Q9M156 (U72B1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
UDP-glycosyltransferase 72B1
EC=2.4.1.-

Alternative name(s):
Arbutin synthase
Probable hydroquinone glucosyltransferase
EC=2.4.1.218

Gene names

Name:	UGT72B1
Ordered Locus Names:	At4g01070
ORF Names:	F2N1.15

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	480 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Bifunctional O-glycosyltransferase and N-glycosyltransferase that can detoxify xenobiotics. Possesses high activity to metabolize the peristent pollutants 2,4,5-trichlorophenol (TCP) and 3,4-dichloroaniline (DCA). Also active on benzoates and benzoate derivatives in vitro. Ref.6 Ref.7 Ref.8
Catalytic activity	UDP-glucose + hydroquinone = UDP + hydroquinone-O-beta-D-glucopyranoside.
Disruption phenotype	No visible phenotype under normal growth condition. Ref.7
Sequence similarities	Belongs to the UDP-glycosyltransferase family.
Biophysicochemical properties	Kinetic parameters: KM=34.3 µM for 3,4-dichlorophenol Ref.8 KM=16.5 µM for 3,4-dichloroaniline
Sequence caution	The sequence AAB61023.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Detoxification
Coding sequence diversity	Alternative splicing
Molecular function	Glycosyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	response to salt stress Inferred from expression pattern. Source: TAIR response to toxin Inferred from direct assay. Source: TAIR xenobiotic catabolic process Inferred from direct assay. Source: TAIR
Molecular function	hydroquinone glucosyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q9M156-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 480

480

UDP-glycosyltransferase 72B1

PRO_0000074160

Regions

Region

347 – 349

3

UDP-glucose binding

Region

364 – 372

9

UDP-glucose binding

Region

386 – 389

4

UDP-glucose binding

Sites

Binding site

277

1

UDP-glucose

Experimental info

Mutagenesis

14

1

S → A: Loss of activity. Ref.8

Mutagenesis

19

1

H → A: Loss of activity. Ref.8

Mutagenesis

19

1

H → Q: Reduces N-glycosyltransferase activity. Loss of O-glycosyltransferase activity. Ref.8

Mutagenesis

117

1

D → A: Loss of activity. Ref.8

Mutagenesis

312

1

N → D: Decreases activity. Loss of N-glycosyltransferase activity; when associated with F-315. Ref.8

Mutagenesis

315

1

Y → F: Decreases activity. Loss of N-glycosyltransferase activity; when associated with D-312. Ref.8

Secondary structure

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480

Helix Strand Turn

Details...

