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U7E12_ARATH
ID   U7E12_ARATH             Reviewed;         458 AA.
AC   Q94AB5; Q9SNB2;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Flavonol 3-O-glucosyltransferase UGT76E12 {ECO:0000305};
DE            EC=2.4.1.91 {ECO:0000269|PubMed:15352060};
DE   AltName: Full=Flavonol 7-O-beta-glucosyltransferase UGT76E12 {ECO:0000305};
DE            EC=2.4.1.237 {ECO:0000269|PubMed:15352060};
DE   AltName: Full=UDP-glycosyltransferase 76E12 {ECO:0000303|PubMed:11042215};
GN   Name=UGT76E12 {ECO:0000303|PubMed:11042215};
GN   OrderedLocusNames=At3g46660 {ECO:0000312|Araport:AT3G46660};
GN   ORFNames=F12A12.180 {ECO:0000312|EMBL:CAB62336.1};
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=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(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, 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. {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   -!- SEQUENCE CAUTION:
CC       Sequence=CAB62336.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AL133314; CAB62336.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP002686; AEE78190.1; -; Genomic_DNA.
DR   EMBL; AY048297; AAK82559.1; -; mRNA.
DR   EMBL; AY120731; AAM53289.1; -; mRNA.
DR   EMBL; BT000356; AAN15675.1; -; mRNA.
DR   EMBL; BT002638; AAO11554.1; -; mRNA.
DR   PIR; T45603; T45603.
DR   RefSeq; NP_566885.1; NM_114533.2.
DR   AlphaFoldDB; Q94AB5; -.
DR   SMR; Q94AB5; -.
DR   STRING; 3702.AT3G46660.1; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   iPTMnet; Q94AB5; -.
DR   PaxDb; Q94AB5; -.
DR   PRIDE; Q94AB5; -.
DR   ProteomicsDB; 228677; -.
DR   EnsemblPlants; AT3G46660.1; AT3G46660.1; AT3G46660.
DR   GeneID; 823819; -.
DR   Gramene; AT3G46660.1; AT3G46660.1; AT3G46660.
DR   KEGG; ath:AT3G46660; -.
DR   Araport; AT3G46660; -.
DR   TAIR; locus:2075215; AT3G46660.
DR   eggNOG; KOG1192; Eukaryota.
DR   HOGENOM; CLU_001724_0_0_1; -.
DR   InParanoid; Q94AB5; -.
DR   OMA; NSTRECL; -.
DR   OrthoDB; 508327at2759; -.
DR   PhylomeDB; Q94AB5; -.
DR   PRO; PR:Q94AB5; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q94AB5; baseline and differential.
DR   Genevisible; Q94AB5; 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   CDD; cd03784; GT1_Gtf-like; 1.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   Pfam; PF00201; UDPGT; 1.
PE   1: Evidence at protein level;
KW   Glycosyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..458
FT                   /note="Flavonol 3-O-glucosyltransferase UGT76E12"
FT                   /id="PRO_0000409095"
FT   BINDING         280
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         339..341
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         356..364
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         378..381
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   458 AA;  51662 MW;  064AC578C026B098 CRC64;
     MQVLGMEEKP ARRSVVLVPF PAQGHISPMM QLAKTLHLKG FSITVVQTKF NYFSPSDDFT
     HDFQFVTIPE SLPESDFKNL GPIQFLFKLN KECKVSFKDC LGQLVLQQSN EISCVIYDEF
     MYFAEAAAKE CKLPNIIFST TSATAFACRS VFDKLYANNV QAPLKETKGQ QEELVPEFYP
     LRYKDFPVSR FASLESIMEV YRNTVDKRTA SSVIINTASC LESSSLSFLQ QQQLQIPVYP
     IGPLHMVASA PTSLLEENKS CIEWLNKQKV NSVIYISMGS IALMEINEIM EVASGLAASN
     QHFLWVIRPG SIPGSEWIES MPEEFSKMVL DRGYIVKWAP QKEVLSHPAV GGFWSHCGWN
     STLESIGQGV PMICRPFSGD QKVNARYLEC VWKIGIQVEG ELDRGVVERA VKRLMVDEEG
     EEMRKRAFSL KEQLRASVKS GGSSHNSLEE FVHFIRTL
 
 
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