U71C1_ARATH
ID U71C1_ARATH Reviewed; 481 AA.
AC O82381;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Flavonol 3-O-glucosyltransferase UGT71C1 {ECO:0000305};
DE EC=2.4.1.91 {ECO:0000269|PubMed:15352060};
DE AltName: Full=Flavonol 7-O-beta-glucosyltransferase UGT71C1 {ECO:0000305};
DE EC=2.4.1.237 {ECO:0000269|PubMed:15352060};
DE AltName: Full=UDP-glycosyltransferase 71C1 {ECO:0000303|PubMed:11042215};
GN Name=UGT71C1 {ECO:0000303|PubMed:11042215};
GN OrderedLocusNames=At2g29750 {ECO:0000312|Araport:AT2G29750};
GN ORFNames=T27A16.15 {ECO:0000312|EMBL:AAC35226.1};
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].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF Clones.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 [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=19261311; DOI=10.1016/j.phytochem.2009.01.013;
RA Hansen E.H., Osmani S.A., Kristensen C., Moeller B.L., Hansen J.;
RT "Substrate specificities of family 1 UGTs gained by domain swapping.";
RL Phytochemistry 70:473-482(2009).
CC -!- FUNCTION: Possesses quercetin 7-O-glucosyltransferase and 3'-O-
CC glucosyltransferase activities in vitro. Also active in vitro on
CC benzoates and benzoate derivatives. Glucosylates other secondary
CC metabolites in vitro like trans-resveratrol, curcumin, vanillin and
CC etoposide. {ECO:0000269|PubMed:11641410, ECO:0000269|PubMed:15352060,
CC ECO:0000269|PubMed:19261311}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.15 mM for curcumin {ECO:0000269|PubMed:19261311};
CC KM=0.5 mM for trans-resveratrol {ECO:0000269|PubMed:19261311};
CC KM=1.12 mM for vanillin {ECO:0000269|PubMed:19261311};
CC KM=2.7 mM for etoposide {ECO:0000269|PubMed:19261311};
CC Vmax=1.2 umol/min/mg enzyme towards vanillin
CC {ECO:0000269|PubMed:19261311};
CC Vmax=0.063 umol/min/mg enzyme towards trans-resveratrol
CC {ECO:0000269|PubMed:19261311};
CC Vmax=0.022 umol/min/mg enzyme towards curcumin
CC {ECO:0000269|PubMed:19261311};
CC Vmax=0.013 umol/min/mg enzyme towards etoposide
CC {ECO:0000269|PubMed:19261311};
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AC005496; AAC35226.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08300.1; -; Genomic_DNA.
DR EMBL; BT023426; AAY56417.1; -; mRNA.
DR EMBL; BT026458; ABH04565.1; -; mRNA.
DR PIR; B84700; B84700.
DR RefSeq; NP_180536.1; NM_128529.3.
DR AlphaFoldDB; O82381; -.
DR SMR; O82381; -.
DR STRING; 3702.AT2G29750.1; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR PaxDb; O82381; -.
DR PRIDE; O82381; -.
DR ProteomicsDB; 228536; -.
DR EnsemblPlants; AT2G29750.1; AT2G29750.1; AT2G29750.
DR GeneID; 817525; -.
DR Gramene; AT2G29750.1; AT2G29750.1; AT2G29750.
DR KEGG; ath:AT2G29750; -.
DR Araport; AT2G29750; -.
DR TAIR; locus:2060654; AT2G29750.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_001724_3_2_1; -.
DR InParanoid; O82381; -.
DR OMA; QNDASNM; -.
DR OrthoDB; 508327at2759; -.
DR PhylomeDB; O82381; -.
DR BRENDA; 2.4.1.128; 399.
DR SABIO-RK; O82381; -.
DR PRO; PR:O82381; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O82381; baseline and differential.
DR Genevisible; O82381; 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:0080045; 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..481
FT /note="Flavonol 3-O-glucosyltransferase UGT71C1"
FT /id="PRO_0000409053"
FT BINDING 293
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 352..354
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 369..377
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 391..394
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
SQ SEQUENCE 481 AA; 53875 MW; 21283D9B69C4C97C CRC64;
MGKQEDAELV IIPFPFSGHI LATIELAKRL ISQDNPRIHT ITILYWGLPF IPQADTIAFL
RSLVKNEPRI RLVTLPEVQD PPPMELFVEF AESYILEYVK KMVPIIREAL STLLSSRDES
GSVRVAGLVL DFFCVPMIDV GNEFNLPSYI FLTCSAGFLG MMKYLPERHR EIKSEFNRSF
NEELNLIPGY VNSVPTKVLP SGLFMKETYE PWVELAERFP EAKGILVNSY TALEPNGFKY
FDRCPDNYPT IYPIGPILCS NDRPNLDSSE RDRIITWLDD QPESSVVFLC FGSLKNLSAT
QINEIAQALE IVDCKFIWSF RTNPKEYASP YEALPHGFMD RVMDQGIVCG WAPQVEILAH
KAVGGFVSHC GWNSILESLG FGVPIATWPM YAEQQLNAFT MVKELGLALE MRLDYVSEDG
DIVKADEIAG TVRSLMDGVD VPKSKVKEIA EAGKEAVDGG SSFLAVKRFI GDLIDGVSIS
K
