UGT1_BARVU
ID UGT1_BARVU Reviewed; 495 AA.
AC K4GHR9;
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 1 {ECO:0000303|PubMed:23027665};
DE Short=BvUGT1 {ECO:0000303|PubMed:23027665};
DE EC=2.4.1.368 {ECO:0000269|PubMed:23027665};
DE AltName: Full=Oleanolate 3-O-glucosyltransferase UGT1 {ECO:0000305};
GN Name=UGT1 {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 [MRNA], 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 (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; JQ291611; AFN26664.1; -; mRNA.
DR AlphaFoldDB; K4GHR9; -.
DR SMR; K4GHR9; -.
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 1"
FT /id="PRO_0000452126"
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; 55599 MW; A01665455BCEEF5B 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 ELLEWFSDSG FEERVKDRGL LIKGWSPQML
ILAHHSVGGF LTHCGWNSTL EGITSGIPLL TWPLFGDQFC NQKLVVQVLK VGVSAGVEEV
TNWGEEEKIG VLVDKEGVKK AVEELMGESD DAKERRKRVK ELGQLAQKAV EEGGSSHSNI
TSLLEDIMQL AQSNN