U71C4_ARATH
ID U71C4_ARATH Reviewed; 479 AA.
AC Q9LML6; Q94BM9;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Flavonol 3-O-glucosyltransferase UGT71C4 {ECO:0000305};
DE EC=2.4.1.91 {ECO:0000269|PubMed:15352060};
DE AltName: Full=Flavonol 7-O-beta-glucosyltransferase UGT71C4 {ECO:0000305};
DE EC=2.4.1.237 {ECO:0000269|PubMed:15352060};
DE AltName: Full=UDP-glycosyltransferase 71C4 {ECO:0000303|PubMed:11042215};
GN Name=UGT71C4 {ECO:0000303|PubMed:11042215};
GN OrderedLocusNames=At1g07250 {ECO:0000312|Araport:AT1G07250};
GN ORFNames=F10K1.4 {ECO:0000312|EMBL:AAG18592.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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 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).
CC -!- FUNCTION: Possesses quercetin 3-O-glucosyltransferase and 7-O-
CC glucosyltransferase activities in vitro. Also active in vitro on
CC benzoates and benzoate derivatives. {ECO:0000269|PubMed:11641410,
CC ECO:0000269|PubMed:15352060}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a flavonol + UDP-alpha-D-glucose = a flavonol 3-O-beta-D-
CC glucoside + H(+) + UDP; Xref=Rhea:RHEA:22300, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16816, ChEBI:CHEBI:28802, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885; EC=2.4.1.91;
CC Evidence={ECO:0000269|PubMed:15352060};
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 -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AC067971; AAG18592.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28097.1; -; Genomic_DNA.
DR EMBL; AY040019; AAK64176.2; -; mRNA.
DR EMBL; BT001938; AAN71937.1; -; mRNA.
DR PIR; G86207; G86207.
DR RefSeq; NP_563784.2; NM_100599.4.
DR AlphaFoldDB; Q9LML6; -.
DR SMR; Q9LML6; -.
DR STRING; 3702.AT1G07250.1; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR iPTMnet; Q9LML6; -.
DR MetOSite; Q9LML6; -.
DR PaxDb; Q9LML6; -.
DR PRIDE; Q9LML6; -.
DR ProteomicsDB; 228586; -.
DR DNASU; 837236; -.
DR EnsemblPlants; AT1G07250.1; AT1G07250.1; AT1G07250.
DR GeneID; 837236; -.
DR Gramene; AT1G07250.1; AT1G07250.1; AT1G07250.
DR KEGG; ath:AT1G07250; -.
DR Araport; AT1G07250; -.
DR TAIR; locus:2007462; AT1G07250.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_001724_3_2_1; -.
DR InParanoid; Q9LML6; -.
DR OMA; MPSNVGF; -.
DR OrthoDB; 508327at2759; -.
DR PhylomeDB; Q9LML6; -.
DR PRO; PR:Q9LML6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LML6; baseline and differential.
DR Genevisible; Q9LML6; AT.
DR GO; GO:0102360; F:daphnetin 3-O-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0047893; F:flavonol 3-O-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0033836; F:flavonol 7-O-beta-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0102425; F:myricetin 3-O-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0080043; F:quercetin 3-O-glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0080044; F:quercetin 7-O-glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0035251; F:UDP-glucosyltransferase activity; IDA:TAIR.
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; Reference proteome; Transferase.
FT CHAIN 1..479
FT /note="Flavonol 3-O-glucosyltransferase UGT71C4"
FT /id="PRO_0000409056"
FT BINDING 291
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 350..352
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 367..375
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 389..392
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
SQ SEQUENCE 479 AA; 52844 MW; BEAFE2D5C86F8920 CRC64;
MVKETELIFI PVPSTGHILV HIEFAKRLIN LDHRIHTITI LNLSSPSSPH ASVFARSLIA
SQPKIRLHDL PPIQDPPPFD LYQRAPEAYI VKLIKKNTPL IKDAVSSIVA SRRGGSDSVQ
VAGLVLDLFC NSLVKDVGNE LNLPSYIYLT CNARYLGMMK YIPDRHRKIA SEFDLSSGDE
ELPVPGFINA IPTKFMPPGL FNKEAYEAYV ELAPRFADAK GILVNSFTEL EPHPFDYFSH
LEKFPPVYPV GPILSLKDRA SPNEEAVDRD QIVGWLDDQP ESSVVFLCFG SRGSVDEPQV
KEIARALELV GCRFLWSIRT SGDVETNPND VLPEGFMGRV AGRGLVCGWA PQVEVLAHKA
IGGFVSHCGW NSTLESLWFG VPVATWPMYA EQQLNAFTLV KELGLAVDLR MDYVSSRGGL
VTCDEIARAV RSLMDGGDEK RKKVKEMADA ARKALMDGGS SSLATARFIA ELFEDGSSC
