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 27-MAR-2024, entry version 133. 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}; 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; 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.Q94AB5; -. DR CAZy; GT1; Glycosyltransferase Family 1. DR iPTMnet; Q94AB5; -. DR PaxDb; 3702-AT3G46660-1; -. 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; AT3G46660; UGT76E12. DR eggNOG; KOG1192; Eukaryota. DR HOGENOM; CLU_001724_0_0_1; -. DR InParanoid; Q94AB5; -. DR OMA; ICSSDWI; -. DR OrthoDB; 1208604at2759; -. DR PhylomeDB; Q94AB5; -. DR PRO; PR:Q94AB5; -. DR Proteomes; UP000006548; Chromosome 3. DR ExpressionAtlas; Q94AB5; baseline and differential. 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 Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2. DR InterPro; IPR002213; UDP_glucos_trans. DR PANTHER; PTHR48045:SF25; UDP-GLUCURONOSYL_UDP-GLUCOSYLTRANSFERASE-RELATED; 1. DR PANTHER; PTHR48045; UDP-GLYCOSYLTRANSFERASE 72B1; 1. DR Pfam; PF00201; UDPGT; 1. DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1. DR Genevisible; Q94AB5; AT. 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 ACT_SITE 25 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03" FT ACT_SITE 118 FT /note="Charge relay" FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03" FT BINDING 25 FT /ligand="an anthocyanidin" FT /ligand_id="ChEBI:CHEBI:143576" FT /evidence="ECO:0000250|UniProtKB:P51094" FT BINDING 140 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03" FT BINDING 339 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03" FT BINDING 341 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03" FT BINDING 356 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03" FT BINDING 359 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03" FT BINDING 360 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03" FT BINDING 361 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03" FT BINDING 364 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03" FT BINDING 379 FT /ligand="an anthocyanidin" FT /ligand_id="ChEBI:CHEBI:143576" FT /evidence="ECO:0000250|UniProtKB:P51094" FT BINDING 380 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03" FT BINDING 381 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03" 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 //