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Q8RXD9

- DPE2_ARATH

UniProt

Q8RXD9 - DPE2_ARATH

Protein

4-alpha-glucanotransferase DPE2

Gene

DPE2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (01 Jun 2002)
      Previous versions | rss
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    Functioni

    Cytosolic alpha-glucanotransferase essential for the cytosolic metabolism of maltose, an intermediate on the pathway by which starch is converted to sucrose in leaves at night. Metabolizes maltose exported from the chloroplast and is specific for beta-maltose. May play a role in freezing tolerance. Temperature drop induces inactivation of DPE2 that leads to rapid accumulation of maltose, a solute that protects cells from freezing damage.5 Publications

    Catalytic activityi

    Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan.

    Enzyme regulationi

    Inactivated in response to cold stress.1 Publication

    GO - Molecular functioni

    1. 4-alpha-glucanotransferase activity Source: TAIR
    2. heteropolysaccharide binding Source: TAIR
    3. starch binding Source: InterPro

    GO - Biological processi

    1. glycogen metabolic process Source: GOC
    2. maltose catabolic process Source: TAIR
    3. maltose metabolic process Source: TAIR
    4. polysaccharide metabolic process Source: TAIR
    5. starch catabolic process Source: TAIR

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Carbohydrate metabolism

    Enzyme and pathway databases

    BioCyciARA:AT2G40840-MONOMER.

    Protein family/group databases

    CAZyiCBM20. Carbohydrate-Binding Module Family 20.
    GH77. Glycoside Hydrolase Family 77.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    4-alpha-glucanotransferase DPE2 (EC:2.4.1.25)
    Alternative name(s):
    Amylomaltase
    Disproportionating enzyme
    Short name:
    D-enzyme
    Protein DISPROPORTIONATING ENZYME 2
    Gene namesi
    Name:DPE2
    Ordered Locus Names:At2g40840
    ORF Names:T20B5.4
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 2

    Organism-specific databases

    TAIRiAT2G40840.

    Subcellular locationi

    Cytoplasmcytosol 3 Publications

    GO - Cellular componenti

    1. cytosol Source: TAIR

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Dwarf plants with yellowish leaves that accumulate large amounts of maltose. Increased tolerance to cold.4 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 9559554-alpha-glucanotransferase DPE2PRO_0000407919Add
    BLAST

    Proteomic databases

    PaxDbiQ8RXD9.
    PRIDEiQ8RXD9.

    Expressioni

    Inductioni

    Circadian-regulation with a peak in expression in the middle of the light period.2 Publications

    Gene expression databases

    GenevestigatoriQ8RXD9.

    Interactioni

    Protein-protein interaction databases

    BioGridi4019. 3 interactions.
    STRINGi3702.AT2G40840.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8RXD9.
    SMRiQ8RXD9. Positions 19-104, 163-263, 297-586.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini13 – 122110CBM20 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini157 – 270114CBM20 2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the disproportionating enzyme family.Curated
    Contains 2 CBM20 (carbohydrate binding type-20) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG1640.
    HOGENOMiHOG000291097.
    InParanoidiQ8RXD9.
    KOiK00705.
    OMAiSEKSFGV.
    PhylomeDBiQ8RXD9.

