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Protein

UDP-glycosyltransferase 72B1

Gene

UGT72B1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

UDP-glucose + hydroquinone = UDP + hydroquinone-O-beta-D-glucopyranoside.

Kineticsi

  1. KM=34.3 µM for 3,4-dichlorophenol1 Publication
  2. KM=16.5 µM for 3,4-dichloroaniline1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei277 – 2771UDP-glucoseCombined sources1 Publication

    GO - Molecular functioni

    GO - Biological processi

    • flavonoid biosynthetic process Source: GO_Central
    • flavonoid glucuronidation Source: GO_Central
    • response to salt stress Source: TAIR
    • response to toxic substance Source: TAIR
    • xenobiotic catabolic process Source: TAIR
    • xenobiotic metabolic process Source: TAIR
    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Detoxification

    Enzyme and pathway databases

    BioCyciARA:GQT-1165-MONOMER.

    Protein family/group databases

    CAZyiGT1. Glycosyltransferase Family 1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    UDP-glycosyltransferase 72B1 (EC:2.4.1.-)
    Alternative name(s):
    Arbutin synthase
    Probable hydroquinone glucosyltransferase (EC:2.4.1.218)
    Gene namesi
    Name:UGT72B1
    Ordered Locus Names:At4g01070
    ORF Names:F2N1.15
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    Proteomesi
    • UP000006548 Componenti: Chromosome 4

    Organism-specific databases

    TAIRiAT4G01070.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Pathology & Biotechi

    Disruption phenotypei

    No visible phenotype under normal growth condition.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi14 – 141S → A: Loss of activity. 1 Publication
    Mutagenesisi19 – 191H → A: Loss of activity. 1 Publication
    Mutagenesisi19 – 191H → Q: Reduces N-glycosyltransferase activity. Loss of O-glycosyltransferase activity. 1 Publication
    Mutagenesisi117 – 1171D → A: Loss of activity. 1 Publication
    Mutagenesisi312 – 3121N → D: Decreases activity. Loss of N-glycosyltransferase activity; when associated with F-315. 1 Publication
    Mutagenesisi315 – 3151Y → F: Decreases activity. Loss of N-glycosyltransferase activity; when associated with D-312. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 480480UDP-glycosyltransferase 72B1PRO_0000074160Add
    BLAST

    Proteomic databases

    PaxDbiQ9M156.
    PRIDEiQ9M156.

    Expressioni

    Gene expression databases

    ExpressionAtlasiQ9M156. baseline and differential.
    GenevisibleiQ9M156. AT.

    Interactioni

    Protein-protein interaction databases

    BioGridi13203. 1 interaction.
    STRINGi3702.AT4G01070.1.

    Structurei

    Secondary structure

    1
    480
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 125Combined sources
    Helixi17 – 3418Combined sources
    Beta strandi37 – 426Combined sources
    Beta strandi45 – 473Combined sources
    Helixi52 – 565Combined sources
    Beta strandi63 – 675Combined sources
    Helixi82 – 9110Combined sources
    Helixi94 – 10613Combined sources
    Beta strandi112 – 1165Combined sources
    Helixi121 – 1233Combined sources
    Helixi124 – 1296Combined sources
    Beta strandi134 – 1385Combined sources
    Helixi142 – 15716Combined sources
    Helixi162 – 1643Combined sources
    Helixi179 – 1813Combined sources
    Helixi184 – 1863Combined sources
    Helixi192 – 20312Combined sources
    Helixi204 – 2063Combined sources
    Beta strandi208 – 2136Combined sources
    Turni216 – 2183Combined sources
    Helixi220 – 2278Combined sources
    Beta strandi236 – 2383Combined sources
    Helixi257 – 2637Combined sources
    Beta strandi270 – 2745Combined sources
    Turni276 – 2783Combined sources
    Helixi283 – 29513Combined sources
    Beta strandi299 – 3046Combined sources
    Turni311 – 3166Combined sources
    Helixi324 – 3274Combined sources
    Helixi332 – 3354Combined sources
    Turni336 – 3394Combined sources
    Beta strandi340 – 3456Combined sources
    Helixi349 – 3546Combined sources
    Beta strandi358 – 3636Combined sources
    Helixi367 – 37610Combined sources
    Beta strandi380 – 3823Combined sources
    Helixi389 – 39810Combined sources
    Helixi416 – 42712Combined sources
    Helixi431 – 44919Combined sources
    Helixi455 – 47521Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2VCEX-ray1.90A1-480[»]
    2VCHX-ray1.45A1-480[»]
    2VG8X-ray1.75A1-480[»]
    ProteinModelPortaliQ9M156.
    SMRiQ9M156. Positions 6-476.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9M156.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni346 – 3472UDP-glucose bindingCombined sources1 Publication
    Regioni364 – 3729UDP-glucose bindingCombined sources1 Publication
    Regioni386 – 3894UDP-glucose bindingCombined sources1 Publication

    Sequence similaritiesi

    Belongs to the UDP-glycosyltransferase family.Curated

    Phylogenomic databases

    eggNOGiKOG1192. Eukaryota.
    COG1819. LUCA.
    HOGENOMiHOG000237568.
    InParanoidiQ9M156.
    OMAiHHGARYR.
    PhylomeDBiQ9M156.

