U72B1_ARATH
ID U72B1_ARATH Reviewed; 480 AA.
AC Q9M156; O04622;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=UDP-glycosyltransferase 72B1;
DE EC=2.4.1.-;
DE AltName: Full=Arbutin synthase;
DE AltName: Full=Probable hydroquinone glucosyltransferase;
DE EC=2.4.1.218;
GN Name=UGT72B1; OrderedLocusNames=At4g01070; ORFNames=F2N1.15;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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].
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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) 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, AND DISRUPTION PHENOTYPE.
RX PubMed=15860014; DOI=10.1111/j.1365-313x.2005.02398.x;
RA Brazier-Hicks M., Edwards R.;
RT "Functional importance of the family 1 glucosyltransferase UGT72B1 in the
RT metabolism of xenobiotics in Arabidopsis thaliana.";
RL Plant J. 42:556-566(2005).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH
RP 2,4,5-TRICHLOROPHENOL AND UDP-GLUCOSE, FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF SER-14; HIS-19; ASP-117; ASN-312 AND
RP TYR-315.
RX PubMed=18077347; DOI=10.1073/pnas.0706421104;
RA Brazier-Hicks M., Offen W.A., Gershater M.C., Revett T.J., Lim E.K.,
RA Bowles D.J., Davies G.J., Edwards R.;
RT "Characterization and engineering of the bifunctional N- and O-
RT glucosyltransferase involved in xenobiotic metabolism in plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:20238-20243(2007).
CC -!- FUNCTION: Bifunctional O-glycosyltransferase and N-glycosyltransferase
CC that can detoxify xenobiotics. Possesses high activity to metabolize
CC the persistent pollutants 2,4,5-trichlorophenol (TCP) and 3,4-
CC dichloroaniline (DCA). Also active on benzoates and benzoate
CC derivatives in vitro. {ECO:0000269|PubMed:11641410,
CC ECO:0000269|PubMed:15860014, ECO:0000269|PubMed:18077347}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydroquinone + UDP-alpha-D-glucose = H(+) + hydroquinone O-
CC beta-D-glucopyranoside + UDP; Xref=Rhea:RHEA:12560,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17594, ChEBI:CHEBI:18305,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.218;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=34.3 uM for 3,4-dichlorophenol {ECO:0000269|PubMed:18077347};
CC KM=16.5 uM for 3,4-dichloroaniline {ECO:0000269|PubMed:18077347};
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=Q9M156-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC condition. {ECO:0000269|PubMed:15860014}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB61023.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
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DR EMBL; AF007269; AAB61023.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161491; CAB80916.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE81977.1; -; Genomic_DNA.
DR EMBL; AF360262; AAK25972.1; -; mRNA.
DR EMBL; AY040075; AAK64133.1; -; mRNA.
DR EMBL; AY084892; AAM61455.1; -; mRNA.
DR PIR; B85014; B85014.
DR PIR; T01732; T01732.
DR RefSeq; NP_192016.1; NM_116337.3. [Q9M156-1]
DR PDB; 2VCE; X-ray; 1.90 A; A=1-480.
DR PDB; 2VCH; X-ray; 1.45 A; A=1-480.
DR PDB; 2VG8; X-ray; 1.75 A; A=1-480.
DR PDBsum; 2VCE; -.
DR PDBsum; 2VCH; -.
DR PDBsum; 2VG8; -.
DR AlphaFoldDB; Q9M156; -.
DR SMR; Q9M156; -.
DR BioGRID; 13203; 1.
DR STRING; 3702.AT4G01070.1; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR PaxDb; Q9M156; -.
DR PRIDE; Q9M156; -.
DR ProteomicsDB; 242611; -. [Q9M156-1]
DR DNASU; 827912; -.
DR EnsemblPlants; AT4G01070.1; AT4G01070.1; AT4G01070. [Q9M156-1]
DR GeneID; 827912; -.
DR Gramene; AT4G01070.1; AT4G01070.1; AT4G01070. [Q9M156-1]
DR KEGG; ath:AT4G01070; -.
DR Araport; AT4G01070; -.
DR TAIR; locus:2125023; AT4G01070.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_001724_3_2_1; -.
DR InParanoid; Q9M156; -.
DR PhylomeDB; Q9M156; -.
DR EvolutionaryTrace; Q9M156; -.
DR PRO; PR:Q9M156; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M156; baseline and differential.
DR Genevisible; Q9M156; AT.
DR GO; GO:0050505; F:hydroquinone glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0035251; F:UDP-glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IDA:TAIR.
DR GO; GO:0009809; P:lignin biosynthetic process; IMP:TAIR.
DR GO; GO:0009636; P:response to toxic substance; IDA:TAIR.
DR GO; GO:0042178; P:xenobiotic catabolic process; IDA:TAIR.
