ID   U71E1_STERE             Reviewed;         474 AA.
AC   Q6VAB2;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=UDP-glycosyltransferase 71E1 {ECO:0000303|PubMed:15610349};
DE            EC=2.4.1.- {ECO:0000305};
GN   Name=UGT71E1 {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].
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).
CC   -!- FUNCTION: May glycosylate diterpenes or flavonols in leaves.
CC       {ECO:0000250|UniProtKB:Q6VAA6}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AY345976; AAR06914.1; -; mRNA.
DR   AlphaFoldDB; Q6VAB2; -.
DR   SMR; Q6VAB2; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   PRIDE; Q6VAB2; -.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Glycosyltransferase; Transferase.
FT   CHAIN           1..474
FT                   /note="UDP-glycosyltransferase 71E1"
FT                   /id="PRO_0000434462"
FT   BINDING         275
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         341..342
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         359..367
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         381..384
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
SQ   SEQUENCE   474 AA;  52743 MW;  F9A5012FD485EC2E CRC64;
     MSTSELVFIP SPGAGHLPPT VELAKLLLHR DQRLSVTIIV MNLWLGPKHN TEARPCVPSL
     RFVDIPCDES TMALISPNTF ISAFVEHHKP RVRDIVRGII ESDSVRLAGF VLDMFCMPMS
     DVANEFGVPS YNYFTSGAAT LGLMFHLQWK RDHEGYDATE LKNSDTELSV PSYVNPVPAK
     VLPEVVLDKE GGSKMFLDLA ERIRESKGII VNSCQAIERH ALEYLSSNNN GIPPVFPVGP
     ILNLENKKDD AKTDEIMRWL NEQPESSVVF LCFGSMGSFN EKQVKEIAVA IERSGHRFLW
     SLRRPTPKEK IEFPKEYENL EEVLPEGFLK RTSSIGKVIG WAPQMAVLSH PSVGGFVSHC
     GWNSTLESMW CGVPMAAWPL YAEQTLNAFL LVVELGLAAE IRMDYRTDTK AGYDGGMEVT
     VEEIEDGIRK LMSDGEIRNK VKDVKEKSRA AVVEGGSSYA SIGKFIEHVS NVTI