U75B2_ARATH
ID U75B2_ARATH Reviewed; 455 AA.
AC Q9ZVY5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=UDP-glycosyltransferase 75B2;
DE EC=2.4.1.-;
DE AltName: Full=(Uridine 5'-diphosphate-glucose:indol-3-ylacetyl)-beta-D-glucosyl transferase 2;
DE AltName: Full=IAA-Glu synthase 2;
DE AltName: Full=Indole-3-acetate beta-glucosyltransferase 2;
DE EC=2.4.1.121;
GN Name=UGT75B2; Synonyms=UGT2; OrderedLocusNames=At1g05530;
GN ORFNames=T25N20.18;
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 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 [4]
RP FUNCTION.
RX PubMed=11042207; DOI=10.1074/jbc.m006185200;
RA Jackson R.G., Lim E.-K., Li Y., Kowalczyk M., Sandberg G., Hoggett J.,
RA Ashford D.A., Bowles D.J.;
RT "Identification and biochemical characterization of an Arabidopsis indole-
RT 3-acetic acid glucosyltransferase.";
RL J. Biol. Chem. 276:4350-4356(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).
CC -!- FUNCTION: Possesses low catalytic activity in vitro. Also active as
CC glucosyltransferase in vitro on benzoates and benzoate derivatives.
CC {ECO:0000269|PubMed:11042207, ECO:0000269|PubMed:11641410}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(indol-3-yl)acetate + UDP-alpha-D-glucose = 1-O-(indol-3-
CC ylacetyl)-beta-D-glucose + UDP; Xref=Rhea:RHEA:14921,
CC ChEBI:CHEBI:17990, ChEBI:CHEBI:30854, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885; EC=2.4.1.121;
CC -!- PATHWAY: Plant hormone metabolism; auxin conjugation.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AC005106; AAF79732.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27849.1; -; Genomic_DNA.
DR RefSeq; NP_172044.1; NM_100432.2.
DR AlphaFoldDB; Q9ZVY5; -.
DR SMR; Q9ZVY5; -.
DR STRING; 3702.AT1G05530.1; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR PaxDb; Q9ZVY5; -.
DR PRIDE; Q9ZVY5; -.
DR ProteomicsDB; 242810; -.
DR EnsemblPlants; AT1G05530.1; AT1G05530.1; AT1G05530.
DR GeneID; 837055; -.
DR Gramene; AT1G05530.1; AT1G05530.1; AT1G05530.
DR KEGG; ath:AT1G05530; -.
DR Araport; AT1G05530; -.
DR TAIR; locus:2201066; AT1G05530.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_001724_0_1_1; -.
DR InParanoid; Q9ZVY5; -.
DR OMA; LWIQPAF; -.
DR OrthoDB; 508327at2759; -.
DR PhylomeDB; Q9ZVY5; -.
DR BioCyc; ARA:AT1G05530-MON; -.
DR BioCyc; MetaCyc:AT1G05530-MON; -.
DR UniPathway; UPA00376; -.
DR PRO; PR:Q9ZVY5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9ZVY5; baseline and differential.
DR Genevisible; Q9ZVY5; AT.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0047215; F:indole-3-acetate beta-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0080043; F:quercetin 3-O-glucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0080044; F:quercetin 7-O-glucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0035251; F:UDP-glucosyltransferase activity; IDA: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 Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..455
FT /note="UDP-glycosyltransferase 75B2"
FT /id="PRO_0000334598"
FT BINDING 270
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 335..337
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 352..360
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 374..377
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
SQ SEQUENCE 455 AA; 51190 MW; CFCFA2B93EA3F547 CRC64;
MAQPHFLLVT FPAQGHVNPS LRFARRLIKT TGARVTFATC LSVIHRSMIP NHNNVENLSF
LTFSDGFDDG VISNTDDVQN RLVHFERNGD KALSDFIEAN QNGDSPVSCL IYTILPNWVP
KVARRFHLPS VHLWIQPAFA FDIYYNYSTG NNSVFEFPNL PSLEIRDLPS FLSPSNTNKA
AQAVYQELMD FLKEESNPKI LVNTFDSLEP EFLTAIPNIE MVAVGPLLPA EIFTGSESGK
DLSRDHQSSS YTLWLDSKTE SSVIYVSFGT MVELSKKQIE ELARALIEGG RPFLWVITDK
LNREAKIEGE EETEIEKIAG FRHELEEVGM IVSWCSQIEV LRHRAIGCFL THCGWSSSLE
SLVLGVPVVA FPMWSDQPAN AKLLEEIWKT GVRVRENSEG LVERGEIMRC LEAVMEAKSV
ELRENAEKWK RLATEAGREG GSSDKNVEAF VKSLF
