U73B4_ARATH
ID U73B4_ARATH Reviewed; 484 AA.
AC Q7Y232; Q3EBZ8; Q9ZQG3;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=UDP-glycosyltransferase 73B4;
DE EC=2.4.1.-;
DE AltName: Full=Flavonol 3-O-glucosyltransferase UGT73B4;
DE EC=2.4.1.91;
GN Name=UGT73B4; OrderedLocusNames=At2g15490; ORFNames=F9O13.4;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 [7]
RP FUNCTION.
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).
RN [8]
RP TISSUE SPECIFICITY, AND INDUCTION BY PATHOGEN AND SALICYLIC ACID.
RX PubMed=16306146; DOI=10.1104/pp.105.067223;
RA Langlois-Meurinne M., Gachon C.M., Saindrenan P.;
RT "Pathogen-responsive expression of glycosyltransferase genes UGT73B3 and
RT UGT73B5 is necessary for resistance to Pseudomonas syringae pv tomato in
RT Arabidopsis.";
RL Plant Physiol. 139:1890-1901(2005).
RN [9]
RP FUNCTION.
RX PubMed=18702669; DOI=10.1111/j.1365-313x.2008.03653.x;
RA Gandia-Herrero F., Lorenz A., Larson T., Graham I.A., Bowles D.J.,
RA Rylott E.L., Bruce N.C.;
RT "Detoxification of the explosive 2,4,6-trinitrotoluene in Arabidopsis:
RT discovery of bifunctional O- and C-glucosyltransferases.";
RL Plant J. 56:963-974(2008).
CC -!- FUNCTION: Possesses quercetin 3-O-glucosyltransferase and low 7-O-
CC glucosyltransferase activities in vitro. Also active in vitro on
CC benzoates and benzoate derivatives. Can detoxify the explosive 2,4,6-
CC trinitrotoluene in plant by forming O- or C-glucose conjugates.
CC {ECO:0000269|PubMed:11641410, ECO:0000269|PubMed:15352060,
CC ECO:0000269|PubMed:18702669}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7Y232-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Y232-2; Sequence=VSP_041227;
CC -!- TISSUE SPECIFICITY: Specifically expressed in roots.
CC {ECO:0000269|PubMed:16306146}.
CC -!- INDUCTION: Induced by pathogen infection and salicylic acid.
CC {ECO:0000269|PubMed:16306146}.
CC -!- MISCELLANEOUS: Plants overexpressing UGT73B4 show enhanced root growth
CC in seedlings grown in presence of 2,4,6-trinitrotoluene.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD17393.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC006248; AAD17393.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002685; AEC06407.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06408.1; -; Genomic_DNA.
DR EMBL; BT008319; AAP37678.1; -; mRNA.
DR EMBL; AK227684; BAE99671.1; -; mRNA.
DR PIR; F84529; F84529.
DR RefSeq; NP_179151.2; NM_127109.3. [Q7Y232-1]
DR RefSeq; NP_973469.1; NM_201740.1. [Q7Y232-2]
DR AlphaFoldDB; Q7Y232; -.
DR SMR; Q7Y232; -.
DR STRING; 3702.AT2G15490.1; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR iPTMnet; Q7Y232; -.
DR PaxDb; Q7Y232; -.
DR PRIDE; Q7Y232; -.
DR ProteomicsDB; 228671; -. [Q7Y232-1]
DR EnsemblPlants; AT2G15490.1; AT2G15490.1; AT2G15490. [Q7Y232-1]
DR EnsemblPlants; AT2G15490.2; AT2G15490.2; AT2G15490. [Q7Y232-2]
DR GeneID; 816041; -.
DR Gramene; AT2G15490.1; AT2G15490.1; AT2G15490. [Q7Y232-1]
DR Gramene; AT2G15490.2; AT2G15490.2; AT2G15490. [Q7Y232-2]
DR KEGG; ath:AT2G15490; -.
DR Araport; AT2G15490; -.
DR TAIR; locus:2053669; AT2G15490.
DR eggNOG; KOG1192; Eukaryota.
DR InParanoid; Q7Y232; -.
DR OMA; DADQRSY; -.
DR PhylomeDB; Q7Y232; -.
DR PRO; PR:Q7Y232; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q7Y232; baseline and differential.
DR Genevisible; Q7Y232; 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: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 GO; GO:0051707; P:response to other organism; IEP:TAIR.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR CDD; cd03784; GT1_Gtf-like; 1.
DR InterPro; IPR002213; UDP_glucos_trans.
DR InterPro; IPR035595; UDP_glycos_trans_CS.
DR Pfam; PF00201; UDPGT; 1.
DR PROSITE; PS00375; UDPGT; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Detoxification; Glycosyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..484
FT /note="UDP-glycosyltransferase 73B4"
FT /id="PRO_0000409079"
FT BINDING 294
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 356..358
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 373..381
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 395..398
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT VAR_SEQ 189..402
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041227"
SQ SEQUENCE 484 AA; 53961 MW; 41C07469E63747D7 CRC64;
MNREQIHILF FPFMAHGHMI PLLDMAKLFA RRGAKSTLLT TPINAKILEK PIEAFKVQNP
DLEIGIKILN FPCVELGLPE GCENRDFINS YQKSDSFDLF LKFLFSTKYM KQQLESFIET
TKPSALVADM FFPWATESAE KIGVPRLVFH GTSSFALCCS YNMRIHKPHK KVASSSTPFV
IPGLPGDIVI TEDQANVTNE ETPFGKFWKE VRESETSSFG VLVNSFYELE SSYADFYRSF
VAKKAWHIGP LSLSNRGIAE KAGRGKKANI DEQECLKWLD SKTPGSVVYL SFGSGTGLPN
EQLLEIAFGL EGSGQNFIWV VSKNENQVGT GENEDWLPKG FEERNKGKGL IIRGWAPQVL
ILDHKAIGGF VTHCGWNSTL EGIAAGLPMV TWPMGAEQFY NEKLLTKVLR IGVNVGATEL
VKKGKLISRA QVEKAVREVI GGEKAEERRL RAKELGEMAK AAVEEGGSSY NDVNKFMEEL
NGRK
