U89A2_ARATH
ID U89A2_ARATH Reviewed; 465 AA.
AC Q9LZD8;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=UDP-glycosyltransferase 89A2;
DE EC=2.4.1.-;
GN Name=UGT89A2; OrderedLocusNames=At5g03490; ORFNames=F12E4.260;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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=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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF Clones.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Glucosyltransferase that glucosylates benzoates and benzoate
CC derivatives in vitro. {ECO:0000269|PubMed:11641410}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AL162751; CAB83309.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90611.1; -; Genomic_DNA.
DR EMBL; BT026358; ABH04465.1; -; mRNA.
DR PIR; T48374; T48374.
DR RefSeq; NP_195969.1; NM_120429.4.
DR AlphaFoldDB; Q9LZD8; -.
DR SMR; Q9LZD8; -.
DR STRING; 3702.AT5G03490.1; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR PaxDb; Q9LZD8; -.
DR PRIDE; Q9LZD8; -.
DR ProteomicsDB; 228595; -.
DR EnsemblPlants; AT5G03490.1; AT5G03490.1; AT5G03490.
DR GeneID; 831823; -.
DR Gramene; AT5G03490.1; AT5G03490.1; AT5G03490.
DR KEGG; ath:AT5G03490; -.
DR Araport; AT5G03490; -.
DR TAIR; locus:2142654; AT5G03490.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_001724_2_2_1; -.
DR InParanoid; Q9LZD8; -.
DR OMA; NPPIALI; -.
DR OrthoDB; 508327at2759; -.
DR PhylomeDB; Q9LZD8; -.
DR BioCyc; ARA:AT5G03490-MON; -.
DR PRO; PR:Q9LZD8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LZD8; baseline and differential.
DR Genevisible; Q9LZD8; AT.
DR GO; GO:0035251; F:UDP-glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IMP:TAIR.
DR CDD; cd03784; GT1_Gtf-like; 1.
DR InterPro; IPR002213; UDP_glucos_trans.
DR Pfam; PF00201; UDPGT; 1.
PE 2: Evidence at transcript level;
KW Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..465
FT /note="UDP-glycosyltransferase 89A2"
FT /id="PRO_0000409136"
FT BINDING 291
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 342..344
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 359..367
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT BINDING 381..384
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
SQ SEQUENCE 465 AA; 50942 MW; 3C21B5165CAF6A37 CRC64;
MTEVLLLPGT KSENSKPPHI VVFPFPAQGH LLPLLDLTHQ LCLRGFNVSV IVTPGNLTYL
SPLLSAHPSS VTSVVFPFPP HPSLSPGVEN VKDVGNSGNL PIMASLRQLR EPIINWFQSH
PNPPIALISD FFLGWTHDLC NQIGIPRFAF FSISFFLVSV LQFCFENIDL IKSTDPIHLL
DLPRAPIFKE EHLPSIVRRS LQTPSPDLES IKDFSMNLLS YGSVFNSSEI LEDDYLQYVK
QRMGHDRVYV IGPLCSIGSG LKSNSGSVDP SLLSWLDGSP NGSVLYVCFG SQKALTKDQC
DALALGLEKS MTRFVWVVKK DPIPDGFEDR VSGRGLVVRG WVSQLAVLRH VAVGGFLSHC
GWNSVLEGIT SGAVILGWPM EADQFVNARL LVEHLGVAVR VCEGGETVPD SDELGRVIAE
TMGEGGREVA ARAEEIRRKT EAAVTEANGS SVENVQRLVK EFEKV