AA5GT_DIACA
ID AA5GT_DIACA Reviewed; 502 AA.
AC E3W9M2;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Cyanidin 3-O-glucoside 5-O-glucosyltransferase (acyl-glucose);
DE Short=AA5GT;
DE Short=Dc AA5GT;
DE EC=2.4.1.299;
DE AltName: Full=Acyl-glucose-dependent anthocyanin 5-O-glucosytransferase;
DE AltName: Full=Beta-glucosidase like protein;
DE Short=DcBGLUL;
DE Flags: Precursor;
GN Name=AA5GT;
OS Dianthus caryophyllus (Carnation) (Clove pink).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Caryophyllaceae; Caryophylleae; Dianthus.
OX NCBI_TaxID=3570;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 31-41; 126-138; 141-152 AND
RP 300-311, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RC TISSUE=Petal;
RX PubMed=20971893; DOI=10.1105/tpc.110.077487;
RA Matsuba Y., Sasaki N., Tera M., Okamura M., Abe Y., Okamoto E.,
RA Nakamura H., Funabashi H., Takatsu M., Saito M., Matsuoka H., Nagasawa K.,
RA Ozeki Y.;
RT "A novel glucosylation reaction on anthocyanins catalyzed by acyl-glucose-
RT dependent glucosyltransferase in the petals of carnation and delphinium.";
RL Plant Cell 22:3374-3389(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RX PubMed=22048706; DOI=10.1007/s00438-011-0655-7;
RA Nishizaki Y., Matsuba Y., Okamoto E., Okamura M., Ozeki Y., Sasaki N.;
RT "Structure of the acyl-glucose-dependent anthocyanin 5-O-
RT glucosyltransferase gene in carnations and its disruption by transposable
RT elements in some varieties.";
RL Mol. Genet. Genomics 286:383-394(2011).
CC -!- FUNCTION: Beta-glycosidase that catalyzes the transfer of glucose
CC moiety to anthocyanidin 3-glucoside at the 5 position. Anthocyanins are
CC ubiquitous colored pigments that are responsible for variations in
CC petal color. Uses acyl-glucoses, but not UDP-glucose, as the glucose
CC donor. {ECO:0000269|PubMed:20971893}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-(trans-sinapoyl)-beta-D-glucose + cyanidin 3-O-beta-D-
CC glucoside = cyanidin 3,5-di-O-beta-D-glucoside + E-sinapate;
CC Xref=Rhea:RHEA:35427, ChEBI:CHEBI:16546, ChEBI:CHEBI:30023,
CC ChEBI:CHEBI:71511, ChEBI:CHEBI:77857; EC=2.4.1.299;
CC Evidence={ECO:0000269|PubMed:20971893};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13 mM for cyanidin 3-glucopyranoside (with native enzyme at pH 5.0
CC and 30 degrees Celsius) {ECO:0000269|PubMed:20971893};
CC KM=46.5 mM for 1-O-beta-D-vanillyl-glucose (with native enzyme at pH
CC 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:20971893};
CC KM=6.5 mM for cyanidin 3-glucopyranoside (with recombinant enzyme at
CC pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:20971893};
CC KM=51.9 mM for 1-O-beta-D-vanillyl-glucose (with recombinant enzyme
CC at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:20971893};
CC Note=kcat is 0.06 sec(-1) with cyanidin 3-glucopyranoside (with
CC native enzyme at pH 5.0 and 30 degrees Celsius). kcat is 0.01 sec(-1)
CC with 1-O-beta-D-vanillyl-glucose (with native enzyme at pH 5.0 and 30
CC degrees Celsius). kcat is 0.07 sec(-1) with cyanidin 3-
CC glucopyranoside (with recombinant enzyme at pH 5.0 and 30 degrees
CC Celsius). kcat is 0.01 sec(-1) with 1-O-beta-D-vanillyl-glucose (with
CC recombinant enzyme at pH 5.0 and 30 degrees Celsius).;
CC pH dependence:
CC Optimum pH is 4.5-5.0. {ECO:0000269|PubMed:20971893};
CC Temperature dependence:
CC Optimum temperature is 48 degrees Celsius.