    Family and domain databases

    InterProiIPR002213. UDP_glucos_trans.
    [Graphical view]
    PANTHERiPTHR11926. PTHR11926. 1 hit.
    PfamiPF00201. UDPGT. 1 hit.
    [Graphical view]
    PROSITEiPS00375. UDPGT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

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

    Isoform 1 (identifier: Q9M156-1) [UniParc]FASTAAdd to basket

    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.

    « Hide

            10         20         30         40         50
    MEESKTPHVA IIPSPGMGHL IPLVEFAKRL VHLHGLTVTF VIAGEGPPSK
    60 70 80 90 100
    AQRTVLDSLP SSISSVFLPP VDLTDLSSST RIESRISLTV TRSNPELRKV
    110 120 130 140 150
    FDSFVEGGRL PTALVVDLFG TDAFDVAVEF HVPPYIFYPT TANVLSFFLH
    160 170 180 190 200
    LPKLDETVSC EFRELTEPLM LPGCVPVAGK DFLDPAQDRK DDAYKWLLHN
    210 220 230 240 250
    TKRYKEAEGI LVNTFFELEP NAIKALQEPG LDKPPVYPVG PLVNIGKQEA
    260 270 280 290 300
    KQTEESECLK WLDNQPLGSV LYVSFGSGGT LTCEQLNELA LGLADSEQRF
    310 320 330 340 350
    LWVIRSPSGI ANSSYFDSHS QTDPLTFLPP GFLERTKKRG FVIPFWAPQA
    360 370 380 390 400
    QVLAHPSTGG FLTHCGWNST LESVVSGIPL IAWPLYAEQK MNAVLLSEDI
    410 420 430 440 450
    RAALRPRAGD DGLVRREEVA RVVKGLMEGE EGKGVRNKMK ELKEAACRVL
    460 470 480
    KDDGTSTKAL SLVALKWKAH KKELEQNGNH
    Length:480
    Mass (Da):52,930
    Last modified:October 1, 2000 - v1
    Checksum:i3E0315C1D71D2DB0
    GO

    Sequence cautioni

    The sequence AAB61023.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    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.
    PIRiB85014.
    T01732.
    RefSeqiNP_192016.1. NM_116337.2. [Q9M156-1]
    UniGeneiAt.22609.

    Genome annotation databases

    EnsemblPlantsiAT4G01070.1; AT4G01070.1; AT4G01070. [Q9M156-1]
    GeneIDi827912.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    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.
    PIRiB85014.
    T01732.
    RefSeqiNP_192016.1. NM_116337.2. [Q9M156-1]
    UniGeneiAt.22609.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2VCEX-ray1.90A1-480[»]
    2VCHX-ray1.45A1-480[»]
    2VG8X-ray1.75A1-480[»]
    ProteinModelPortaliQ9M156.
    SMRiQ9M156. Positions 6-476.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi13203. 1 interaction.
    STRINGi3702.AT4G01070.1.

    Protein family/group databases

    CAZyiGT1. Glycosyltransferase Family 1.

    Proteomic databases

    PaxDbiQ9M156.
    PRIDEiQ9M156.

    Protocols and materials databases

    DNASUi827912.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT4G01070.1; AT4G01070.1; AT4G01070. [Q9M156-1]
    GeneIDi827912.

    Organism-specific databases

    TAIRiAT4G01070.

    Phylogenomic databases

    eggNOGiKOG1192. Eukaryota.
    COG1819. LUCA.
    HOGENOMiHOG000237568.
    InParanoidiQ9M156.
    OMAiHHGARYR.
    PhylomeDBiQ9M156.

    Enzyme and pathway databases

    BioCyciARA:GQT-1165-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiQ9M156.
    PROiQ9M156.

    Gene expression databases

    ExpressionAtlasiQ9M156. baseline and differential.
    GenevisibleiQ9M156. AT.

    Family and domain databases

    InterProiIPR002213. UDP_glucos_trans.
    [Graphical view]
    PANTHERiPTHR11926. PTHR11926. 1 hit.
    PfamiPF00201. UDPGT. 1 hit.
    [Graphical view]
    PROSITEiPS00375. UDPGT. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH 2,4,5-TRICHLOROPHENOL AND UDP-GLUCOSE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF SER-14; HIS-19; ASP-117; ASN-312 AND TYR-315.

    Entry informationi

    Entry nameiU72B1_ARATH
    AccessioniPrimary (citable) accession number: Q9M156
    Secondary accession number(s): O04622
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 12, 2003
    Last sequence update: October 1, 2000
    Last modified: November 11, 2015
    This is version 101 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.