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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: 4 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
  • 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)DescriptionActionsGraphical viewLength
Transit peptidei1 – 45ChloroplastSequence analysisAdd BLAST45
ChainiPRO_000040791846 – 5764-alpha-glucanotransferase DPE1, chloroplastic/amyloplasticAdd BLAST531

Proteomic databases

PaxDbiQ9LV91.

PTM databases

iPTMnetiQ9LV91.

Expressioni

Gene expression databases

GenevisibleiQ9LV91. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT5G64860.1.

Structurei

Secondary structure

1576
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi69 – 71Combined sources3
Helixi78 – 80Combined sources3
Beta strandi83 – 87Combined sources5
Helixi90 – 92Combined sources3
Beta strandi96 – 99Combined sources4
Helixi104 – 116Combined sources13
Beta strandi120 – 122Combined sources3
Helixi135 – 137Combined sources3
Beta strandi141 – 143Combined sources3
Helixi146 – 148Combined sources3
Helixi151 – 156Combined sources6
Helixi162 – 164Combined sources3
Helixi176 – 196Combined sources21
Helixi200 – 210Combined sources11
Helixi212 – 230Combined sources19
Helixi236 – 238Combined sources3
Helixi241 – 244Combined sources4
Helixi248 – 257Combined sources10
Helixi259 – 285Combined sources27
Beta strandi289 – 297Combined sources9
Beta strandi300 – 302Combined sources3
Helixi303 – 306Combined sources4
Helixi307 – 311Combined sources5
Beta strandi320 – 326Combined sources7
Beta strandi332 – 334Combined sources3
Beta strandi336 – 341Combined sources6
Helixi345 – 349Combined sources5
Turni350 – 353Combined sources4
Helixi354 – 366Combined sources13
Beta strandi368 – 373Combined sources6
Helixi375 – 378Combined sources4
Beta strandi380 – 385Combined sources6
Helixi391 – 393Combined sources3
Beta strandi395 – 398Combined sources4
Helixi402 – 412Combined sources11
Beta strandi417 – 419Combined sources3
Helixi427 – 436Combined sources10
Beta strandi440 – 443Combined sources4
Helixi444 – 446Combined sources3
Beta strandi449 – 451Combined sources3
Helixi458 – 460Combined sources3
Beta strandi463 – 469Combined sources7
Helixi477 – 483Combined sources7
Helixi486 – 495Combined sources10
Helixi501 – 503Combined sources3
Helixi504 – 514Combined sources11
Beta strandi518 – 523Combined sources6
Helixi524 – 527Combined sources4
Helixi532 – 534Combined sources3
Helixi556 – 558Combined sources3
Helixi560 – 572Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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.
OMAiEARMNFP.
OrthoDBiEOG093606B7.
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_125884.4.
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_125884.4.
UniGeneiAt.7845.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT5G64860.1.

Protein family/group databases

CAZyiGH77. Glycoside Hydrolase Family 77.

PTM databases

iPTMnetiQ9LV91.

Proteomic databases

PaxDbiQ9LV91.

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.
OMAiEARMNFP.
OrthoDBiEOG093606B7.
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...

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: November 30, 2016
This is version 100 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.