U74F1_ARATH
ID U74F1_ARATH Reviewed; 449 AA.
AC O22820; Q56XT4;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Flavonol 7-O-beta-glucosyltransferase UGT74F1 {ECO:0000305};
DE EC=2.4.1.237 {ECO:0000269|PubMed:15352060};
DE AltName: Full=UDP-glycosyltransferase 74F1 {ECO:0000303|PubMed:11042215};
GN Name=UGT74F1 {ECO:0000303|PubMed:11042215};
GN OrderedLocusNames=At2g43840 {ECO:0000312|Araport:AT2G43840};
GN ORFNames=F18O19.5 {ECO:0000312|EMBL:AAB64022.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 19-449.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENE FAMILY.
RX PubMed=11042215; DOI=10.1074/jbc.m007447200;
RA Li Y., Baldauf S., Lim E.K., Bowles D.J.;
RT "Phylogenetic analysis of the UDP-glycosyltransferase multigene family of
RT Arabidopsis thaliana.";
RL J. Biol. Chem. 276:4338-4343(2001).
RN [5]
RP FUNCTION.
RX PubMed=11641410; DOI=10.1074/jbc.m109287200;
RA Lim E.K., Doucet C.J., Li Y., Elias L., Worrall D., Spencer S.P., Ross J.,
RA Bowles D.J.;
RT "The activity of Arabidopsis glycosyltransferases toward salicylic acid, 4-
RT hydroxybenzoic acid, and other benzoates.";
RL J. Biol. Chem. 277:586-592(2002).
RN [6]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12475971; DOI=10.1074/jbc.m211822200;
RA Quiel J.A., Bender J.;
RT "Glucose conjugation of anthranilate by the Arabidopsis UGT74F2
RT glucosyltransferase is required for tryptophan mutant blue fluorescence.";
RL J. Biol. Chem. 278:6275-6281(2003).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15352060; DOI=10.1002/bit.20154;
RA Lim E.K., Ashford D.A., Hou B., Jackson R.G., Bowles D.J.;
RT "Arabidopsis glycosyltransferases as biocatalysts in fermentation for
RT regioselective synthesis of diverse quercetin glucosides.";
RL Biotechnol. Bioeng. 87:623-631(2004).
RN [8]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18385129; DOI=10.1074/jbc.m709591200;
RA Eudes A., Bozzo G.G., Waller J.C., Naponelli V., Lim E.K., Bowles D.J.,
RA Gregory J.F. III, Hanson A.D.;
RT "Metabolism of the folate precursor p-aminobenzoate in plants: glucose
RT ester formation and vacuolar storage.";
RL J. Biol. Chem. 283:15451-15459(2008).
CC -!- FUNCTION: Possesses quercetin 7-O-glucosyltransferase and 4'-O-
CC glucosyltransferase activities in vitro. Also active in vitro on
CC benzoates and benzoate derivatives. Has low affinity for the tryptophan
CC precursor anthranilate. Catalyzes the formation of anthranilate glucose
CC ester. Is a minor source of this activity in the plant.
CC {ECO:0000269|PubMed:11641410, ECO:0000269|PubMed:12475971,
CC ECO:0000269|PubMed:15352060, ECO:0000269|PubMed:18385129}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 7-O-hydroxy-flavonol + UDP-alpha-D-glucose = a flavonol 7-O-
CC beta-D-glucoside + H(+) + UDP; Xref=Rhea:RHEA:23164,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:52144, ChEBI:CHEBI:52267,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.237;
CC Evidence={ECO:0000269|PubMed:15352060};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=810 uM for anthranilate {ECO:0000269|PubMed:12475971,
CC ECO:0000269|PubMed:18385129};
CC KM=850 uM for 4-aminobenzoate {ECO:0000269|PubMed:12475971,
CC ECO:0000269|PubMed:18385129};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O22820-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AC002333; AAB64022.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10333.1; -; Genomic_DNA.
DR EMBL; AK221589; BAD95102.1; -; mRNA.
DR PIR; B84871; B84871.
DR RefSeq; NP_181912.1; NM_129946.3. [O22820-1]
DR AlphaFoldDB; O22820; -.
DR SMR; O22820; -.
DR STRING; 3702.AT2G43840.1; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR iPTMnet; O22820; -.
DR PaxDb; O22820; -.
DR PRIDE; O22820; -.
DR ProteomicsDB; 228645; -. [O22820-1]
DR EnsemblPlants; AT2G43840.1; AT2G43840.1; AT2G43840. [O22820-1]
DR GeneID; 818988; -.
DR Gramene; AT2G43840.1; AT2G43840.1; AT2G43840. [O22820-1]
DR KEGG; ath:AT2G43840; -.
DR Araport; AT2G43840; -.
DR eggNOG; KOG1192; Eukaryota.
DR InParanoid; O22820; -.
DR PhylomeDB; O22820; -.
DR PRO; PR:O22820; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22820; baseline and differential.
DR Genevisible; O22820; AT.
DR GO; GO:0033836; F:flavonol 7-O-beta-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0080043; F:quercetin 3-O-glucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0080044; F:quercetin 7-O-glucosyltransferase activity; IBA:GO_Central.
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 Alternative splicing; Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..449
FT /note="Flavonol 7-O-beta-glucosyltransferase UGT74F1"
FT /id="PRO_0000409103"
FT BINDING 273
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 325..327
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 342..350
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 364..367
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
SQ SEQUENCE 449 AA; 50332 MW; CE3F8622946E4C78 CRC64;
MEKMRGHVLA VPFPSQGHIT PIRQFCKRLH SKGFKTTHTL TTFIFNTIHL DPSSPISIAT
ISDGYDQGGF SSAGSVPEYL QNFKTFGSKT VADIIRKHQS TDNPITCIVY DSFMPWALDL
AMDFGLAAAP FFTQSCAVNY INYLSYINNG SLTLPIKDLP LLELQDLPTF VTPTGSHLAY
FEMVLQQFTN FDKADFVLVN SFHDLDLHEE ELLSKVCPVL TIGPTVPSMY LDQQIKSDND
YDLNLFDLKE AALCTDWLDK RPEGSVVYIA FGSMAKLSSE QMEEIASAIS NFSYLWVVRA
SEESKLPPGF LETVDKDKSL VLKWSPQLQV LSNKAIGCFM THCGWNSTME GLSLGVPMVA
MPQWTDQPMN AKYIQDVWKV GVRVKAEKES GICKREEIEF SIKEVMEGEK SKEMKENAGK
WRDLAVKSLS EGGSTDININ EFVSKIQIK
