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   27-MAR-2024, entry version 124.
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.Q9ZQG4; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   iPTMnet; Q9ZQG4; -.
DR   PaxDb; 3702-AT2G15480-2; -.
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; AT2G15480; UGT73B5.
DR   eggNOG; KOG1192; Eukaryota.
DR   InParanoid; Q9ZQG4; -.
DR   OMA; DADQRSY; -.
DR   PhylomeDB; Q9ZQG4; -.
DR   BioCyc; ARA:AT2G15480-MONOMER; -.
DR   PRO; PR:Q9ZQG4; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9ZQG4; 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: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   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   InterPro; IPR035595; UDP_glycos_trans_CS.
DR   PANTHER; PTHR48047; GLYCOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR48047:SF45; GLYCOSYLTRANSFERASE; 1.
DR   Pfam; PF00201; UDPGT; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR   PROSITE; PS00375; UDPGT; 1.
DR   Genevisible; Q9ZQG4; AT.
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   ACT_SITE        21
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   ACT_SITE        132
FT                   /note="Charge relay"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         21
FT                   /ligand="an anthocyanidin"
FT                   /ligand_id="ChEBI:CHEBI:143576"
FT                   /evidence="ECO:0000250|UniProtKB:P51094"
FT   BINDING         92
FT                   /ligand="an anthocyanidin"
FT                   /ligand_id="ChEBI:CHEBI:143576"
FT                   /evidence="ECO:0000250|UniProtKB:P51094"
FT   BINDING         356
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         358
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         376
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         377
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         378
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"
FT   BINDING         396
FT                   /ligand="an anthocyanidin"
FT                   /ligand_id="ChEBI:CHEBI:143576"
FT                   /evidence="ECO:0000250|UniProtKB:P51094"
FT   BINDING         397
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         398
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
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
//