U74AE_PANGI
ID U74AE_PANGI Reviewed; 451 AA.
AC A0A0A6ZFR4;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=UDP-glucosyltransferase 74AE2 {ECO:0000303|PubMed:25320211, ECO:0000303|PubMed:27746309};
DE Short=PgUGT74AE2 {ECO:0000303|PubMed:27746309, ECO:0000303|PubMed:29509695};
DE EC=2.4.1.364 {ECO:0000269|PubMed:25320211};
DE AltName: Full=UDP-glucosyltransferase 74A1 {ECO:0000303|PubMed:27746309};
DE Short=PgUGT74A1 {ECO:0000303|PubMed:25320211};
GN Name=UGT74AE2 {ECO:0000303|PubMed:25320211, ECO:0000303|PubMed:27746309};
GN Synonyms=UGT74A1 {ECO:0000303|PubMed:25320211};
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 [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION BY METHYL
RP JASMONATE.
RX PubMed=25320211; DOI=10.1093/pcp/pcu147;
RA Jung S.-C., Kim W., Park S.C., Jeong J., Park M.K., Lim S., Lee Y.,
RA Im W.-T., Lee J.H., Choi G., Kim S.C.;
RT "Two ginseng UDP-glycosyltransferases synthesize ginsenoside Rg3 and Rd.";
RL Plant Cell Physiol. 55:2177-2188(2014).
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 PPD-type ginsenosides or panaxosides) biosynthetic pathway
CC (PubMed:25320211, PubMed:27746309, PubMed:29378087).
CC Glycosyltransferase that catalyzes the biosynthesis of ginsenoside Rh2
CC from protopanaxadiol (PPD) and the conversion of compound K to
CC ginsenoside F2 (PubMed:25320211, PubMed:27746309).
CC {ECO:0000269|PubMed:25320211, ECO:0000269|PubMed:27746309,
CC ECO:0000303|PubMed:29378087}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(20S)-ginsenoside C-K + UDP-alpha-D-glucose = (20S)-
CC ginsenoside F2 + H(+) + UDP; Xref=Rhea:RHEA:57992, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:77145,
CC ChEBI:CHEBI:77146; EC=2.4.1.364;
CC Evidence={ECO:0000269|PubMed:25320211};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57993;
CC Evidence={ECO:0000269|PubMed:25320211};
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; EC=2.4.1.364;
CC Evidence={ECO:0000269|PubMed:25320211};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57997;
CC Evidence={ECO:0000269|PubMed:25320211};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=25 uM for protopanaxadiol (at pH 7 and 35 degrees Celsius)
CC {ECO:0000269|PubMed:25320211};
CC KM=40 uM for compound K (at pH 7 and 35 degrees Celsius)
CC {ECO:0000269|PubMed:25320211};
CC Note=kcat is 55.6 usec(-1) with protopanaxadiol as substrate (at pH 7
CC and 35 degrees Celsius). kcat is 134.7 usec(-1) with compound K as
CC substrate (at pH 7 and 35 degrees Celsius).
CC {ECO:0000269|PubMed:25320211};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed at higher levels in roots than in leaves.
CC {ECO:0000269|PubMed:25320211}.
CC -!- INDUCTION: Induced by methyl jasmonate (MeJA) in roots and leaves
CC (PubMed:25320211). Induced by A.niger mycelium-derived elicitor, thus
CC improving ginsenosides production in adventitious roots culture
CC (PubMed:27746309). {ECO:0000269|PubMed:25320211,
CC ECO:0000269|PubMed:27746309}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; JX898529; AGR44631.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A6ZFR4; -.
DR SMR; A0A0A6ZFR4; -.
DR KEGG; ag:AGR44631; -.
DR BioCyc; MetaCyc:MON-20533; -.
DR BRENDA; 2.4.1.364; 7895.
DR UniPathway; UPA00213; -.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0002238; P:response to molecule of fungal origin; IEP: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..451
FT /note="UDP-glucosyltransferase 74AE2"
FT /id="PRO_0000446961"
FT BINDING 274
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q9M156"
FT BINDING 327..328
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q9M156"
FT BINDING 345..353
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q9M156"
FT BINDING 367..370
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q9M156"
SQ SEQUENCE 451 AA; 50206 MW; 60E6A8BB7CE6A7AC CRC64;
MLSKTHIMFI PFPAQGHMSP MMQFAKRLAW KGVRITIVLP AQIRDSMQIT NSLINTECIS
FDFDKDDGMP YSMQAYMGVV KLKVTNKLSD LLEKQKTNGY PVNLLVVDSL YPSRVEMCHQ
LGVKGAPFFT HSCAVGAIYY NAHLGKLKIP PEEGLTSVSL PSIPLLGRDD LPIIRTGTFP
DLFEHLGNQF SDLDKADWIF FNTFDKLENE EAKWLSSQWP ITSIGPLIPS MYLDKQLPND
KGNGINLYKA DVGSCIKWLD AKDPGSVVYA SFGSVKHNFG DDYMDEVAWG LLHSKYNFIW
VVIEPERTKL SSDFLAEAEE KGLIVSWCPQ LEVLSHKSIG SFMTHCGWNS TVEALSLGVP
MVAVPQQFDQ PVNAKYIVDV WQIGVRVPIG EDGVVLRGEV ANCIKDVMEG EIGDELRGNA
LKWKGLAVEA MEKGGSSDKN IDEFISKLVS S
