ID   U85C1_STERE             Reviewed;         483 AA.
AC   Q6VAA4;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=UDP-glycosyltransferase 85C1 {ECO:0000303|PubMed:15610349};
DE            EC=2.4.1.- {ECO:0000305};
GN   Name=UGT85C1 {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; AY345984; AAR06922.1; -; mRNA.
DR   AlphaFoldDB; Q6VAA4; -.
DR   SMR; Q6VAA4; -.
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..483
FT                   /note="UDP-glycosyltransferase 85C1"
FT                   /id="PRO_0000434469"
FT   BINDING         304
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         360..361
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         378..386
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         400..403
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
SQ   SEQUENCE   483 AA;  54898 MW;  03D2785052671B11 CRC64;
     MDQMAKIDEK KPHVVFIPFP AQSHIKCMLK LARILHQKGL YITFINTDTN HERLVASGGT
     QWLENAPGFW FKTVPDGFGS AKDDGVKPTD ALRELMDYLK TNFFDLFLDL VLKLEVPATC
     IICDGCMTFA NTIRAAEKLN IPVILFWTMA ACGFMAFYQA KVLKEKEIVP VKDETYLTNG
     YLDMEIDWIP GMKRIRLRDL PEFILATKQN YFAFEFLFET AQLADKVSHM IIHTFEELEA
     SLVSEIKSIF PNVYTIGPLQ LLLNKITQKE TNNDSYSLWK EEPECVEWLN SKEPNSVVYV
     NFGSLAVMSL QDLVEFGWGL VNSNHYFLWI IRANLIDGKP AVMPQELKEA MNEKGFVGSW
     CSQEEVLNHP AVGGFLTHCG WGSIIESLSA GVPMLGWPSI GDQRANCRQM CKEWEVGMEI
     GKNVKRDEVE KLVRMLMEGL EGERMRKKAL EWKKSATLAT CCNGSSSLDV EKLANEIKKL
     SRN