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Q8RXD9

- DPE2_ARATH

UniProt

Q8RXD9 - DPE2_ARATH

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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

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
Complete GO annotation...

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
Complete GO annotation...

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

        10         20         30         40         50
MMNLGSLSLS TSKSSKPMVS ISFWIPYFTH WGESLLVCGS APGLGSGNVK
60 70 80 90 100
KGLLLKPSQQ DDQLIWSGSV SVPPGFSSDY CYYVVDDSKS VLRSEFGMKR
110 120 130 140 150
KLVVPETLTG GESVHLRDLW QSGDQALPFR SAFKDVIFHH SFDVKVEKPL
160 170 180 190 200
GVFMNKSDQD DSVVVQFKIC CPDIGEGTSV YVLGTPEKLG NWKVENGLRL
210 220 230 240 250
NYVDDSIWEA DCLIPKADFP IKYRYCKVQK EDSIGFESGG NRELSLHSIG
260 270 280 290 300
SKQEYIVMSD GLFRAMPWRG AGVAVPMFSV RSEDDVGVGE FLDLKLLVDW
310 320 330 340 350
AVDSGLHLVQ LLPVNDTSVH KMWWDSYPYS SLSVFALHPL YLRVQALSER
360 370 380 390 400
LPEDIKEEIQ KAKNQLDKND VDYEATMETK LSIAKKIFDI EKDQTLNSST
410 420 430 440 450
FQKFFSENEG WLKPYAAFCF LRDFFETSDH SQWGTFSDYT DDKLEKLISK
460 470 480 490 500
DNLHYNTICF HYYIQYHLHV QLSAAAEYAR KKGVVLKGDL PIGVDRNSVD
510 520 530 540 550
TWVYRNLFRM NTSTGAPPDY FDKNGQNWGF PTYNWEEMSK DNYAWWRARL
560 570 580 590 600
TQMGKYFTAY RIDHILGFFR IWELPAHAMT GLVGKFRPSI PLSQEELEKE
610 620 630 640 650
GIWDFDRLSK PYIQKKFLEE KFGDFWPFIA SNFLNETQKD MYEFKEDCNT
660 670 680 690 700
EKKIVAKLKS LAEKSLLLEN EDKVRRDVFD ILRNVVLIKD PEDARKFYPR
710 720 730 740 750
FNIEDTSSFQ DLDDHSKNVL KRLYYDYYFQ RQEDLWRKNA LKTLPALLNS
760 770 780 790 800
SNMLACGEDL GLIPSCVHPV MQELGLVGLR IQRMPSESDV KFGIPSNYDY
810 820 830 840 850
MTVCAPSCHD CSTLRAWWEE DEERRQQYFK EVIGVDGIPP SQCIPEITHF
860 870 880 890 900
ILRQHVEAPS MWAIFPLQDM MALKEEYTTR PATEETINDP TNPKHYWRYR
910 920 930 940 950
VHVTLDSLLK DTDLKSTIKN LVSSSGRSVP ANVSGEDINK SRGEVIANGS

TKPNP
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

« Hide 'large scale' publications
  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