ID   5GT2_PERFR              Reviewed;         443 AA.
AC   Q9ZR26;
DT   29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Anthocyanidin 3-O-glucoside 5-O-glucosyltransferase 2;
DE            EC=2.4.1.298;
DE   AltName: Full=UDP-glucose:anthocyanin 5-O-glucosyltransferase 3R6;
DE            Short=p3R6;
DE   Flags: Precursor;
GN   Name=PF3R6;
OS   Perilla frutescens (Beefsteak mint) (Perilla ocymoides).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Elsholtzieae; Perilla.
OX   NCBI_TaxID=48386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
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 (By similarity). {ECO:0000250}.
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}.
CC   -!- CAUTION: No enzymatic activity has been detected when expressed in
CC       yeast, suggesting it may be inactive. {ECO:0000305|PubMed:10066805}.
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DR   EMBL; AB013597; BAA36422.1; -; mRNA.
DR   AlphaFoldDB; Q9ZR26; -.
DR   SMR; Q9ZR26; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   BRENDA; 2.4.1.298; 4681.
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..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..443
FT                   /note="Anthocyanidin 3-O-glucoside 5-O-glucosyltransferase
FT                   2"
FT                   /id="PRO_0000422565"
FT   BINDING         278
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         338..340
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         355..363
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         377..380
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   443 AA;  49110 MW;  7563B333ED164B2D CRC64;
     MVRRRVLLAT FPAQGHINPA LQFAKRLLKA GTDVTFFTSV YAWRRMANTA SAAAGNPPGL
     DFVAFSDGYD DGLKPGGDGK RYMSEMKARG SEALRNLLLN NDDVTFVVYS HLFAWAAEVA
     RLSHVPTALL WVEPATVLCI YHFYFNGYAD EIDAGSNEIQ LPRLPSLEQR SLPTFLLPAT
     PERFRLMMKE KLETLDGEEK AKVLVNTFDA LEPDALTAID RYELIGIGPL IPSAFLDGED
     PSETSYGGDL FEKSEENNCV EWLNSKPKSS VVYVSFGSVL RFPKAQMEEI GKGLLACGRP
     FLWMIREQKN DDGEEEEEEE ELSCIGELKK MGKIVSWCSQ LEVLAHPALG CFVTHCGWNS
     AVESLSCGIP VVAVPQWFDQ TTNAKLIEDA WGTGVRVRMN EGGGVDGCEI ERCVEMVMDG
     GDKTKLVREN AIKWKTLARQ AMG