GenomeNet

Database: UniProt
Entry: U71C4_ARATH
LinkDB: U71C4_ARATH
Original site: 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   27-MAR-2024, entry version 132.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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.Q9LML6; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   iPTMnet; Q9LML6; -.
DR   MetOSite; Q9LML6; -.
DR   PaxDb; 3702-AT1G07250-1; -.
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; AT1G07250; UGT71C4.
DR   eggNOG; KOG1192; Eukaryota.
DR   HOGENOM; CLU_001724_3_2_1; -.
DR   InParanoid; Q9LML6; -.
DR   OMA; QTHECVR; -.
DR   OrthoDB; 1050337at2759; -.
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   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   InterPro; IPR035595; UDP_glycos_trans_CS.
DR   PANTHER; PTHR48048; GLYCOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR48048:SF58; GLYCOSYLTRANSFERASE; 1.
DR   Pfam; PF00201; UDPGT; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 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   ACT_SITE        17
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   ACT_SITE        127
FT                   /note="Charge relay"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         17
FT                   /ligand="an anthocyanidin"
FT                   /ligand_id="ChEBI:CHEBI:143576"
FT                   /evidence="ECO:0000250|UniProtKB:P51094"
FT   BINDING         150
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         350
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         352
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         367
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         370
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         371
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         372
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         375
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         390
FT                   /ligand="an anthocyanidin"
FT                   /ligand_id="ChEBI:CHEBI:143576"
FT                   /evidence="ECO:0000250|UniProtKB:P51094"
FT   BINDING         391
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         392
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
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
//
DBGET integrated database retrieval system