ID   73C25_BARVU             Reviewed;         495 AA.
AC   A0A2R4LMF9;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2018, sequence version 1.
DT   03-AUG-2022, entry version 12.
DE   RecName: Full=UDP-glycosyltransferase 73C25 {ECO:0000303|PubMed:29603041};
DE            EC=2.4.1.- {ECO:0000269|PubMed:29603041};
GN   Name=UGT73C25 {ECO:0000303|PubMed:29603041};
OS   Barbarea vulgaris (Yellow rocket) (Erysimum barbarea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Cardamineae; Barbarea.
OX   NCBI_TaxID=50459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   PubMed=29603041; DOI=10.1007/s11103-018-0723-z;
RA   Erthmann P.O., Agerbirk N., Bak S.;
RT   "A tandem array of UDP-glycosyltransferases from the UGT73C subfamily
RT   glycosylate sapogenins, forming a spectrum of mono- and bisdesmosidic
RT   saponins.";
RL   Plant Mol. Biol. 97:37-55(2018).
CC   -!- FUNCTION: Catalyzes the transfer of a glucose (Glc) moiety from UDP-Glc
CC       to the C-28 carboxylic group of oleanolate 3-O-beta-D-glucoside to form
CC       oleanolate 3,28-O-beta-D-diglucoside. {ECO:0000269|PubMed:29603041}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; MF448366; AVW82181.1; -; mRNA.
DR   AlphaFoldDB; A0A2R4LMF9; -.
DR   SMR; A0A2R4LMF9; -.
DR   GO; GO:0046527; F:glucosyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
DR   GO; GO:0016134; P:saponin metabolic process; IDA:UniProtKB.
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..495
FT                   /note="UDP-glycosyltransferase 73C25"
FT                   /id="PRO_0000452132"
FT   ACT_SITE        24
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   ACT_SITE        129
FT                   /note="Charge relay"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         23..26
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         355..358
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         373..381
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         397..398
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
SQ   SEQUENCE   495 AA;  56021 MW;  2C4BE9FFD107EDAC CRC64;
     MASITNHKSD PLHFVLFPFM AQGHMIPMVD IARLLAQRGL TITIVTTPHN ASRFKNVLNR
     AIESGLPINI LHVKLPYQEV GLPEGLENID CFDSMEHMIP FFKGVNMVEE SVQKLFEEMS
     PRPSCIISDF CLPYTSKVAK KFNIPKILFH GMCCLCLLCM HVLRKNPKIL ENLKSDKEHF
     VVPYFPDKIE LTRPQVPMDT YVPGELKEFM EDLVEADKTS YGVIVNTFQE LEPAYVKDYK
     ETRSGKAWSV GPVALCNKAR IDKAERGNKS DIDQDECLKW LDSKEERSVL YVCLGSICNL
     PLAQLKELGL GLEESTRPFI WVIRGWDKNK QLVEWFSESG FEERIKDRGL LIKGWSPQML
     ILSHQSVGGF LTHCGWNSTL EGITAGLPLL TWPLFADQFC NEKLVVQVLN SGVRAGVEQP
     MKWGEEEKIG VLVDKEGVKK AVEELMGESD EANERRRRAK ELGELAHKAV EEGGSSHSNI
     TFLLQDIMQL AQSNN