ID   U91D1_STERE             Reviewed;         485 AA.
AC   Q6VAA8;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=UDP-glycosyltransferase 91D1 {ECO:0000303|PubMed:15610349};
DE            EC=2.4.1.- {ECO:0000305};
GN   Name=UGT91D1 {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; AY345980; AAR06918.1; -; mRNA.
DR   AlphaFoldDB; Q6VAA8; -.
DR   SMR; Q6VAA8; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
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..485
FT                   /note="UDP-glycosyltransferase 91D1"
FT                   /id="PRO_0000434473"
FT   BINDING         296
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   485 AA;  54640 MW;  DCB16DB3EED86333 CRC64;
     MYNVTYHQNS KAMATSDSIV DDRKQLHVAT FPWLAFGHIL PFLQLSKLIA EKGHKVSFLS
     TTRNIQRLSS HISPLINVVQ LTLPRVQELP EDAEATTDVH PEDIQYLKKA VDGLQPEVTR
     FLEQHSPDWI IYDFTHYWLP SIAASLGISR AYFCVITPWT IAYLAPSSDA MINDSDGRTT
     VEDLTTPPKW FPFPTKVCWR KHDLARMEPY EAPGISDGYR MGMVFKGSDC LLFKCYHEFG
     TQWLPLLETL HQVPVVPVGL LPPEIPGDEK DETWVSIKKW LDGKQKGSVV YVALGSEALV
     SQTEVVELAL GLELSGLPFV WAYRKPKGPA KSDSVELPDG FVERTRDRGL VWTSWAPQLR
     ILSHESVCGF LTHCGSGSIV EGLMFGHPLI MLPIFCDQPL NARLLEDKQV GIEIPRNEED
     GCLTKESVAR SLRSVVVENE GEIYKANARA LSKIYNDTKV EKEYVSQFVD YLEKNARAVA
     IDHES