKD DGMPYSMQAY MGVVKLKVTN KLSDLLEKQR TNGYPVNLLV VDSLYPSRVE
     MCHQLGVKGA PFFTHSCAVG AIYYNARLGK LKIPPEEGLT SVSLPSIPLL GRDDLPIIRT
     GTFPDLFEHL GNQFSDLDKA DWIFFNTFDK LENEEAKWLS SQWPITSIGP LIPSMYLDKQ
     LPNDKDNGIN FYKADVGSCI KWLDAKDPGS VVYASFGSVK HNLGDDYMDE VAWGLLHSKY
     HFIWVVIESE RTKLSSDFLA EAEAEEKGLI VSWCPQLQVL SHKSIGSFMT HCGWNSTVEA
     LSLGVPMVAL PQQFDQPANA KYIVDVWQIG VRVPIGEEGV VLRGEVANCI KDVMEGEIGD
     ELRGNALKWK GLAVEAMEKG GSSDKNIDEF ISKLVSS