位置:首页 > 蛋白库 > UGT1_BARVU
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024