U89B1_ARATH
ID U89B1_ARATH Reviewed; 473 AA.
AC Q9C9B0; Q8RWP1;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Flavonol 3-O-glucosyltransferase UGT89B1 {ECO:0000305};
DE EC=2.4.1.91 {ECO:0000269|PubMed:15352060};
DE AltName: Full=Flavonol 7-O-beta-glucosyltransferase UGT89B1 {ECO:0000305};
DE EC=2.4.1.237 {ECO:0000269|PubMed:15352060};
DE AltName: Full=UDP-glycosyltransferase 89B1 {ECO:0000303|PubMed:11042215};
GN Name=UGT89B1 {ECO:0000303|PubMed:11042215};
GN OrderedLocusNames=At1g73880 {ECO:0000312|Araport:AT1G73880};
GN ORFNames=F2P9.25 {ECO:0000312|EMBL:AAG52529.1};
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, 7-O-
CC glucosyltransferase and 4'-O-glucosyltransferase activities in vitro.
CC Also active in vitro on benzoates and benzoate derivatives.
CC {ECO:0000269|PubMed:11641410, 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=AAG52529.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAM12962.1; Type=Frameshift; 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; AC016662; AAG52529.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35520.1; -; Genomic_DNA.
DR EMBL; AY092963; AAM12962.1; ALT_FRAME; mRNA.
DR EMBL; BT006596; AAP31940.1; -; mRNA.
DR PIR; D96766; D96766.
DR RefSeq; NP_177529.2; NM_106048.4.
DR AlphaFoldDB; Q9C9B0; -.
DR SMR; Q9C9B0; -.
DR STRING; 3702.AT1G73880.1; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR PaxDb; Q9C9B0; -.
DR PRIDE; Q9C9B0; -.
DR ProteomicsDB; 243237; -.
DR EnsemblPlants; AT1G73880.1; AT1G73880.1; AT1G73880.
DR GeneID; 843725; -.
DR Gramene; AT1G73880.1; AT1G73880.1; AT1G73880.
DR KEGG; ath:AT1G73880; -.
DR Araport; AT1G73880; -.
DR TAIR; locus:2031566; AT1G73880.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_001724_2_2_1; -.
DR InParanoid; Q9C9B0; -.
DR OMA; WCKAQRR; -.
DR OrthoDB; 508327at2759; -.
DR PRO; PR:Q9C9B0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C9B0; baseline and differential.
DR Genevisible; Q9C9B0; 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:0080046; F:quercetin 4'-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 Pfam; PF00201; UDPGT; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..473
FT /note="Flavonol 3-O-glucosyltransferase UGT89B1"
FT /id="PRO_0000409137"
FT BINDING 289
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 348..350
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 365..373
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 387..390
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
SQ SEQUENCE 473 AA; 52106 MW; 293587240C506F6A CRC64;
MKVNEENNKP TKTHVLIFPF PAQGHMIPLL DFTHRLALRG GAALKITVLV TPKNLPFLSP
LLSAVVNIEP LILPFPSHPS IPSGVENVQD LPPSGFPLMI HALGNLHAPL ISWITSHPSP
PVAIVSDFFL GWTKNLGIPR FDFSPSAAIT CCILNTLWIE MPTKINEDDD NEILHFPKIP
NCPKYRFDQI SSLYRSYVHG DPAWEFIRDS FRDNVASWGL VVNSFTAMEG VYLEHLKREM
GHDRVWAVGP IIPLSGDNRG GPTSVSVDHV MSWLDAREDN HVVYVCFGSQ VVLTKEQTLA
LASGLEKSGV HFIWAVKEPV EKDSTRGNIL DGFDDRVAGR GLVIRGWAPQ VAVLRHRAVG
AFLTHCGWNS VVEAVVAGVL MLTWPMRADQ YTDASLVVDE LKVGVRACEG PDTVPDPDEL
ARVFADSVTG NQTERIKAVE LRKAALDAIQ ERGSSVNDLD GFIQHVVSLG LNK