    Family and domain databases

    Gene3Di2.60.40.10. 2 hits.
    3.20.20.80. 2 hits.
    InterProiIPR013784. Carb-bd-like_fold.
    IPR002044. CBM_fam20.
    IPR003385. Glyco_hydro_77.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR013783. Ig-like_fold.
    [Graphical view]
    PfamiPF00686. CBM_20. 2 hits.
    PF02446. Glyco_hydro_77. 1 hit.
    [Graphical view]
    SMARTiSM01065. CBM_2. 2 hits.
    [Graphical view]
    SUPFAMiSSF49452. SSF49452. 2 hits.
    SSF51445. SSF51445. 2 hits.
    PROSITEiPS51166. CBM20. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8RXD9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMNLGSLSLS TSKSSKPMVS ISFWIPYFTH WGESLLVCGS APGLGSGNVK    50
    KGLLLKPSQQ DDQLIWSGSV SVPPGFSSDY CYYVVDDSKS VLRSEFGMKR 100
    KLVVPETLTG GESVHLRDLW QSGDQALPFR SAFKDVIFHH SFDVKVEKPL 150
    GVFMNKSDQD DSVVVQFKIC CPDIGEGTSV YVLGTPEKLG NWKVENGLRL 200
    NYVDDSIWEA DCLIPKADFP IKYRYCKVQK EDSIGFESGG NRELSLHSIG 250
    SKQEYIVMSD GLFRAMPWRG AGVAVPMFSV RSEDDVGVGE FLDLKLLVDW 300
    AVDSGLHLVQ LLPVNDTSVH KMWWDSYPYS SLSVFALHPL YLRVQALSER 350
    LPEDIKEEIQ KAKNQLDKND VDYEATMETK LSIAKKIFDI EKDQTLNSST 400
    FQKFFSENEG WLKPYAAFCF LRDFFETSDH SQWGTFSDYT DDKLEKLISK 450
    DNLHYNTICF HYYIQYHLHV QLSAAAEYAR KKGVVLKGDL PIGVDRNSVD 500
    TWVYRNLFRM NTSTGAPPDY FDKNGQNWGF PTYNWEEMSK DNYAWWRARL 550
    TQMGKYFTAY RIDHILGFFR IWELPAHAMT GLVGKFRPSI PLSQEELEKE 600
    GIWDFDRLSK PYIQKKFLEE KFGDFWPFIA SNFLNETQKD MYEFKEDCNT 650
    EKKIVAKLKS LAEKSLLLEN EDKVRRDVFD ILRNVVLIKD PEDARKFYPR 700
    FNIEDTSSFQ DLDDHSKNVL KRLYYDYYFQ RQEDLWRKNA LKTLPALLNS 750
    SNMLACGEDL GLIPSCVHPV MQELGLVGLR IQRMPSESDV KFGIPSNYDY 800
    MTVCAPSCHD CSTLRAWWEE DEERRQQYFK EVIGVDGIPP SQCIPEITHF 850
    ILRQHVEAPS MWAIFPLQDM MALKEEYTTR PATEETINDP TNPKHYWRYR 900
    VHVTLDSLLK DTDLKSTIKN LVSSSGRSVP ANVSGEDINK SRGEVIANGS 950
    TKPNP 955
    Length:955
    Mass (Da):109,777
    Last modified:June 1, 2002 - v1
    Checksum:i248BCED6B0CE79BC
    GO

    Sequence cautioni

    The sequence AAB86444.1 differs from that shown. Reason: Erroneous gene model prediction.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC002409 Genomic DNA. Translation: AAB86444.1. Sequence problems.
    CP002685 Genomic DNA. Translation: AEC09889.1.
    AY081315 mRNA. Translation: AAL91204.1.
    BT010364 mRNA. Translation: AAQ56807.1.
    PIRiT00748.
    RefSeqiNP_181616.3. NM_129647.3.
    UniGeneiAt.44028.

    Genome annotation databases

    EnsemblPlantsiAT2G40840.1; AT2G40840.1; AT2G40840.
    GeneIDi818682.
    KEGGiath:AT2G40840.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC002409 Genomic DNA. Translation: AAB86444.1 . Sequence problems.
    CP002685 Genomic DNA. Translation: AEC09889.1 .
    AY081315 mRNA. Translation: AAL91204.1 .
    BT010364 mRNA. Translation: AAQ56807.1 .
    PIRi T00748.
    RefSeqi NP_181616.3. NM_129647.3.
    UniGenei At.44028.

    3D structure databases

    ProteinModelPortali Q8RXD9.
    SMRi Q8RXD9. Positions 19-104, 163-263, 297-586.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 4019. 3 interactions.
    STRINGi 3702.AT2G40840.1-P.

    Protein family/group databases

    CAZyi CBM20. Carbohydrate-Binding Module Family 20.
    GH77. Glycoside Hydrolase Family 77.

    Proteomic databases

    PaxDbi Q8RXD9.
    PRIDEi Q8RXD9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT2G40840.1 ; AT2G40840.1 ; AT2G40840 .
    GeneIDi 818682.
    KEGGi ath:AT2G40840.

