ID   U88B1_STERE             Reviewed;         461 AA.
AC   Q6VAA7;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=UDP-glycosyltransferase 88B1 {ECO:0000303|PubMed:15610349};
DE            EC=2.4.1.- {ECO:0000305};
GN   Name=UGT88B1 {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; AY345981; AAR06919.1; -; mRNA.
DR   AlphaFoldDB; Q6VAA7; -.
DR   SMR; Q6VAA7; -.
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..461
FT                   /note="UDP-glycosyltransferase 88B1"
FT                   /id="PRO_0000434471"
FT   BINDING         278
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         340..341
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         358..366
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         380..383
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
SQ   SEQUENCE   461 AA;  50901 MW;  A0B21043D350A9E3 CRC64;
     MESSKVILYP SPGIGHLVSM VELGKLIHTH HPSLSVIILV LPATYETGST TTYINTVSTT
     TPFITFHHLP VIPLPPDSSS EFIDLAFDIP QLYNPVVYNT LVAISETSTI KAVILDFFVN
     AAFQISKSLD LPTYYFFTSG ASGLCAFLHL PTIYKTYSGN FKDLDTFINI PGVPPIHSSD
     MPTVLFDKES NSYKNFVKTS NNMAKSSGVI ANSFLQLEER AAQTLRDGKS ITDGPSPPIY
     LIGPLIASGN QVDHNENECL KWLNTQPSKS VVFLCFGSQG VFKKEQLKEI AVGLERSGQR
     FLWVVRKPPS DGGKEFGLDD VLPEGFVART KEKGLVVKNW APQPAILGHE SVGGFVSHCG
     WNSSLEAVVF GVPMVAWPLY AEQKMNRVYL VEEIKVALWL RMSADGFVSA EAVEETVRQL
     MDGRRVRERI LEMSTKAKAA VEDGGSSRVD FFKLTESWTH K