ID   73C12_BARVU             Reviewed;         495 AA.
AC   K4GIP0;
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 73C12 {ECO:0000303|PubMed:23027665};
DE            EC=2.4.1.368 {ECO:0000269|PubMed:23027665};
DE   AltName: Full=Oleanolate 3-O-glucosyltransferase UGT73C12 {ECO:0000305};
GN   Name=UGT73C12 {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=24 uM for UDP-glucose {ECO:0000269|PubMed:23027665};
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; JQ291615; AFN26668.1; -; Genomic_DNA.
DR   AlphaFoldDB; K4GIP0; -.
DR   SMR; K4GIP0; -.
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 73C12"
FT                   /id="PRO_0000452130"
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;  55576 MW;  316FC29C4908E60C CRC64;
     MVSEITHKSY PLHFVLFPFM AQGHMIPMVD IARLLAQRGV KITIVTTPHN AARFKNVLSR
     AIESGLPISI VQVKLPSQEA GLPEGNETLD SLVSMELMIH FLKAVNMLEE PVQKLFEEMS
     PQPSCIISDF CLPYTSKIAK KFNIPKILFH GMCCFCLLCM HILRKNREIV ENLKSDKEHF
     VVPYFPDRVE FTRPQVPVAT YVPGDWHEIT EDMVEADKTS YGVIVNTYQE LEPAYANDYK
     EARSGKAWTI GPVSLCNKVG ADKAERGNKA DIDQDECLKW LNSKEEGSVL YVCLGSICNL
     PLSQLKELGL GLEESQRPFI WVIRGWEKNK ELHEWFSESG FEERIKDRGL LIKGWAPQML
     ILSHHSVGGF LTHCGWNSTL EGLTAGLPLL TWPLFADQFC NEKLAVQVLK AGVSAGVDQP
     MKWGEEEKIG VLVDKEGVKK AVEELMGESD DAKEIRRRAK ELGELAHKAV EEGGSSHSNI
     TSLLEDIMQL AQSNN