ID   73C11_BARVU             Reviewed;         495 AA.
AC   K4GGT4;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 1.
DT   03-AUG-2022, entry version 29.
DE   RecName: Full=UDP-glycosyltransferase 73C11 {ECO:0000303|PubMed:23027665};
DE            EC=2.4.1.368 {ECO:0000269|PubMed:23027665};
DE   AltName: Full=Oleanolate 3-O-glucosyltransferase UGT73C11 {ECO:0000305};
GN   Name=UGT73C11 {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, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=9.7 uM for oleanolate {ECO:0000269|PubMed:23027665};
CC         KM=3.3 uM for hederagenin {ECO:0000269|PubMed:23027665};
CC         KM=95 uM for UDP-glucose {ECO:0000269|PubMed:23027665};
CC         Vmax=817 nmol/min/mg enzyme with oleanolate as substrate
CC         {ECO:0000269|PubMed:23027665};
CC         Vmax=390 nmol/min/mg enzyme with hederagenin as substrate
CC         {ECO:0000269|PubMed:23027665};
CC         Note=kcat is 0.023 sec(-1) with oleanolate as substrate
CC         (PubMed:23027665). kcat is 0.006 sec(-1) with hederagenin as
CC         substrate (PubMed:23027665). {ECO:0000269|PubMed:23027665};
CC       pH dependence:
CC         Optimum pH is 8.6. {ECO:0000269|PubMed:23027665};
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; JQ291614; AFN26667.1; -; Genomic_DNA.
DR   AlphaFoldDB; K4GGT4; -.
DR   SMR; K4GGT4; -.
DR   KEGG; ag:AFN26667; -.
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 73C11"
FT                   /id="PRO_0000452129"
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;  55613 MW;  4E0CD544F0D4E451 CRC64;
     MVSEITHKSY PLHFVLFPFM AQGHMIPMVD IARLLAQRGV KITIVTTPHN AARFENVLSR
     AIESGLPISI VQVKLPSQEA GLPEGNETFD SLVSMELLVP FFKAVNMLEE PVQKLFEEMS
     PQPSCIISDF CLPYTSKIAK KFNIPKILFH GMCCFCLLCM HVLRKNREIL ENLKSDKEHF
     VVPYFPDRVE FTRPQVPMAT YVPGEWHEIK EDIVEADKTS YGVIVNTYQE LEPAYANDYK
     EARSGKAWTI GPVSLCNKVG ADKAERGNKA DIDQDECLKW LDSKEEGSVL YVCLGSICSL
     PLSQLKELGL GLEESQRPFI WVVRGWEKNK ELLEWFSESG FEERVKDRGL LIKGWSPQML
     ILAHHSVGGF LTHCGWNSTL EGITSGIPLL TWPLFGDQFC NQKLVVQVLK VGVSAGVEEV
     TNWGEEEKIG VLVDKEGVKK AVEELMGESD DAKERRKRVK ELGQLAQKAV EEGGSSHSNI
     TSLLEDIMQL AQSNN