ID   73C10_BARVU             Reviewed;         495 AA.
AC   K4GKX2;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 1.
DT   03-AUG-2022, entry version 30.
DE   RecName: Full=UDP-glycosyltransferase 73C10 {ECO:0000303|PubMed:23027665};
DE            EC=2.4.1.368 {ECO:0000269|PubMed:23027665};
DE   AltName: Full=Oleanolate 3-O-glucosyltransferase UGT73C10 {ECO:0000305};
GN   Name=UGT73C10 {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], FUNCTION, AND CATALYTIC ACTIVITY.
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: Catalyzes the transfer of a glucose (Glc) moiety from UDP-Glc
CC       to the C-3 position of the oleanane sapogenins oleanolate and
CC       hederagenin, and to the C-28 carboxylic group of the lupane sapogenin
CC       betulinate (PubMed:23027665). The monoglucosylated hederagenin 3-O-
CC       beta-D-glucoside is a feeding deterrent of the yellow-striped flea
CC       beetle (Phyllotreta nemorum) (PubMed:23027665).
CC       {ECO:0000269|PubMed:23027665}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=oleanolate + UDP-alpha-D-glucose = H(+) + oleanolate 3-O-beta-
CC         D-glucoside + UDP; Xref=Rhea:RHEA:58024, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:82828,
CC         ChEBI:CHEBI:142488; EC=2.4.1.368;
CC         Evidence={ECO:0000269|PubMed:23027665};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58025;
CC         Evidence={ECO:0000269|PubMed:23027665};
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; JQ291613; AFN26666.1; -; Genomic_DNA.
DR   AlphaFoldDB; K4GKX2; -.
DR   SMR; K4GKX2; -.
DR   KEGG; ag:AFN26666; -.
DR   BRENDA; 2.4.1.368; 16171.
DR   GO; GO:0035251; F:UDP-glucosyltransferase activity; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   Glycosyltransferase; Transferase.
FT   CHAIN           1..495
FT                   /note="UDP-glycosyltransferase 73C10"
FT                   /id="PRO_0000452128"
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;  55486 MW;  EF327C45BAF9958D CRC64;
     MVSEITHKSY PLHFVLFPFM AQGHMIPMVD IARLLAQRGV KITIVTTPHN AARFENVLSR
     AIESGLPISI VQVKLPSQEA GLPEGNETFD SLVSTKLLVP FFKAVNMLEE PVQKLFEEMS
     PQPSCIISDF CLPYTSKIAK KFNIPKILFH GMCCFCLLCM HVLRKNREIL ENLKSDKEHF
     VVPYFPDRVE FTRPQVPLAT YVPGEWHEIK EDMVEADKTS YGVIVNTYQE LEPAYANGYK
     EARSGKAWTI GPVSLCNKVG ADKAERGNKA DIDQDECLKW LDSKEEGSVL YVCLGSICSL
     PLSQLKELGL GLEESQRPFI WVVRGWEKNK ELLEWFSESG FEERVKDRGL LIKGWSPQML
     ILAHHSVGGF LTHCGWNSTL EGITSGVPLL TWPLFGDQFC NQKLVVQVLK VGVSAGVEEV
     TNWGEEEKIG VLVDKEGVKK AVEELMGESD DAKEIRKRVK ELGQLAHKAV EEGGSSHSNI
     TSLLEDIMQL AQPNN