Beta strand

8 – 12

5

Helix

17 – 34

18

Beta strand

37 – 42

6

Beta strand

45 – 47

3

Helix

52 – 56

5

Beta strand

63 – 67

5

Helix

82 – 91

10

Helix

94 – 106

13

Beta strand

112 – 116

5

Helix

121 – 123

3

Helix

124 – 129

6

Beta strand

134 – 138

5

Helix

142 – 157

16

Helix

162 – 164

3

Helix

179 – 181

3

Helix

184 – 186

3

Helix

192 – 203

12

Helix

204 – 206

3

Beta strand

208 – 213

6

Turn

216 – 218

3

Helix

220 – 227

8

Beta strand

236 – 238

3

Helix

257 – 263

7

Beta strand

270 – 274

5

Turn

276 – 278

3

Helix

283 – 295

13

Beta strand

299 – 304

6

Turn

311 – 316

6

Helix

324 – 327

4

Helix

332 – 335

4

Turn

336 – 339

4

Beta strand

340 – 345

6

Helix

349 – 354

6

Beta strand

358 – 363

6

Helix

367 – 376

10

Beta strand

380 – 382

3

Helix

389 – 398

10

Helix

416 – 427

12

Helix

431 – 449

19

Helix

455 – 475

21

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 3E0315C1D71D2DB0	FASTA	480	52,930
	10 20 30 40 50 60 MEESKTPHVA IIPSPGMGHL IPLVEFAKRL VHLHGLTVTF VIAGEGPPSK AQRTVLDSLP 70 80 90 100 110 120 SSISSVFLPP VDLTDLSSST RIESRISLTV TRSNPELRKV FDSFVEGGRL PTALVVDLFG 130 140 150 160 170 180 TDAFDVAVEF HVPPYIFYPT TANVLSFFLH LPKLDETVSC EFRELTEPLM LPGCVPVAGK 190 200 210 220 230 240 DFLDPAQDRK DDAYKWLLHN TKRYKEAEGI LVNTFFELEP NAIKALQEPG LDKPPVYPVG 250 260 270 280 290 300 PLVNIGKQEA KQTEESECLK WLDNQPLGSV LYVSFGSGGT LTCEQLNELA LGLADSEQRF 310 320 330 340 350 360 LWVIRSPSGI ANSSYFDSHS QTDPLTFLPP GFLERTKKRG FVIPFWAPQA QVLAHPSTGG 370 380 390 400 410 420 FLTHCGWNST LESVVSGIPL IAWPLYAEQK MNAVLLSEDI RAALRPRAGD DGLVRREEVA 430 440 450 460 470 480 RVVKGLMEGE EGKGVRNKMK ELKEAACRVL KDDGTSTKAL SLVALKWKAH KKELEQNGNH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"Phylogenetic analysis of the UDP-glycosyltransferase multigene family of Arabidopsis thaliana." Li Y., Baldauf S., Lim E.K., Bowles D.J. J. Biol. Chem. 276:4338-4343(2001) [PubMed: 11042215] [Abstract] Cited for: GENE FAMILY.
[6]	"The activity of Arabidopsis glycosyltransferases toward salicylic acid, 4-hydroxybenzoic acid, and other benzoates." Lim E.K., Doucet C.J., Li Y., Elias L., Worrall D., Spencer S.P., Ross J., Bowles D.J. J. Biol. Chem. 277:586-592(2002) [PubMed: 11641410] [Abstract] Cited for: FUNCTION.
[7]	"Functional importance of the family 1 glucosyltransferase UGT72B1 in the metabolism of xenobiotics in Arabidopsis thaliana." Brazier-Hicks M., Edwards R. Plant J. 42:556-566(2005) [PubMed: 15860014] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[8]	"Characterization and engineering of the bifunctional N- and O-glucosyltransferase involved in xenobiotic metabolism in plants." Brazier-Hicks M., Offen W.A., Gershater M.C., Revett T.J., Lim E.K., Bowles D.J., Davies G.J., Edwards R. Proc. Natl. Acad. Sci. U.S.A. 104:20238-20243(2007) [PubMed: 18077347] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH UDP, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF SER-14; HIS-19; ASP-117; ASN-312 AND TYR-315.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF007269 Genomic DNA. Translation: AAB61023.1. Sequence problems.
AL161491 Genomic DNA. Translation: CAB80916.1.
CP002687 Genomic DNA. Translation: AEE81977.1.
AF360262 mRNA. Translation: AAK25972.1.
AY040075 mRNA. Translation: AAK64133.1.
AY084892 mRNA. Translation: AAM61455.1.

IPI

IPI00525765.

PIR

B85014.
T01732.

RefSeq

NP_192016.1. NM_116337.2.

UniGene

At.22609.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2VCE	X-ray	1.90	A	1-480	[»]
2VCH	X-ray	1.45	A	1-480	[»]
2VG8	X-ray	1.75	A	1-480	[»]

ProteinModelPortal

Q9M156.

SMR

Q9M156. Positions 6-476.

ModBase

Search...

Protein family/group databases

CAZy

GT1. Glycosyltransferase Family 1.

Proteomic databases

PRIDE

Q9M156.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

AT4G01070.1; AT4G01070.1; AT4G01070.

GeneID

827912.

GenomeReviews

Gene locus AT4G01070 in contig CT486007_GR.

KEGG

ath:AT4G01070.

NMPDR

fig|3702.1.peg.17890.

Organism-specific databases

TAIR

At4g01070.

Phylogenomic databases

GeneTree

EPGT00050000005352.

HOGENOM

HBG746957.

InParanoid

Q9M156.

OMA

QTEESEC.

PhylomeDB

Q9M156.

ProtClustDB

CLSN2682857.

Gene expression databases

ArrayExpress

Q9M156.

Genevestigator

Q9M156.

GermOnline

AT4G01070. Arabidopsis thaliana.

Family and domain databases

InterPro

IPR002213. UDP_glucos_trans.
[Graphical view]

KO

K08237.

PANTHER

PTHR11926. UDP_glucos_trans. 1 hit.

Pfam

PF00201. UDPGT. 1 hit.
[Graphical view]

PROSITE

PS00375. UDPGT. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

U72B1_ARATH

Accession

Primary (citable) accession number: Q9M156
Secondary accession number(s): O04622

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	October 1, 2000
Last modified:	December 14, 2011
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program