5GT1_PERFR
ID 5GT1_PERFR Reviewed; 460 AA.
AC Q9ZR27;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Anthocyanidin 3-O-glucoside 5-O-glucosyltransferase 1;
DE EC=2.4.1.298;
DE AltName: Full=UDP-glucose:anthocyanin 5-O-glucosyltransferase 3R4;
DE Short=p3R4;
DE Flags: Precursor;
GN Name=PF3R4;
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], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
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. {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; Evidence={ECO:0000269|PubMed:10066805};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=31.4 mM for 3-O-glucoside {ECO:0000269|PubMed:10066805};
CC KM=940 mM for UDP-glucose {ECO:0000269|PubMed:10066805};
CC pH dependence:
CC Optimum pH is 8.0-8.5. {ECO:0000269|PubMed:10066805};
CC -!- PATHWAY: Pigment biosynthesis; anthocyanin biosynthesis.
CC {ECO:0000269|PubMed:10066805}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AB013596; BAA36421.1; -; mRNA.
DR AlphaFoldDB; Q9ZR27; -.
DR SMR; Q9ZR27; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR PRIDE; Q9ZR27; -.
DR KEGG; ag:BAA36421; -.
DR BRENDA; 2.4.1.298; 4681.
DR SABIO-RK; Q9ZR27; -.
DR UniPathway; UPA00009; -.
DR GO; GO:0016758; F:hexosyltransferase activity; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0043473; P:pigmentation; TAS: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; Signal; Transferase.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..460
FT /note="Anthocyanidin 3-O-glucoside 5-O-glucosyltransferase
FT 1"
FT /id="PRO_0000422564"
FT BINDING 278
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 460 AA; 50974 MW; 5AE632733535D089 CRC64;
MVRRRVLLAT FPAQGHINPA LQFAKRLLKA GTDVTFFTSV YAWRRMANTA SAAAGNPPGL
DFVAFSDGYD DGLKPCGDGK RYMSEMKARG SEALRNLLLN NHDVTFVVYS HLFAWAAEVA
RESQVPSALL WVEPATVLCI YYFYFNGYAD EIDAGSDEIQ LPRLPPLEQR SLPTFLLPET
PERFRLMMKE KLETLDGEEK AKVLVNTFDA LEPDALTAID RYELIGIGPL IPSAFLDGGD
PSETSYGGDL FEKSEENNCV EWLDTKPKSS VVYVSFGSVL RFPKAQMEEI GKGLLACGRP
FLWMIREQKN DDGEEEEEEL SCIGELKKMG KIVSWCSQLE VLAHPALGCF VTHCGWNSAV
ESLSCGVPVV AVPQWFDQTT NAKLIEDAWG TGVRVRMNEG GGVDGSEIER CVEMVMDGGE
KSKLVRENAI KWKTLAREAM GEDGSSLKNL NAFLHQVARA