    Organism-specific databases

    TAIRi AT2G40840.

    Phylogenomic databases

    eggNOGi COG1640.
    HOGENOMi HOG000291097.
    InParanoidi Q8RXD9.
    KOi K00705.
    OMAi SEKSFGV.
    PhylomeDBi Q8RXD9.

    Enzyme and pathway databases

    BioCyci ARA:AT2G40840-MONOMER.

    Gene expression databases

    Genevestigatori Q8RXD9.

    Family and domain databases

    Gene3Di 2.60.40.10. 2 hits.
    3.20.20.80. 2 hits.
    InterProi IPR013784. Carb-bd-like_fold.
    IPR002044. CBM_fam20.
    IPR003385. Glyco_hydro_77.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR013783. Ig-like_fold.
    [Graphical view ]
    Pfami PF00686. CBM_20. 2 hits.
    PF02446. Glyco_hydro_77. 1 hit.
    [Graphical view ]
    SMARTi SM01065. CBM_2. 2 hits.
    [Graphical view ]
    SUPFAMi SSF49452. SSF49452. 2 hits.
    SSF51445. SSF51445. 2 hits.
    PROSITEi PS51166. CBM20. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. 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. "The role of amylomaltase in maltose metabolism in the cytosol of photosynthetic cells."
      Lu Y., Sharkey T.D.
      Planta 218:466-473(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, INDUCTION.
    5. "A cytosolic glucosyltransferase is required for conversion of starch to sucrose in Arabidopsis leaves at night."
      Chia T., Thorneycroft D., Chapple A., Messerli G., Chen J., Zeeman S.C., Smith S.M., Smith A.M.
      Plant J. 37:853-863(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
    6. "beta-Maltose is the metabolically active anomer of maltose during transitory starch degradation."
      Weise S.E., Kim K.S., Stewart R.P., Sharkey T.D.
      Plant Physiol. 137:756-761(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    7. "Daylength and circadian effects on starch degradation and maltose metabolism."
      Lu Y., Gehan J.P., Sharkey T.D.
      Plant Physiol. 138:2280-2291(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    8. "Mutants of Arabidopsis lacking starch branching enzyme II substitute plastidial starch synthesis by cytoplasmic maltose accumulation."
      Dumez S., Wattebled F., Dauvillee D., Delvalle D., Planchot V., Ball S.G., D'Hulst C.
      Plant Cell 18:2694-2709(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Cellular and organ level localization of maltose in maltose-excess Arabidopsis mutants."
      Lu Y., Steichen J.M., Weise S.E., Sharkey T.D.
      Planta 224:935-943(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    10. "A transglucosidase necessary for starch degradation and maltose metabolism in leaves at night acts on cytosolic heteroglycans (SHG)."
      Fettke J., Chia T., Eckermann N., Smith A., Steup M.
      Plant J. 46:668-684(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Repression of both isoforms of disproportionating enzyme leads to higher malto-oligosaccharide content and reduced growth in potato."
      Luetken H., Lloyd J.R., Glaring M.A., Baunsgaard L., Laursen K.H., Haldrup A., Kossmann J., Blennow A.
      Planta 232:1127-1139(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    12. "Starch-related cytosolic heteroglycans in roots from Arabidopsis thaliana."
      Malinova I., Steup M., Fettke J.
      J. Plant Physiol. 168:1406-1414(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "Proteomics analysis reveals post-translational mechanisms for cold-induced metabolic changes in Arabidopsis."
      Li T., Xu S.L., Oses-Prieto J.A., Putil S., Xu P., Wang R.J., Li K.H., Maltby D.A., An L.H., Burlingame A.L., Deng Z.P., Wang Z.Y.
      Mol. Plant 4:361-374(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, DISRUPTION PHENOTYPE.
    14. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiDPE2_ARATH
    AccessioniPrimary (citable) accession number: Q8RXD9
    Secondary accession number(s): O22198
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: June 1, 2002
    Last modified: October 1, 2014
    This is version 89 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

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3