ID   73C13_BARVU             Reviewed;         495 AA.
AC   K4GHS2;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 1.
DT   03-AUG-2022, entry version 27.
DE   RecName: Full=UDP-glycosyltransferase 73C13 {ECO:0000303|PubMed:23027665};
DE            EC=2.4.1.368 {ECO:0000269|PubMed:23027665};
DE   AltName: Full=Oleanolate 3-O-glucosyltransferase UGT73C13 {ECO:0000305};
GN   Name=UGT73C13 {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=7.6 uM for oleanolate {ECO:0000269|PubMed:23027665};
CC         KM=22.9 uM for hederagenin {ECO:0000269|PubMed:23027665};
CC         Vmax=176 nmol/min/mg enzyme with oleanolate as substrate
CC         {ECO:0000269|PubMed:23027665};
CC         Vmax=131 nmol/min/mg enzyme with hederagenin as substrate
CC         {ECO:0000269|PubMed:23027665};
CC         Note=kcat is 0.816 sec(-1) with oleanolate as substrate
CC         (PubMed:23027665). kcat is 0.389 sec(-1) with hederagenin as
CC         substrate (PubMed:23027665). {ECO:0000269|PubMed:23027665};
CC       pH dependence:
CC         Optimum pH is 7.9. {ECO:0000269|PubMed:23027665};
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; JQ291616; AFN26669.1; -; Genomic_DNA.
DR   AlphaFoldDB; K4GHS2; -.
DR   SMR; K4GHS2; -.
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 73C13"
FT                   /id="PRO_0000452131"
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;  55427 MW;  162450488637A6CF CRC64;
     MVSEITHKSY PLHFVLFPFM AQGHMIPMVD IARLLAQRGV KITIVTTPHN AARFENVLNR
     AIESGLPISI VQVKLPSQEA GLPEGNETFD SLVSMELLVP FFKSVNMLEE PVQKLFEEMS
     PQPSCIISDF CLPYTSKIAK KFNIPKILFH GMCCFCLLCM HVLRKNHEIV ENLKSDKEHF
     VVPYFPDRVE FTRPQVPVAT YVPGDWHEIT GDMVEADKTS YGVIVNTCQE LEPAYANDYK
     EARSGKAWTI GPVSLCNKVG ADKAERGNKA DIDQDECLKW LNSKEEGSVL YVCLGSICNL
     PLSQLKELGL GLEESQRPFI WVIRGWEKNK ELLEWFSESG FEERIKDRGL LIKGWAPQML
     ILSHHSVGGF LTHCGWNSTL EGLTAGLPLL TWPLFADQFC NEKLAVQVLK AGVSAGVDQP
     MKWGEEEKIG VLVDKEGVKK AVEELMGESD DAKEIRRRAK ELGELAHKAV EEGGSSHSNI
     TSLLEDIMQL AQSNN