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   24-JAN-2024, entry version 119.
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   IntAct; Q7Y232; 1.
DR   STRING; 3702.Q7Y232; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   iPTMnet; Q7Y232; -.
DR   PaxDb; 3702-AT2G15490-1; -.
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; AT2G15490; UGT73B4.
DR   eggNOG; KOG1192; Eukaryota.
DR   InParanoid; Q7Y232; -.
DR   OMA; RSQMMEP; -.
DR   OrthoDB; 1208220at2759; -.
DR   PhylomeDB; Q7Y232; -.
DR   PRO; PR:Q7Y232; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q7Y232; 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: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   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; Q7Y232; AT.
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   ACT_SITE        18
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   ACT_SITE        129
FT                   /note="Charge relay"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT   BINDING         18
FT                   /ligand="an anthocyanidin"
FT                   /ligand_id="ChEBI:CHEBI:143576"
FT                   /evidence="ECO:0000250|UniProtKB:P51094"
FT   BINDING         89
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"
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
//