ID   U79A2_STERE             Reviewed;         454 AA.
AC   Q6VAA3;
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 79A2 {ECO:0000303|PubMed:15610349};
DE            EC=2.4.1.- {ECO:0000305};
GN   Name=UGT79A2 {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; AY345985; AAR06923.1; -; mRNA.
DR   AlphaFoldDB; Q6VAA3; -.
DR   SMR; Q6VAA3; -.
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..454
FT                   /note="UDP-glycosyltransferase 79A2"
FT                   /id="PRO_0000434467"
FT   BINDING         269
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         330..331
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         348..356
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         370..373
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
SQ   SEQUENCE   454 AA;  50875 MW;  F7918369767A4DAA CRC64;
     MSLKGNDKEL HLVMFPFFAF GHITPFVQLS NKISSLYPGV KITFLAASAS VSRIETMLNP
     STNTKVIPLT LPRVDGLPEG VENTADASPA TIGLLVVAID LMQPQIKTLL ANLKPDFVIF
     DFVHWWLPEI ASELGIKTIY FSVYMANIVM PSTSKLTGNK PSTVEDIKAL QQSYGIPVKT
     FEAISLMNVF KSFHDWMDKC INGCNLMLIK SCREMEGSRI DDVTKQSTRP VFLIGPVVPE
     PHSGELDETW ANWLNRFPAK SVIYCSFGSE TFLTDDQIRE LALGLELTGL PFFLVLNFPA
     NVDKSAELKR TLPDGFLERV KDKGIVHSGW VQQRHILAHD SVGCYVFHAG YGSVIEGLVN
     DCQLVMLPMK VDQFTNSKVI ALELKAGVEV NRRDEDGYFG KDDVFEAVES VMMDTENEPA
     KSIRENHRKL KEFLQNDEIQ KKYIADFVEN LKAL