ID   73C9_BARVU              Reviewed;         495 AA.
AC   K4GMD6;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 1.
DT   03-AUG-2022, entry version 28.
DE   RecName: Full=UDP-glycosyltransferase 73C9 {ECO:0000303|PubMed:23027665};
DE            EC=2.4.1.- {ECO:0000269|PubMed:23027665};
GN   Name=UGT73C9 {ECO:0000303|PubMed:23027665};
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 [GENOMIC DNA], AND FUNCTION.
RX   PubMed=23027665; DOI=10.1104/pp.112.202747;
RA   Augustin J.M., Drok S., Shinoda T., Sanmiya K., Nielsen J.K., Khakimov B.,
RA   Olsen C.E., Hansen E.H., Kuzina V., Ekstrom C.T., Hauser T., Bak S.;
RT   "UDP-glycosyltransferases from the UGT73C subfamily in Barbarea vulgaris
RT   catalyze sapogenin 3-O-glucosylation in saponin-mediated insect
RT   resistance.";
RL   Plant Physiol. 160:1881-1895(2012).
CC   -!- FUNCTION: Possesses very weak glucosyltransferase activity toward
CC       2,4,5-trichlorophenol (TCP), when assayed with high concentrations of
CC       TCP. {ECO:0000269|PubMed:23027665}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; JQ291612; AFN26665.1; -; Genomic_DNA.
DR   AlphaFoldDB; K4GMD6; -.
DR   SMR; K4GMD6; -.
DR   GO; GO:0046527; F:glucosyltransferase activity; IEA:UniProt.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
DR   GO; GO:0016134; P:saponin metabolic process; IEA:UniProt.
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   3: Inferred from homology;
KW   Glycosyltransferase; Transferase.
FT   CHAIN           1..495
FT                   /note="UDP-glycosyltransferase 73C9"
FT                   /id="PRO_0000452127"
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;  55543 MW;  54DE55906E918CCE CRC64;
     MVSEITHQSY PLHFVLFPYM AQGHMIPMVD IARLLAQRGV KITIVTTPQN AARFENVLSR
     AIESGLPISI VQVKLPSQEA GLPEGIETFE SLVSMELLVP FFKAVNMLEE PVQKLFEEMS
     PQPSCIISDF CLHYTSKIAK KFNIPKILFH GMCCFCLLCM HVLRKNCEIL ENLKSDKEHF
     VVPYFPDRVE FTRPQVPMAT YAPGDWQEIR EDIVEADKTS YGVIVNTYQE LEPAYANDYK
     EARSGKAWTI GPVSLCNKVG ADKAERGNKA DIDQDECLKW LDSKEEGSVL YVCLGSNCSV
     PLSQLKELGL GLEESQRPFI WVVRGWEKNK ELLEWFSESG FEERVKDRGL LIKGWSPQML
     ILAHHSVGGF LTHCGWNSTL EGITSGIPLL TWPLIVDQFC NQKLVVQVLK VGVSAGVEEV
     TNWGEEEKIG VLVDKEGVKK AVEELMGESD DAKERRKRVK ALGQLAHKAV EEGGSSHSNI
     TSLLEDIMQL AQSNN