ID   U89B2_STERE             Reviewed;         468 AA.
AC   Q6VAA5;
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 89B2 {ECO:0000303|PubMed:15610349};
DE            EC=2.4.1.- {ECO:0000305};
GN   Name=UGT89B2 {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; AY345983; AAR06921.1; -; mRNA.
DR   AlphaFoldDB; Q6VAA5; -.
DR   SMR; Q6VAA5; -.
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   Pfam; PF00201; UDPGT; 1.
PE   2: Evidence at transcript level;
KW   Transferase.
FT   CHAIN           1..468
FT                   /note="UDP-glycosyltransferase 89B2"
FT                   /id="PRO_0000434472"
FT   BINDING         287
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         347..348
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         365..373
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         387..390
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
SQ   SEQUENCE   468 AA;  51628 MW;  11ED735F67586221 CRC64;
     MPISDINAGS HILVFPYPAQ GHMLTLLDLT HQLAIRNLTI TILVTPKNLP TISPLLAAHP
     TTVSALLLPL PPHPAIPSGI ENVKDLPNDA FKAMMVALGD LYNPLRDWFR NQPNPPVAII
     SDFFLGWTHH LAVELGIRRY TFSPSGALAL SVIFSLWRYQ PKRIDVENEK EAIKFPKIPN
     SPEYPWWQLS PIYRSYVEGD PDSEFIKDGF LADIASWGIV INSFTELEQV YVDHLKHELG
     HDQVFAVGPL LPPGDKTSGR GGSSSNDVLS WLDTCADRTV VYVCFGSQMV LTNGQMEVVA
     LGLEKSRVKF VWSVKEPTVG HEAANYGRVP PGFEDRVSGR GLVIRGWVPQ VAILSHDSVG
     VFLTHCGWNS VMEAVAAEVL MLTWPMSADQ FSNATLLHEL KVGIKVCEGS NIVPNSDELA
     ELFSKSLSDE TRLERKRVKE FAKSAKEAVG PKGSSVGELE RLVDNLSL