4CGT_ANTMA
ID 4CGT_ANTMA Reviewed; 457 AA.
AC Q33DV3; A6YS03;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Chalcone 4'-O-glucosyltransferase;
DE Short=4'CGT;
DE Short=Am4'CGT;
DE EC=2.4.1.286;
OS Antirrhinum majus (Garden snapdragon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Plantaginaceae; Antirrhineae; Antirrhinum.
OX NCBI_TaxID=4151;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16832053; DOI=10.1073/pnas.0604246103;
RA Ono E., Fukuchi-Mizutani M., Nakamura N., Fukui Y., Yonekura-Sakakibara K.,
RA Yamaguchi M., Nakayama T., Tanaka T., Kusumi T., Tanaka Y.;
RT "Yellow flowers generated by expression of the aurone biosynthetic
RT pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11075-11080(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA Wang C.-K., To K.-Y.;
RT "Genes involved in aurone biosynthesis.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Glycosyltransferase involved in the biosynthesis of aurones,
CC plant flavonoids that provide yellow coloration to flowers.
CC {ECO:0000269|PubMed:16832053}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2',4,4',6'-tetrahydroxychalcone + UDP-alpha-D-glucose =
CC 2',4,4',6'-tetrahydroxychalcone 4'-O-beta-D-glucoside + H(+) + UDP;
CC Xref=Rhea:RHEA:34291, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:77645, ChEBI:CHEBI:77978;
CC EC=2.4.1.286; Evidence={ECO:0000269|PubMed:16832053};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2',3,4,4',6'-pentahydroxychalcone + UDP-alpha-D-glucose =
CC 2',3,4,4',6'-pentahydroxychalcone 4'-O-beta-D-glucoside + H(+) + UDP;
CC Xref=Rhea:RHEA:34295, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:77621, ChEBI:CHEBI:77622;
CC EC=2.4.1.286; Evidence={ECO:0000269|PubMed:16832053};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16832053}.
CC -!- TISSUE SPECIFICITY: Expressed in petals. Not detected in stems and
CC leaves. {ECO:0000269|PubMed:16832053}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AB198665; BAE48239.1; -; mRNA.
DR EMBL; EF650015; ABR57234.1; -; mRNA.
DR EMBL; JQ234673; AFC90118.1; -; Genomic_DNA.
DR AlphaFoldDB; Q33DV3; -.
DR SMR; Q33DV3; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR KEGG; ag:BAE48239; -.
DR BRENDA; 2.4.1.286; 376.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0102891; F:2'4'6'34-pentahydroxychalcone 4'-O-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016758; F:hexosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0102890; F:naringenin chalcone 4'-O-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
DR GO; GO:0046148; P:pigment biosynthetic process; IDA: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 Cytoplasm; Glycosyltransferase; Transferase.
FT CHAIN 1..457
FT /note="Chalcone 4'-O-glucosyltransferase"
FT /id="PRO_0000421820"
FT CONFLICT 99
FT /note="R -> G (in Ref. 2; AFC90118/ABR57234)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="T -> S (in Ref. 2; AFC90118/ABR57234)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="L -> V (in Ref. 2; AFC90118/ABR57234)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="E -> D (in Ref. 2; AFC90118/ABR57234)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="V -> A (in Ref. 2; AFC90118/ABR57234)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="S -> N (in Ref. 2; AFC90118/ABR57234)"
FT /evidence="ECO:0000305"
FT CONFLICT 446..447
FT /note="AS -> VA (in Ref. 2; AFC90118/ABR57234)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 457 AA; 50857 MW; EE79B17EDADDB331 CRC64;
MGEEYKKTHT IVFHTSEEHL NSSIALAKFI TKHHSSISIT IISTAPAESS EVAKIINNPS
ITYRGLTAVA LPENLTSNIN KNPVELFFEI PRLQNANLRE ALLDISRKSD IKALIIDFFC
NAAFEVSTSM NIPTYFDVSG GAFLLCTFLH HPTLHQTVRG DIADLNDSVE MPGFPLIHSS
DLPMSLFYRK TNVYKHFLDT SLNMRKSSGI LVNTFVALEF RAKEALSNGL YGPTPPLYLL
SHTIAEPHDT KVLVNQHECL SWLDLQPSKS VIFLCFGRRG AFSAQQLKEI AIGLEKSGCR
FLWLARISPE MDLNALLPEG FLSRTKGVGF VTNTWVPQKE VLSHDAVGGF VTHCGWSSVL
EALSFGVPMI GWPLYAEQRI NRVFMVEEIK VALPLDEEDG FVTAMELEKR VRELMESVKG
KEVKRRVAEL KISTKAAVSK GGSSLASLEK FINSVTR