ID   5GT_VERHY               Reviewed;         461 AA.
AC   Q9ZR25;
DT   29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Anthocyanidin 3-O-glucoside 5-O-glucosyltransferase;
DE            EC=2.4.1.298;
DE   AltName: Full=UDP-glucose:anthocyanin 5-O-glucosyltransferase HGT8;
DE   Flags: Precursor;
GN   Name=HGT8;
OS   Verbena hybrida (Garden vervain) (Verbena hortensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Verbenaceae; Verbeneae; Glandularia.
OX   NCBI_TaxID=76714;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   TISSUE=Petal;
RX   PubMed=10066805; DOI=10.1074/jbc.274.11.7405;
RA   Yamazaki M., Gong Z., Fukuchi-Mizutani M., Fukui Y., Tanaka Y., Kusumi T.,
RA   Saito K.;
RT   "Molecular cloning and biochemical characterization of a novel anthocyanin
RT   5-O-glucosyltransferase by mRNA differential display for plant forms
RT   regarding anthocyanin.";
RL   J. Biol. Chem. 274:7405-7411(1999).
CC   -!- FUNCTION: Catalyzes the glucosylation at the O-5 position of
CC       anthocyanidin 3-glucosides to form anthocyanidin 3,5-di-O-glucosides
CC       using UDP-glucose as sugar donor. Anthocyanidin 3,5-di-O-glucosides are
CC       molecules that are responsible for pigmentation. Also acts on
CC       anthocyanidin 3-O-(6-O-malonylglucoside). Much less active with
CC       hydroxycinnamoylglucose derivatives. No activity in the absence of the
CC       3-O-glucoside group. {ECO:0000269|PubMed:10066805}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an anthocyanidin 3-O-beta-D-glucoside + UDP-alpha-D-glucose =
CC         an anthocyanidin 3,5-di-O-beta-D-glucoside + 2 H(+) + UDP;
CC         Xref=Rhea:RHEA:35423, ChEBI:CHEBI:15378, ChEBI:CHEBI:16307,
CC         ChEBI:CHEBI:57503, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885;
CC         EC=2.4.1.298;
CC   -!- PATHWAY: Pigment biosynthesis; anthocyanin biosynthesis.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AB013598; BAA36423.1; -; mRNA.
DR   AlphaFoldDB; Q9ZR25; -.
DR   SMR; Q9ZR25; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   PRIDE; Q9ZR25; -.
DR   KEGG; ag:BAA36423; -.
DR   BRENDA; 2.4.1.298; 6615.
DR   UniPathway; UPA00009; -.
DR   GO; GO:0102816; F:UDP-D-glucose:delphinidin 3-O-glucosyl-5-O-caffeoylglucoside -O-beta-D-glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
DR   GO; GO:0009718; P:anthocyanin-containing compound biosynthetic process; IEA:UniProtKB-UniPathway.
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   2: Evidence at transcript level;
KW   Glycosyltransferase; Signal; Transferase.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..461
FT                   /note="Anthocyanidin 3-O-glucoside 5-O-glucosyltransferase"
FT                   /id="PRO_0000422566"
FT   BINDING         283
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         336..338
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         353..361
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         375..378
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   461 AA;  51347 MW;  BCD31A5497FF46D4 CRC64;
     MSRAHVLLAT FPAQGHINPA LQFAKRLANA DIQVTFFTSV YAWRRMSRTA AGSNGLINFV
     SFSDGYDDGL QPGDDGKNYM SEMKSRGIKA LSDTLAANNV DQKSSKITFV VYSHLFAWAA
     KVAREFHLRS ALLWIEPATV LDIFYFYFNG YSDEIDAGSD AIHLPGGLPV LAQRDLPSFL
     LPSTHERFRS LMKEKLETLE GEEKPKVLVN SFDALEPDAL KAIDKYEMIA IGPLIPSAFL
     DGKDPSDRSF GGDLFEKGSN DDDCLEWLST NPRSSVVYVS FGSFVNTTKS QMEEIARGLL
     DCGRPFLWVV RVNEGEEVLI SCMEELKRVG KIVSWCSQLE VLTHPSLGCF VTHCGWNSTL
     ESISFGVPMV AFPQWFDQGT NAKLMEDVWR TGVRVRANEE GSVVDGDEIR RCIEEVMDGG
     EKSRKLRESA GKWKDLARKA MEEDGSSVNN LKVFLDEVVG I