ID   U73E1_STERE             Reviewed;         495 AA.
AC   Q6VAA9;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=UDP-glycosyltransferase 73E1 {ECO:0000303|PubMed:15610349};
DE            EC=2.4.1.- {ECO:0000305};
GN   Name=UGT73E1 {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; AY345979; AAR06917.1; -; mRNA.
DR   AlphaFoldDB; Q6VAA9; -.
DR   SMR; Q6VAA9; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   PRIDE; Q6VAA9; -.
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..495
FT                   /note="UDP-glycosyltransferase 73E1"
FT                   /id="PRO_0000434463"
FT   BINDING         299
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         355..356
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         373..381
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         395..398
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
SQ   SEQUENCE   495 AA;  55216 MW;  D429D4160B60BF5A CRC64;
     MSPKMVAPPT NLHFVLFPLM AQGHLVPMVD IARILAQRGA TVTIITTPYH ANRVRPVISR
     AIATNLKIQL LELQLRSTEA GLPEGCESFD QLPSFEYWKN ISTAIDLLQQ PAEDLLRELS
     PPPDCIISDF LFPWTTDVAR RLNIPRLVFN GPGCFYLLCI HVAITSNILG ENEPVSSNTE
     RVVLPGLPDR IEVTKLQIVG SSRPANVDEM GSWLRAVEAE KASFGIVVNT FEELEPEYVE
     EYKTVKDKKM WCIGPVSLCN KTGPDLAERG NKAAITEHNC LKWLDERKLG SVLYVCLGSL
     ARISAAQAIE LGLGLESINR PFIWCVRNET DELKTWFLDG FEERVRDRGL IVHGWAPQVL
     ILSHPTIGGF LTHCGWNSTI ESITAGVPMI TWPFFADQFL NEAFIVEVLK IGVRIGVERA
     CLFGEEDKVG VLVKKEDVKK AVECLMDEDE DGDQRRKRVI ELAKMAKIAM AEGGSSYENV
     SSLIRDVTET VRAPH