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Protein

4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic

Gene

DPE1

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

  • 4-alpha-glucanotransferase activity Source: UniProtKB

GO - Biological processi

  • glucose metabolic process Source: TAIR
  • glycogen metabolic process Source: GOC
  • maltose catabolic process Source: UniProtKB
  • 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
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G64860.

Subcellular locationi

GO - Cellular componenti

  • amyloplast Source: UniProtKB-SubCell
  • 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 – 4545ChloroplastSequence analysisAdd
BLAST
Chaini46 – 5765314-alpha-glucanotransferase DPE1, chloroplastic/amyloplasticPRO_0000407918Add
BLAST

Proteomic databases

PaxDbiQ9LV91.
PRIDEiQ9LV91.

Expressioni

Gene expression databases

GenevisibleiQ9LV91. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT5G64860.1.

Structurei

Secondary structure

1
576
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi69 – 713Combined sources
Helixi78 – 803Combined sources
Beta strandi83 – 875Combined sources
Helixi90 – 923Combined sources
Beta strandi96 – 994Combined sources
Helixi104 – 11613Combined sources
Beta strandi120 – 1223Combined sources
Helixi135 – 1373Combined sources
Beta strandi141 – 1433Combined sources
Helixi146 – 1483Combined sources
Helixi151 – 1566Combined sources
Helixi162 – 1643Combined sources
Helixi176 – 19621Combined sources
Helixi200 – 21011Combined sources
Helixi212 – 23019Combined sources
Helixi236 – 2383Combined sources
Helixi241 – 2444Combined sources
Helixi248 – 25710Combined sources
Helixi259 – 28527Combined sources
Beta strandi289 – 2979Combined sources
Beta strandi300 – 3023Combined sources
Helixi303 – 3064Combined sources
Helixi307 – 3115Combined sources
Beta strandi320 – 3267Combined sources
Beta strandi332 – 3343Combined sources
Beta strandi336 – 3416Combined sources
Helixi345 – 3495Combined sources
Turni350 – 3534Combined sources
Helixi354 – 36613Combined sources
Beta strandi368 – 3736Combined sources
Helixi375 – 3784Combined sources
Beta strandi380 – 3856Combined sources
Helixi391 – 3933Combined sources
Beta strandi395 – 3984Combined sources
Helixi402 – 41211Combined sources
Beta strandi417 – 4193Combined sources
Helixi427 – 43610Combined sources
Beta strandi440 – 4434Combined sources
Helixi444 – 4463Combined sources
Beta strandi449 – 4513Combined sources
Helixi458 – 4603Combined sources
Beta strandi463 – 4697Combined sources
Helixi477 – 4837Combined sources
Helixi486 – 49510Combined sources
Helixi501 – 5033Combined sources
Helixi504 – 51411Combined sources
Beta strandi518 – 5236Combined sources
Helixi524 – 5274Combined sources
Helixi532 – 5343Combined sources
Helixi556 – 5583Combined sources
Helixi560 – 57213Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5CPQX-ray2.13A/B46-576[»]
5CPSX-ray1.80A/B46-576[»]
5CPTX-ray2.30A/B46-576[»]
5CQ1X-ray2.30A/B46-576[»]
5CSUX-ray2.53A/B46-576[»]
5CSYX-ray2.05A/B46-576[»]
ProteinModelPortaliQ9LV91.
SMRiQ9LV91. Positions 60-576.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the disproportionating enzyme family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410IFXE. Eukaryota.
COG1640. LUCA.
HOGENOMiHOG000017376.
InParanoidiQ9LV91.
KOiK00705.
OMAiTGQLWGT.
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

        10         20         30         40         50
MSILLRPSSS PSLCSSLKLF RLSSPDSLID AAVLRNRTKP SQSFRMEVVS
60 70 80 90 100
SNSTCLSSIS VGEDFPSEYE QWLPVPDPES RRRAGVLLHP TSFRGPHGIG
110 120 130 140 150
DLGEEAFRFI DWLHSTGCSV WQVLPLVPPD EGGSPYAGQD ANCGNTLLIS
160 170 180 190 200
LDELVKDGLL IKDELPQPID ADSVNYQTAN KLKSPLITKA AKRLIDGNGE
210 220 230 240 250
LKSKLLDFRN DPSISCWLED AAYFAAIDNT LNAYSWFEWP EPLKNRHLSA
260 270 280 290 300
LEAIYESQKE FIDLFIAKQF LFQRQWQKVR EYARRQGVDI MGDMPIYVGY
310 320 330 340 350
HSADVWANKK HFLLNKKGFP LLVSGVPPDL FSETGQLWGS PLYDWKAMES
360 370 380 390 400
DQYSWWVNRI RRAQDLYDEC RIDHFRGFAG FWAVPSEAKV AMVGRWKVGP
410 420 430 440 450
GKSLFDAISK GVGKIKIIAE DLGVITKDVV ELRKSIGAPG MAVLQFAFGG
460 470 480 490 500
GADNPHLPHN HEVNQVVYSG THDNDTIRGW WDTLDQEEKS KAMKYLSIAG
510 520 530 540 550
EDDISWSVIQ AAFSSTAQTA IIPMQDILGL GSSARMNTPA TEVGNWGWRI
560 570
PSSTSFDNLE TESDRLRDLL SLYGRL
Length:576
Mass (Da):64,412
Last modified:October 1, 2000 - v1
Checksum:i1363A43AF365A491
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
GrameneiAT5G64860.1; AT5G64860.1; AT5G64860.
KEGGiath:AT5G64860.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5CPQX-ray2.13A/B46-576[»]
5CPSX-ray1.80A/B46-576[»]
5CPTX-ray2.30A/B46-576[»]
5CQ1X-ray2.30A/B46-576[»]
5CSUX-ray2.53A/B46-576[»]
5CSYX-ray2.05A/B46-576[»]
ProteinModelPortaliQ9LV91.
SMRiQ9LV91. Positions 60-576.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT5G64860.1.

Protein family/group databases

CAZyiGH77. Glycoside Hydrolase Family 77.

Proteomic databases

PaxDbiQ9LV91.
PRIDEiQ9LV91.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G64860.1; AT5G64860.1; AT5G64860.
GeneIDi836609.
GrameneiAT5G64860.1; AT5G64860.1; AT5G64860.
KEGGiath:AT5G64860.

Organism-specific databases

TAIRiAT5G64860.

Phylogenomic databases

eggNOGiENOG410IFXE. Eukaryota.
COG1640. LUCA.
HOGENOMiHOG000017376.
InParanoidiQ9LV91.
KOiK00705.
OMAiTGQLWGT.
PhylomeDBiQ9LV91.

Enzyme and pathway databases

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

Miscellaneous databases

PROiQ9LV91.

Gene expression databases

GenevisibleiQ9LV91. AT.

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.
ProtoNetiSearch...

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: February 17, 2016
This is version 94 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.