ID   HQGT_RAUSE              Reviewed;         470 AA.
AC   Q9AR73;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Hydroquinone glucosyltransferase;
DE            EC=2.4.1.218;
DE   AltName: Full=Arbutin synthase;
GN   Name=AS;
OS   Rauvolfia serpentina (Serpentine wood) (Ophioxylon serpentinum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae; Vinceae;
OC   Rauvolfiinae; Rauvolfia.
OX   NCBI_TaxID=4060;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RX   PubMed=11937332; DOI=10.1016/s0968-0896(02)00029-9;
RA   Hefner T., Arend J., Warzecha H., Siems K., Stoeckigt J.;
RT   "Arbutin synthase, a novel member of the NRD1beta glycosyltransferase
RT   family, is a unique multifunctional enzyme converting various natural
RT   products and xenobiotics.";
RL   Bioorg. Med. Chem. 10:1731-1741(2002).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RX   PubMed=10680170; DOI=10.1016/s0031-9422(99)00539-7;
RA   Arend J., Warzecha H., Stoeckigt J.;
RT   "Hydroquinone:O-glucosyltransferase from cultivated Rauvolfia cells:
RT   enrichment and partial amino acid sequences.";
RL   Phytochemistry 53:187-193(2000).
CC   -!- FUNCTION: Broad spectrum multifunctional glucosyltransferase. In
CC       addition to hydroquinone it accept at least 45 natural and synthetic
CC       phenols as well as two cinnamyl alcohols as substrates. Hydroquinone
CC       was however the best substrate. In contrast to this broad acceptor
CC       substrate specificity, only pyrimidine nucleotide activated glucose is
CC       tolerated as a donor substrate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hydroquinone + UDP-alpha-D-glucose = H(+) + hydroquinone O-
CC         beta-D-glucopyranoside + UDP; Xref=Rhea:RHEA:12560,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17594, ChEBI:CHEBI:18305,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.218;
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; AJ310148; CAC35167.1; -; mRNA.
DR   AlphaFoldDB; Q9AR73; -.
DR   SMR; Q9AR73; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   KEGG; ag:CAC35167; -.
DR   BRENDA; 2.4.1.218; 5309.
DR   GO; GO:0050505; F:hydroquinone glucosyltransferase activity; IEA:UniProtKB-EC.
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   Direct protein sequencing; Glycosyltransferase; Transferase.
FT   CHAIN           1..470
FT                   /note="Hydroquinone glucosyltransferase"
FT                   /id="PRO_0000074161"
SQ   SEQUENCE   470 AA;  51794 MW;  9C1B4A0760321F51 CRC64;
     MEHTPHIAMV PTPGMGHLIP LVEFAKRLVL RHNFGVTFII PTDGPLPKAQ KSFLDALPAG
     VNYVLLPPVS FDDLPADVRI ETRICLTITR SLPFVRDAVK TLLATTKLAA LVVDLFGTDA
     FDVAIEFKVS PYIFYPTTAM CLSLFFHLPK LDQMVSCEYR DVPEPLQIPG CIPIHGKDFL
     DPAQDRKNDA YKCLLHQAKR YRLAEGIMVN TFNDLEPGPL KALQEEDQGK PPVYPIGPLI
     RADSSSKVDD CECLKWLDDQ PRGSVLFISF GSGGAVSHNQ FIELALGLEM SEQRFLWVVR
     SPNDKIANAT YFSIQNQNDA LAYLPEGFLE RTKGRCLLVP SWAPQTEILS HGSTGGFLTH
     CGWNSILESV VNGVPLIAWP LYAEQKMNAV MLTEGLKVAL RPKAGENGLI GRVEIANAVK
     GLMEGEEGKK FRSTMKDLKD AASRALSDDG SSTKALAELA CKWENKISST