U73B5_ARATH
ID U73B5_ARATH Reviewed; 484 AA.
AC Q9ZQG4; Q8L7Q5;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=UDP-glycosyltransferase 73B5;
DE EC=2.4.1.-;
DE AltName: Full=Flavonol 3-O-glucosyltransferase UGT73B5;
DE EC=2.4.1.91;
GN Name=UGT73B5; OrderedLocusNames=At2g15480; ORFNames=F9O13.3;
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] OF 35-484.
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] OF 113-484.
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2004) 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=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 [7]
RP FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND INDUCTION BY
RP 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).
CC -!- FUNCTION: Possesses quercetin 3-O-glucosyltransferase activity in
CC vitro. Involved in stress or defense responses.
CC {ECO:0000269|PubMed:15352060, ECO:0000269|PubMed:16306146}.
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=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9ZQG4-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots and senescent leaves.
CC {ECO:0000269|PubMed:16306146}.
CC -!- INDUCTION: Induced by pathogen infection, H(2)O(2) and salicylic acid.
CC {ECO:0000269|PubMed:16306146}.
CC -!- DISRUPTION PHENOTYPE: Decreased resistance to avirulent strains of
CC P.syringae. {ECO:0000269|PubMed:16306146}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM91525.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC006248; AAD17392.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06405.1; -; Genomic_DNA.
DR EMBL; AY128322; AAM91525.1; ALT_INIT; mRNA.
DR EMBL; BT015865; AAU94428.1; -; mRNA.
DR PIR; E84529; E84529.
DR RefSeq; NP_179150.3; NM_127108.4. [Q9ZQG4-1]
DR AlphaFoldDB; Q9ZQG4; -.
DR SMR; Q9ZQG4; -.
DR STRING; 3702.AT2G15480.2; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR iPTMnet; Q9ZQG4; -.
DR PaxDb; Q9ZQG4; -.
DR PRIDE; Q9ZQG4; -.
DR ProteomicsDB; 228639; -. [Q9ZQG4-1]
DR EnsemblPlants; AT2G15480.1; AT2G15480.1; AT2G15480. [Q9ZQG4-1]
DR GeneID; 816040; -.
DR Gramene; AT2G15480.1; AT2G15480.1; AT2G15480. [Q9ZQG4-1]
DR KEGG; ath:AT2G15480; -.
DR Araport; AT2G15480; -.
DR TAIR; locus:2053618; AT2G15480.
DR eggNOG; KOG1192; Eukaryota.
DR InParanoid; Q9ZQG4; -.
DR OMA; RNSAEWM; -.
DR PhylomeDB; Q9ZQG4; -.
DR BioCyc; ARA:AT2G15480-MON; -.
DR PRO; PR:Q9ZQG4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZQG4; baseline and differential.
DR Genevisible; Q9ZQG4; 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:0035251; F:UDP-glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0051707; P:response to other organism; IMP:TAIR.
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; Glycosyltransferase; Plant defense;
KW Reference proteome; Transferase.
FT CHAIN 1..484
FT /note="UDP-glycosyltransferase 73B5"
FT /id="PRO_0000409080"
FT BINDING 297
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"
SQ SEQUENCE 484 AA; 54184 MW; B94342034C3394A6 CRC64;
MNREVSERIH ILFFPFMAQG HMIPILDMAK LFSRRGAKST LLTTPINAKI FEKPIEAFKN
QNPDLEIGIK IFNFPCVELG LPEGCENADF INSYQKSDSG DLFLKFLFST KYMKQQLESF
IETTKPSALV ADMFFPWATE SAEKLGVPRL VFHGTSFFSL CCSYNMRIHK PHKKVATSST
PFVIPGLPGD IVITEDQANV AKEETPMGKF MKEVRESETN SFGVLVNSFY ELESAYADFY
RSFVAKRAWH IGPLSLSNRE LGEKARRGKK ANIDEQECLK WLDSKTPGSV VYLSFGSGTN
FTNDQLLEIA FGLEGSGQSF IWVVRKNENQ GDNEEWLPEG FKERTTGKGL IIPGWAPQVL
ILDHKAIGGF VTHCGWNSAI EGIAAGLPMV TWPMGAEQFY NEKLLTKVLR IGVNVGATEL
VKKGKLISRA QVEKAVREVI GGEKAEERRL WAKKLGEMAK AAVEEGGSSY NDVNKFMEEL
NGRK