DR GO; GO:0006805; P:xenobiotic metabolic process; IMP: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 3D-structure; Alternative splicing; Detoxification; Glycosyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..480
FT /note="UDP-glycosyltransferase 72B1"
FT /id="PRO_0000074160"
FT BINDING 277
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000269|PubMed:18077347,
FT ECO:0007744|PDB:2VCE"
FT BINDING 346..347
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000269|PubMed:18077347,
FT ECO:0007744|PDB:2VCE"
FT BINDING 364..372
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000269|PubMed:18077347,
FT ECO:0007744|PDB:2VCE"
FT BINDING 386..389
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000269|PubMed:18077347,
FT ECO:0007744|PDB:2VCE"
FT MUTAGEN 14
FT /note="S->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18077347"
FT MUTAGEN 19
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18077347"
FT MUTAGEN 19
FT /note="H->Q: Reduces N-glycosyltransferase activity. Loss
FT of O-glycosyltransferase activity."
FT /evidence="ECO:0000269|PubMed:18077347"
FT MUTAGEN 117
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18077347"
FT MUTAGEN 312
FT /note="N->D: Decreases activity. Loss of N-
FT glycosyltransferase activity; when associated with F-315."
FT /evidence="ECO:0000269|PubMed:18077347"
FT MUTAGEN 315
FT /note="Y->F: Decreases activity. Loss of N-
FT glycosyltransferase activity; when associated with D-312."
FT /evidence="ECO:0000269|PubMed:18077347"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:2VCH"
FT HELIX 17..34
FT /evidence="ECO:0007829|PDB:2VCH"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:2VCH"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:2VCH"
FT HELIX 52..56
FT /evidence="ECO:0007829|PDB:2VCH"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:2VCH"
FT HELIX 82..91
FT /evidence="ECO:0007829|PDB:2VCH"
FT HELIX 94..106
FT /evidence="ECO:0007829|PDB:2VCH"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:2VCH"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:2VCH"
FT HELIX 124..129
FT /evidence="ECO:0007829|PDB:2VCH"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:2VCH"
FT HELIX 142..157
FT /evidence="ECO:0007829|PDB:2VCH"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:2VCH"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:2VCH"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:2VCH"
FT HELIX 192..203
FT /evidence="ECO:0007829|PDB:2VCH"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:2VCH"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:2VCH"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:2VCH"
FT HELIX 220..227
FT /evidence="ECO:0007829|PDB:2VCH"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:2VCH"
FT HELIX 257..263
FT /evidence="ECO:0007829|PDB:2VCH"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:2VCH"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:2VCH"
FT HELIX 283..295
FT /evidence="ECO:0007829|PDB:2VCH"
FT STRAND 299..304
FT /evidence="ECO:0007829|PDB:2VCH"
FT TURN 311..316
FT /evidence="ECO:0007829|PDB:2VCH"
FT HELIX 324..327
FT /evidence="ECO:0007829|PDB:2VCH"
FT HELIX 332..335
FT /evidence="ECO:0007829|PDB:2VCH"
FT TURN 336..339
FT /evidence="ECO:0007829|PDB:2VCH"
FT STRAND 340..345
FT /evidence="ECO:0007829|PDB:2VCH"
FT HELIX 349..354
FT /evidence="ECO:0007829|PDB:2VCH"
FT STRAND 358..363
FT /evidence="ECO:0007829|PDB:2VCH"
FT HELIX 367..376
FT /evidence="ECO:0007829|PDB:2VCH"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:2VCH"
FT HELIX 389..398
FT /evidence="ECO:0007829|PDB:2VCH"
FT HELIX 416..427
FT /evidence="ECO:0007829|PDB:2VCH"
FT HELIX 431..449
FT /evidence="ECO:0007829|PDB:2VCH"
FT HELIX 455..475
FT /evidence="ECO:0007829|PDB:2VCH"
SQ SEQUENCE 480 AA; 52930 MW; 3E0315C1D71D2DB0 CRC64;
MEESKTPHVA IIPSPGMGHL IPLVEFAKRL VHLHGLTVTF VIAGEGPPSK AQRTVLDSLP
SSISSVFLPP VDLTDLSSST RIESRISLTV TRSNPELRKV FDSFVEGGRL PTALVVDLFG
TDAFDVAVEF HVPPYIFYPT TANVLSFFLH LPKLDETVSC EFRELTEPLM LPGCVPVAGK
DFLDPAQDRK DDAYKWLLHN TKRYKEAEGI LVNTFFELEP NAIKALQEPG LDKPPVYPVG
PLVNIGKQEA KQTEESECLK WLDNQPLGSV LYVSFGSGGT LTCEQLNELA LGLADSEQRF
LWVIRSPSGI ANSSYFDSHS QTDPLTFLPP GFLERTKKRG FVIPFWAPQA QVLAHPSTGG
FLTHCGWNST LESVVSGIPL IAWPLYAEQK MNAVLLSEDI RAALRPRAGD DGLVRREEVA
RVVKGLMEGE EGKGVRNKMK ELKEAACRVL KDDGTSTKAL SLVALKWKAH KKELEQNGNH
