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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
 
 
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