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Q9LV91

- DPE1_ARATH

UniProt

Q9LV91 - DPE1_ARATH

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Protein
4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic
Gene
DPE1, At5g64860, MXK3.9
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

Chloroplastic alpha-glucanotransferase involved in maltotriose metabolism. Probably uses maltotriose as substrate to transfer a maltosyl unit from one molecule to another, resulting in glucose and maltopentaose. The latter can then be further metabolized to maltose and maltotriose by beta-amylase. Required for normal starch degradation in leaves.2 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.

GO - Molecular functioni

  1. 4-alpha-glucanotransferase activity Source: UniProtKB

GO - Biological processi

  1. glucose metabolic process Source: TAIR
  2. glycogen metabolic process Source: GOC
  3. maltose catabolic process Source: UniProtKB
  4. starch catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism

Enzyme and pathway databases

BioCyciARA:AT5G64860-MONOMER.
MetaCyc:AT5G64860-MONOMER.
BRENDAi2.4.1.25. 399.

Protein family/group databases

CAZyiGH77. Glycoside Hydrolase Family 77.

Names & Taxonomyi

Protein namesi
Recommended name:
4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic (EC:2.4.1.25)
Alternative name(s):
Amylomaltase
Disproportionating enzyme
Short name:
D-enzyme
Protein DISPROPORTIONATING ENZYME 1
Gene namesi
Name:DPE1
Ordered Locus Names:At5g64860
ORF Names:MXK3.9
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 5

Organism-specific databases

TAIRiAT5G64860.

Subcellular locationi

Plastidchloroplast. Plastidamyloplast Reviewed prediction

GO - Cellular componenti

  1. amyloplast Source: UniProtKB-SubCell
  2. chloroplast Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Amyloplast, Chloroplast, Plastid

Pathology & Biotechi

Disruption phenotypei

Increased amounts of maltotriose and leaf starch.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4545Chloroplast Reviewed prediction
Add
BLAST
Chaini46 – 5765314-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic
PRO_0000407918Add
BLAST

Proteomic databases

PaxDbiQ9LV91.
PRIDEiQ9LV91.

Expressioni

Gene expression databases

GenevestigatoriQ9LV91.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT5G64860.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ9LV91.
SMRiQ9LV91. Positions 60-576.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1640.
HOGENOMiHOG000017376.
InParanoidiQ9LV91.
KOiK00705.
OMAiDFWEIPG.
PhylomeDBiQ9LV91.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR003385. Glyco_hydro_77.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF02446. Glyco_hydro_77. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
TIGRFAMsiTIGR00217. malQ. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9LV91-1 [UniParc]FASTAAdd to Basket

« Hide

MSILLRPSSS PSLCSSLKLF RLSSPDSLID AAVLRNRTKP SQSFRMEVVS    50
SNSTCLSSIS VGEDFPSEYE QWLPVPDPES RRRAGVLLHP TSFRGPHGIG 100
DLGEEAFRFI DWLHSTGCSV WQVLPLVPPD EGGSPYAGQD ANCGNTLLIS 150
LDELVKDGLL IKDELPQPID ADSVNYQTAN KLKSPLITKA AKRLIDGNGE 200
LKSKLLDFRN DPSISCWLED AAYFAAIDNT LNAYSWFEWP EPLKNRHLSA 250
LEAIYESQKE FIDLFIAKQF LFQRQWQKVR EYARRQGVDI MGDMPIYVGY 300
HSADVWANKK HFLLNKKGFP LLVSGVPPDL FSETGQLWGS PLYDWKAMES 350
DQYSWWVNRI RRAQDLYDEC RIDHFRGFAG FWAVPSEAKV AMVGRWKVGP 400
GKSLFDAISK GVGKIKIIAE DLGVITKDVV ELRKSIGAPG MAVLQFAFGG 450
GADNPHLPHN HEVNQVVYSG THDNDTIRGW WDTLDQEEKS KAMKYLSIAG 500
EDDISWSVIQ AAFSSTAQTA IIPMQDILGL GSSARMNTPA TEVGNWGWRI 550
PSSTSFDNLE TESDRLRDLL SLYGRL 576
Length:576
Mass (Da):64,412
Last modified:October 1, 2000 - v1
Checksum:i1363A43AF365A491
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB019236 Genomic DNA. Translation: BAA97298.1.
CP002688 Genomic DNA. Translation: AED97962.1.
AY037231 mRNA. Translation: AAK59831.1.
AY081744 mRNA. Translation: AAL87397.1.
RefSeqiNP_201291.1. NM_125884.3.
UniGeneiAt.7845.

Genome annotation databases

EnsemblPlantsiAT5G64860.1; AT5G64860.1; AT5G64860.
GeneIDi836609.
KEGGiath:AT5G64860.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB019236 Genomic DNA. Translation: BAA97298.1 .
CP002688 Genomic DNA. Translation: AED97962.1 .
AY037231 mRNA. Translation: AAK59831.1 .
AY081744 mRNA. Translation: AAL87397.1 .
RefSeqi NP_201291.1. NM_125884.3.
UniGenei At.7845.

3D structure databases

ProteinModelPortali Q9LV91.
SMRi Q9LV91. Positions 60-576.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 3702.AT5G64860.1-P.

Protein family/group databases

CAZyi GH77. Glycoside Hydrolase Family 77.

Proteomic databases

PaxDbi Q9LV91.
PRIDEi Q9LV91.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT5G64860.1 ; AT5G64860.1 ; AT5G64860 .
GeneIDi 836609.
KEGGi ath:AT5G64860.

Organism-specific databases

TAIRi AT5G64860.

Phylogenomic databases

eggNOGi COG1640.
HOGENOMi HOG000017376.
InParanoidi Q9LV91.
KOi K00705.
OMAi DFWEIPG.
PhylomeDBi Q9LV91.

Enzyme and pathway databases

BioCyci ARA:AT5G64860-MONOMER.
MetaCyc:AT5G64860-MONOMER.
BRENDAi 2.4.1.25. 399.

Gene expression databases

Genevestigatori Q9LV91.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR003385. Glyco_hydro_77.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF02446. Glyco_hydro_77. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
TIGRFAMsi TIGR00217. malQ. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence features of the regions of 3,076,755 bp covered by sixty P1 and TAC clones."
    Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H., Tabata S.
    DNA Res. 7:31-63(2000) [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. "A critical role for disproportionating enzyme in starch breakdown is revealed by a knock-out mutation in Arabidopsis."
    Critchley J.H., Zeeman S.C., Takaha T., Smith A.M., Smith S.M.
    Plant J. 26:89-100(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  5. "Blocking the metabolism of starch breakdown products in Arabidopsis leaves triggers chloroplast degradation."
    Stettler M., Eicke S., Mettler T., Messerli G., Hoertensteiner S., Zeeman S.C.
    Mol. Plant 2:1233-1246(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiDPE1_ARATH
AccessioniPrimary (citable) accession number: Q9LV91
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 85 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

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