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Q8RXD9 (DPE2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:DPE2
Ordered Locus Names:At2g40840
ORF Names:T20B5.4
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length955 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.8 Ref.10 Ref.12 Ref.13

Catalytic activity

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 regulation

Inactivated in response to cold stress. Ref.13

Subcellular location

Cytoplasmcytosol Ref.5 Ref.9 Ref.11.

Induction

Circadian-regulation with a peak in expression in the middle of the light period. Ref.4 Ref.7 Ref.13

Disruption phenotype

Dwarf plants with yellowish leaves that accumulate large amounts of maltose. Increased tolerance to cold. Ref.4 Ref.5 Ref.6 Ref.13

Sequence similarities

Belongs to the disproportionating enzyme family.

Contains 2 CBM20 (carbohydrate binding type-20) domains.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 9559554-alpha-glucanotransferase DPE2
PRO_0000407919

Regions

Domain13 – 122110CBM20 1
Domain157 – 270114CBM20 2

Sequences

Sequence LengthMass (Da)Tools
Q8RXD9 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 248BCED6B0CE79BC

FASTA955109,777
        10         20         30         40         50         60 
MMNLGSLSLS TSKSSKPMVS ISFWIPYFTH WGESLLVCGS APGLGSGNVK KGLLLKPSQQ 

        70         80         90        100        110        120 
DDQLIWSGSV SVPPGFSSDY CYYVVDDSKS VLRSEFGMKR KLVVPETLTG GESVHLRDLW 

       130        140        150        160        170        180 
QSGDQALPFR SAFKDVIFHH SFDVKVEKPL GVFMNKSDQD DSVVVQFKIC CPDIGEGTSV 

       190        200        210        220        230        240 
YVLGTPEKLG NWKVENGLRL NYVDDSIWEA DCLIPKADFP IKYRYCKVQK EDSIGFESGG 

       250        260        270        280        290        300 
NRELSLHSIG SKQEYIVMSD GLFRAMPWRG AGVAVPMFSV RSEDDVGVGE FLDLKLLVDW 

       310        320        330        340        350        360 
AVDSGLHLVQ LLPVNDTSVH KMWWDSYPYS SLSVFALHPL YLRVQALSER LPEDIKEEIQ 

       370        380        390        400        410        420 
KAKNQLDKND VDYEATMETK LSIAKKIFDI EKDQTLNSST FQKFFSENEG WLKPYAAFCF 

       430        440        450        460        470        480 
LRDFFETSDH SQWGTFSDYT DDKLEKLISK DNLHYNTICF HYYIQYHLHV QLSAAAEYAR 

       490        500        510        520        530        540 
KKGVVLKGDL PIGVDRNSVD TWVYRNLFRM NTSTGAPPDY FDKNGQNWGF PTYNWEEMSK 

       550        560        570        580        590        600 
DNYAWWRARL TQMGKYFTAY RIDHILGFFR IWELPAHAMT GLVGKFRPSI PLSQEELEKE 

       610        620        630        640        650        660 
GIWDFDRLSK PYIQKKFLEE KFGDFWPFIA SNFLNETQKD MYEFKEDCNT EKKIVAKLKS 

       670        680        690        700        710        720 
LAEKSLLLEN EDKVRRDVFD ILRNVVLIKD PEDARKFYPR FNIEDTSSFQ DLDDHSKNVL 

       730        740        750        760        770        780 
KRLYYDYYFQ RQEDLWRKNA LKTLPALLNS SNMLACGEDL GLIPSCVHPV MQELGLVGLR 

       790        800        810        820        830        840 
IQRMPSESDV KFGIPSNYDY MTVCAPSCHD CSTLRAWWEE DEERRQQYFK EVIGVDGIPP 

       850        860        870        880        890        900 
SQCIPEITHF ILRQHVEAPS MWAIFPLQDM MALKEEYTTR PATEETINDP TNPKHYWRYR 

       910        920        930        940        950 
VHVTLDSLLK DTDLKSTIKN LVSSSGRSVP ANVSGEDINK SRGEVIANGS TKPNP 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(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. expand/collapse author list , 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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC002409 Genomic DNA. Translation: AAB86444.1. Sequence problems.
CP002685 Genomic DNA. Translation: AEC09889.1.
AY081315 mRNA. Translation: AAL91204.1.
BT010364 mRNA. Translation: AAQ56807.1.
PIRT00748.
RefSeqNP_181616.3. NM_129647.3.
UniGeneAt.44028.

3D structure databases

ProteinModelPortalQ8RXD9.
SMRQ8RXD9. Positions 18-121, 160-259, 297-586.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT2G40840.1-P.

Protein family/group databases

CAZyCBM20. Carbohydrate-Binding Module Family 20.
GH77. Glycoside Hydrolase Family 77.

Proteomic databases

PaxDbQ8RXD9.
PRIDEQ8RXD9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G40840.1; AT2G40840.1; AT2G40840.
GeneID818682.
KEGGath:AT2G40840.

Organism-specific databases

TAIRAT2G40840.

Phylogenomic databases

eggNOGCOG1640.
HOGENOMHOG000291097.
InParanoidQ8RXD9.
KOK00705.
OMASTLRGWW.
PhylomeDBQ8RXD9.
ProtClustDBPLN02950.

Enzyme and pathway databases

BioCycARA:AT2G40840-MONOMER.

Gene expression databases

GenevestigatorQ8RXD9.

Family and domain databases

Gene3D2.60.40.10. 2 hits.
3.20.20.80. 2 hits.
InterProIPR013784. 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]
PfamPF00686. CBM_20. 2 hits.
PF02446. Glyco_hydro_77. 1 hit.
[Graphical view]
SMARTSM01065. CBM_2. 2 hits.
[Graphical view]
SUPFAMSSF49452. SSF49452. 2 hits.
SSF51445. SSF51445. 2 hits.
PROSITEPS51166. CBM20. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDPE2_ARATH
AccessionPrimary (citable) accession number: Q8RXD9
Secondary accession number(s): O22198
Entry history
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: June 1, 2002
Last modified: April 16, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names