U75B1_ARATH
ID U75B1_ARATH Reviewed; 469 AA.
AC Q9LR44;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=UDP-glycosyltransferase 75B1;
DE EC=2.4.1.-;
DE AltName: Full=(Uridine 5'-diphosphate-glucose:indol-3-ylacetyl)-beta-D-glucosyl transferase 1;
DE AltName: Full=IAA-Glu synthase 1;
DE AltName: Full=Indole-3-acetate beta-glucosyltransferase 1;
DE EC=2.4.1.121;
GN Name=UGT75B1; Synonyms=UGT1; OrderedLocusNames=At1g05560;
GN ORFNames=T25N20.20;
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 [MRNA], SUBCELLULAR LOCATION, AND INTERACTION WITH
RP CALS1; ROP1 AND PHRAGMOPLASTIN.
RC STRAIN=cv. Columbia;
RX PubMed=11283335; DOI=10.2307/3871339;
RA Hong Z., Zhang Z., Olson J.M., Verma D.P.S.;
RT "A novel UDP-glucose transferase is part of the callose synthase complex
RT and interacts with phragmoplastin at the forming cell plate.";
RL Plant Cell 13:769-779(2001).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [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=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 [7]
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 [8]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=18385129; DOI=10.1074/jbc.m709591200;
RA Eudes A., Bozzo G.G., Waller J.C., Naponelli V., Lim E.K., Bowles D.J.,
RA Gregory J.F. III, Hanson A.D.;
RT "Metabolism of the folate precursor p-aminobenzoate in plants: glucose
RT ester formation and vacuolar storage.";
RL J. Biol. Chem. 283:15451-15459(2008).
CC -!- FUNCTION: Possesses low catalytic activity on indole-3-acetic acid
CC (IAA) in vitro. May transfer UDP-glucose from sucrose synthase to
CC callose synthase for the synthesis of callose at the forming cell plate
CC during cytokinesis. Has high affinity for 4-aminobenzoate. Catalyzes
CC the formation of 4-aminobenzoate glucose ester which represents a
CC storage form of 4-aminobenzoate in the vacuole. Is the major source of
CC this activity in the plant. Also active in vitro on benzoates and
CC benzoate derivatives. {ECO:0000269|PubMed:11042207,
CC ECO:0000269|PubMed:11641410, ECO:0000269|PubMed:18385129}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=120 uM for 4-aminobenzoate {ECO:0000269|PubMed:18385129};
CC -!- PATHWAY: Plant hormone metabolism; auxin conjugation.
CC -!- SUBUNIT: Interacts with CALS1, ROP1 and phragmoplastin.
CC {ECO:0000269|PubMed:11283335}.
CC -!- INTERACTION:
CC Q9LR44; Q39821; Xeno; NbExp=2; IntAct=EBI-1765823, EBI-1765815;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:11283335}. Cytoplasm, cytoskeleton, phragmoplast
CC {ECO:0000269|PubMed:11283335}. Note=During interphase, distributed in a
CC punctate pattern in the perinuclear region. Localized in the forming
CC cell plate during cytokinesis.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC condition, but strong reduction in 4-aminobenzoate glucosyltransferase
CC activity. {ECO:0000269|PubMed:18385129}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AF196777; AAK37839.1; -; mRNA.
DR EMBL; AC005106; AAF79730.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27854.1; -; Genomic_DNA.
DR EMBL; AF367358; AAK32944.1; -; mRNA.
DR EMBL; AY078051; AAL77752.1; -; mRNA.
DR RefSeq; NP_563742.1; NM_100435.3.
DR AlphaFoldDB; Q9LR44; -.
DR SMR; Q9LR44; -.
DR BioGRID; 22300; 1.
DR IntAct; Q9LR44; 3.
DR STRING; 3702.AT1G05560.1; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR MetOSite; Q9LR44; -.
DR PaxDb; Q9LR44; -.
DR PRIDE; Q9LR44; -.
DR ProteomicsDB; 228587; -.
DR EnsemblPlants; AT1G05560.1; AT1G05560.1; AT1G05560.
DR GeneID; 837058; -.
DR Gramene; AT1G05560.1; AT1G05560.1; AT1G05560.
DR KEGG; ath:AT1G05560; -.
DR Araport; AT1G05560; -.
DR TAIR; locus:2201031; AT1G05560.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_001724_0_1_1; -.
DR InParanoid; Q9LR44; -.
DR PhylomeDB; Q9LR44; -.
DR BioCyc; ARA:AT1G05560-MON; -.
DR BioCyc; MetaCyc:AT1G05560-MON; -.
DR UniPathway; UPA00376; -.
DR PRO; PR:Q9LR44; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LR44; differential.
DR Genevisible; Q9LR44; AT.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009524; C:phragmoplast; 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:0080002; F:UDP-glucose:4-aminobenzoate acylglucosyltransferase activity; IDA:TAIR.
DR GO; GO:0035251; F:UDP-glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; ISS:TAIR.
DR GO; GO:0046482; P:para-aminobenzoic acid metabolic process; IDA:TAIR.
DR GO; GO:0009751; P:response to salicylic acid; IEP: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 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Glycosyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..469
FT /note="UDP-glycosyltransferase 75B1"
FT /id="PRO_0000334597"
FT BINDING 267
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 332..334
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 349..357
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 371..374
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
SQ SEQUENCE 469 AA; 52813 MW; 77C6088342C78D76 CRC64;
MAPPHFLLVT FPAQGHVNPS LRFARRLIKR TGARVTFVTC VSVFHNSMIA NHNKVENLSF
LTFSDGFDDG GISTYEDRQK RSVNLKVNGD KALSDFIEAT KNGDSPVTCL IYTILLNWAP
KVARRFQLPS ALLWIQPALV FNIYYTHFMG NKSVFELPNL SSLEIRDLPS FLTPSNTNKG
AYDAFQEMME FLIKETKPKI LINTFDSLEP EALTAFPNID MVAVGPLLPT EIFSGSTNKS
VKDQSSSYTL WLDSKTESSV IYVSFGTMVE LSKKQIEELA RALIEGKRPF LWVITDKSNR
ETKTEGEEET EIEKIAGFRH ELEEVGMIVS WCSQIEVLSH RAVGCFVTHC GWSSTLESLV
LGVPVVAFPM WSDQPTNAKL LEESWKTGVR VRENKDGLVE RGEIRRCLEA VMEEKSVELR
ENAKKWKRLA MEAGREGGSS DKNMEAFVED ICGESLIQNL CEAEEVKVK