CC {ECO:0000269|PubMed:20971893};
CC -!- PATHWAY: Pigment biosynthesis; anthocyanin biosynthesis.
CC {ECO:0000269|PubMed:20971893}.
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:20971893}.
CC -!- TISSUE SPECIFICITY: Expressed in petals. {ECO:0000269|PubMed:20971893}.
CC -!- DEVELOPMENTAL STAGE: Expression peaks at stage 2 of petal development.
CC {ECO:0000269|PubMed:20971893}.
CC -!- DISRUPTION PHENOTYPE: Petal color variations. Petals accumulate
CC anthocyanin lacking the glucosyl moiety at the 5 position.
CC {ECO:0000269|PubMed:20971893, ECO:0000269|PubMed:22048706}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR EMBL; AB507446; BAJ33501.1; -; mRNA.
DR EMBL; AB646510; BAL45928.1; -; Genomic_DNA.
DR AlphaFoldDB; E3W9M2; -.
DR SMR; E3W9M2; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR KEGG; ag:BAJ33501; -.
DR BioCyc; MetaCyc:MON-17997; -.
DR SABIO-RK; E3W9M2; -.
DR UniPathway; UPA00009; -.
DR GO; GO:0000325; C:plant-type vacuole; IDA:UniProtKB.
DR GO; GO:0102458; F:cyanidin 3-O-glucoside 5-O glucosyltransferase (vanilloyl-glucose dependent) activity; IEA:UniProtKB-EC.
DR GO; GO:0102506; F:cyanidin 3-O-glucoside 5-O-glucosyltransferase (acyl-glucose dependent) activity; IEA:UniProtKB-EC.
DR GO; GO:0102512; F:delphinidin 3-O-glucoside 5-O-glucosyltransferase (acyl-glucose dependent) activity; IEA:UniProtKB-EC.
DR GO; GO:0016758; F:hexosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0102510; F:pelargonidin 3-O-glucoside 5-O-glucosyltransferase (acyl-glucose dependent) activity; IEA:UniProtKB-EC.
DR GO; GO:0009718; P:anthocyanin-containing compound biosynthetic process; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0043473; P:pigmentation; IDA:UniProtKB.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10353; PTHR10353; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Glycosyltransferase; Signal;
KW Transferase; Vacuole.
FT SIGNAL 1..30
FT /evidence="ECO:0000269|PubMed:20971893"
FT CHAIN 31..502
FT /note="Cyanidin 3-O-glucoside 5-O-glucosyltransferase
FT (acyl-glucose)"
FT /id="PRO_0000422568"
FT ACT_SITE 197
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 388
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 320
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 435
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 442..443
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 502 AA; 57480 MW; DEF53E8E049E91E1 CRC64;
MNMSCKFEIV LLVSWWLLLV LVFGVESSMF SEFDRLDFPK HFIFGASSCA YQVEGAAFED
GRTLSTFDIA AHSGHLPGNG DITSDEYHKY KEDVELMVET GLDAYRFSIS WSRLIPNGRG
PVNPKGLEYY NNLVNALLTK GTQPHVTLLH SDLPQALRDE YGGLFISPKF IDDFVAYADV
CFREFGDRVL HWTTFNEANF LAFGDENTPA SALYLSAHHL LLAHASATRL YRENYQASQR
GFIGINVYAY DFIPETNTEV DVIAAKRARD FFIGWFVQPL MNGEYPLTMR KNGGPRLPKF
TPNETELLTG SYDFIGLNYY TAKTVKDDPV MLTVEPRNYY TDQGLISSYL GNIDPYQGHP
FFNTPWGLHD VLQQFKQVYG NPPVYIHENG EVGDHDADYD KLINDIPRVE YLQGHIRAVL
DAVRNGSNVK GYFVWSFLDM YELMYGTKFT FGLYYIDFND PKLTRHPKLS QKWYSRFLKG
EKASTKASIH TPNEAETHTY FY
