ID   U85A8_STERE             Reviewed;         479 AA.
AC   Q6VAB3;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=UDP-glycosyltransferase 85A8 {ECO:0000303|PubMed:15610349};
DE            EC=2.4.1.- {ECO:0000305};
GN   Name=UGT85A8 {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; AY345975; AAR06913.1; -; mRNA.
DR   AlphaFoldDB; Q6VAB3; -.
DR   SMR; Q6VAB3; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   PRIDE; Q6VAB3; -.
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..479
FT                   /note="UDP-glycosyltransferase 85A8"
FT                   /id="PRO_0000434468"
FT   BINDING         302
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         358..359
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         376..384
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         398..401
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
SQ   SEQUENCE   479 AA;  54242 MW;  A71B14144C2AAA9E CRC64;
     MASIAEMQKP HAICIPYPAQ GHINPMMQFA KLLHFKGFHI SFVNNHYNHK RLQRSRGLSA
     LEGLPDFHFY SIPDGLPPSN AEATQSIPGL CESIPKHSLE PFCDLIATLN GSDVPPVSCI
     ISDGVMSFTL QAAERFGLPE VLFWTPSACG FLAYTHYRDL VDKEYIPLKD TNDLTNGYLE
     TSLDWIPGMK NIRLKDFPSF IRTTDINDIM LNYFLIETEA IPKGVAIILN TFDALEKDSI
     TPVLALNPQI YTIGPLHMMQ QYVDHDERLK HIGSNLWKED VSCINWLDTK KPNSVVYVNF
     GSITVMTKEQ LIEFGWGLAN SKKDFLWITR PDIVGGNEAM IPAEFIEETK ERGMVTSWCS
     QEEVLKHPSI GVFLTHSGWN STIESISNGV PMICWPFFAE QQTNCRYCCV EWEIGLEIDT
     DVKREEVEAQ VREMMDGSKG KMMKNKALEW KKKAEEAVSI GGSSYLNFEK LVTDVLLRK