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   24-JAN-2024, entry version 115.
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};
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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.Q9C9B0; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   PaxDb; 3702-AT1G73880-1; -.
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; AT1G73880; UGT89B1.
DR   eggNOG; KOG1192; Eukaryota.
DR   HOGENOM; CLU_001724_2_2_1; -.
DR   InParanoid; Q9C9B0; -.
DR   OMA; NSPKYPW; -.
DR   OrthoDB; 1068116at2759; -.
DR   PRO; PR:Q9C9B0; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9C9B0; 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: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   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   PANTHER; PTHR48047:SF8; FLAVONOL 3-O-GLUCOSYLTRANSFERASE UGT89B1; 1.
DR   PANTHER; PTHR48047; GLYCOSYLTRANSFERASE; 1.
DR   Pfam; PF00201; UDPGT; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR   Genevisible; Q9C9B0; AT.
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   ACT_SITE        25
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         25
FT                   /ligand="an anthocyanidin"
FT                   /ligand_id="ChEBI:CHEBI:143576"
FT                   /evidence="ECO:0000250|UniProtKB:P51094"
FT   BINDING         348
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         365
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         368
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         369
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         373
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         388
FT                   /ligand="an anthocyanidin"
FT                   /ligand_id="ChEBI:CHEBI:143576"
FT                   /evidence="ECO:0000250|UniProtKB:P51094"
FT   BINDING         389
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         390
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
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
//