U74G1_STERE
ID U74G1_STERE Reviewed; 460 AA.
AC Q6VAA6;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=UDP-glycosyltransferase 74G1 {ECO:0000303|PubMed:15610349};
DE EC=2.4.1.- {ECO:0000269|PubMed:15610349};
GN Name=UGT74G1 {ECO:0000303|PubMed:15610349};
OS Stevia rebaudiana (Stevia) (Eupatorium rebaudianum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Eupatorieae; Stevia.
OX NCBI_TaxID=55670;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Leaf;
RX PubMed=15610349; DOI=10.1111/j.1365-313x.2004.02275.x;
RA Richman A., Swanson A., Humphrey T., Chapman R., McGarvey B., Pocs R.,
RA Brandle J.;
RT "Functional genomics uncovers three glucosyltransferases involved in the
RT synthesis of the major sweet glucosides of Stevia rebaudiana.";
RL Plant J. 41:56-67(2005).
RN [2]
RP INDUCTION.
RX PubMed=28215607; DOI=10.1016/j.phytochem.2017.02.002;
RA Yoneda Y., Nakashima H., Miyasaka J., Ohdoi K., Shimizu H.;
RT "Impact of blue, red, and far-red light treatments on gene expression and
RT steviol glycoside accumulation in Stevia rebaudiana.";
RL Phytochemistry 137:57-65(2017).
CC -!- FUNCTION: Involved in the biosynthesis of steviol glycosides in leaves
CC (PubMed:15610349). Converts steviol to the mono-glycoside
CC steviolmonoside (PubMed:15610349). Converts the mono-glycoside
CC steviolmonoside to the bi-glycoside rubusoside (PubMed:15610349).
CC Converts the bi-glycoside steviolbioside to the tri-glycoside
CC stevioside (PubMed:15610349). Converts the tri-glycoside rebaudioside B
CC to the tetra-glycoside rebaudioside A (PubMed:15610349).
CC {ECO:0000269|PubMed:15610349}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=steviolmonoside + UDP-alpha-D-glucose = rubusoside + UDP;
CC Xref=Rhea:RHEA:61736, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:145010, ChEBI:CHEBI:145021;
CC Evidence={ECO:0000269|PubMed:15610349};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61737;
CC Evidence={ECO:0000269|PubMed:15610349};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=steviolbioside + UDP-alpha-D-glucose = stevioside + UDP;
CC Xref=Rhea:RHEA:61744, ChEBI:CHEBI:9271, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:145009;
CC Evidence={ECO:0000269|PubMed:15610349};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61745;
CC Evidence={ECO:0000269|PubMed:15610349};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=steviol + UDP-alpha-D-glucose = H(+) + steviolmonoside + UDP;
CC Xref=Rhea:RHEA:61732, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:145010, ChEBI:CHEBI:145011;
CC Evidence={ECO:0000269|PubMed:15610349};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61733;
CC Evidence={ECO:0000269|PubMed:15610349};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=rebaudioside B + UDP-alpha-D-glucose = rebaudioside A + UDP;
CC Xref=Rhea:RHEA:61760, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:145012, ChEBI:CHEBI:145013;
CC Evidence={ECO:0000269|PubMed:15610349};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61761;
CC Evidence={ECO:0000269|PubMed:15610349};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=147.5 uM for steviol {ECO:0000269|PubMed:15610349};
CC KM=28.4 uM for steviolmonoside {ECO:0000269|PubMed:15610349};
CC KM=26.4 uM for steviolbioside {ECO:0000269|PubMed:15610349};
CC -!- INDUCTION: Induced by blue light and far-red light.
CC {ECO:0000269|PubMed:28215607}.
CC -!- MISCELLANEOUS: Leaves of the 'sweet herb' Stevia rebaudiana contain a
CC mix of steviol glycosides, compounds that are unique in the plant world
CC because of their intense sweetness and high concentration in leaf
CC tissue (Probable). Stevia leaves have been used as natural sweeteners
CC in South America for centuries (Probable). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AY345982; AAR06920.1; -; mRNA.
DR AlphaFoldDB; Q6VAA6; -.
DR SMR; Q6VAA6; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR BioCyc; MetaCyc:MON-17484; -.
DR GO; GO:0035251; F:UDP-glucosyltransferase activity; IDA:UniProtKB.
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; Transferase.
FT CHAIN 1..460
FT /note="UDP-glycosyltransferase 74G1"
FT /id="PRO_0000434464"
FT ACT_SITE 23
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q6VAB4"
FT ACT_SITE 117
FT /note="Charge relay"
FT /evidence="ECO:0000250|UniProtKB:Q6VAB4"
FT BINDING 23
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6VAB4"
FT BINDING 25
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q6VAB4"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6VAB4"
FT BINDING 283
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q6VAB4"
FT BINDING 336..337
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q6VAB4"
FT BINDING 354..362
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q6VAB4"
FT BINDING 376..379
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q9M156"
FT BINDING 378..379
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6VAB4"
SQ SEQUENCE 460 AA; 51402 MW; 4E854443F7DDFBFD CRC64;
MAEQQKIKKS PHVLLIPFPL QGHINPFIQF GKRLISKGVK TTLVTTIHTL NSTLNHSNTT
TTSIEIQAIS DGCDEGGFMS AGESYLETFK QVGSKSLADL IKKLQSEGTT IDAIIYDSMT
EWVLDVAIEF GIDGGSFFTQ ACVVNSLYYH VHKGLISLPL GETVSVPGFP VLQRWETPLI
LQNHEQIQSP WSQMLFGQFA NIDQARWVFT NSFYKLEEEV IEWTRKIWNL KVIGPTLPSM
YLDKRLDDDK DNGFNLYKAN HHECMNWLDD KPKESVVYVA FGSLVKHGPE QVEEITRALI
DSDVNFLWVI KHKEEGKLPE NLSEVIKTGK GLIVAWCKQL DVLAHESVGC FVTHCGFNST
LEAISLGVPV VAMPQFSDQT TNAKLLDEIL GVGVRVKADE NGIVRRGNLA SCIKMIMEEE
RGVIIRKNAV KWKDLAKVAV HEGGSSDNDI VEFVSELIKA
