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Protein

4-alpha-glucanotransferase, chloroplastic/amyloplastic

Gene

DPEP

Organism
Solanum tuberosum (Potato)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

May act during starch breakdown to convert small oligosaccharides into larger molecules upon which starch phosphorylase can act, or may change the structure of starch molecules and grain architecture by modifying chain length, or may generate from starch and glucose oligosaccharides which can serve either as primers for new starch phosphoenzyme.

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

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism

Enzyme and pathway databases

BRENDAi2.4.1.25. 5757.

Protein family/group databases

CAZyiGH77. Glycoside Hydrolase Family 77.

Names & Taxonomyi

Protein namesi
Recommended name:
4-alpha-glucanotransferase, chloroplastic/amyloplastic (EC:2.4.1.25)
Alternative name(s):
Amylomaltase
Disproportionating enzyme
Short name:
D-enzyme
Gene namesi
Name:DPEP
OrganismiSolanum tuberosum (Potato)
Taxonomic identifieri4113 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum
Proteomesi
  • UP000011115 Componenti: Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Amyloplast, Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 52Chloroplast1 PublicationAdd BLAST52
ChainiPRO_000001855053 – 5764-alpha-glucanotransferase, chloroplastic/amyloplasticAdd BLAST524

Proteomic databases

PRIDEiQ06801.

Expressioni

Tissue specificityi

Present in leaves, stems, roots, and stolons but is most abundant in developing and mature tubers.

Interactioni

Protein-protein interaction databases

STRINGi4113.PGSC0003DMT400042739.

Structurei

Secondary structure

1576
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi65 – 67Combined sources3
Helixi74 – 76Combined sources3
Beta strandi79 – 83Combined sources5
Helixi86 – 88Combined sources3
Helixi100 – 112Combined sources13
Beta strandi116 – 118Combined sources3
Beta strandi128 – 130Combined sources3
Beta strandi137 – 139Combined sources3
Beta strandi141 – 143Combined sources3
Helixi146 – 148Combined sources3
Helixi151 – 156Combined sources6
Helixi162 – 164Combined sources3
Turni176 – 178Combined sources3
Helixi179 – 196Combined sources18
Helixi200 – 210Combined sources11
Helixi212 – 231Combined sources20
Helixi236 – 238Combined sources3
Helixi241 – 244Combined sources4
Helixi248 – 257Combined sources10
Helixi259 – 285Combined sources27
Beta strandi289 – 297Combined sources9
Beta strandi300 – 302Combined sources3
Helixi303 – 306Combined sources4
Helixi309 – 311Combined sources3
Beta strandi320 – 326Combined sources7
Beta strandi329 – 333Combined sources5
Helixi345 – 350Combined sources6
Helixi354 – 366Combined sources13
Beta strandi368 – 373Combined sources6
Helixi375 – 378Combined sources4
Beta strandi380 – 385Combined sources6
Beta strandi389 – 393Combined sources5
Beta strandi395 – 398Combined sources4
Helixi402 – 412Combined sources11
Beta strandi416 – 419Combined sources4
Helixi427 – 435Combined sources9
Beta strandi440 – 443Combined sources4
Helixi444 – 446Combined sources3
Beta strandi447 – 450Combined sources4
Helixi458 – 460Combined sources3
Beta strandi463 – 469Combined sources7
Helixi477 – 482Combined sources6
Helixi486 – 495Combined sources10
Helixi501 – 503Combined sources3
Helixi504 – 513Combined sources10
Beta strandi518 – 523Combined sources6
Helixi524 – 527Combined sources4
Helixi532 – 534Combined sources3
Beta strandi542 – 544Combined sources3
Helixi556 – 558Combined sources3
Helixi560 – 572Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1X1NX-ray1.80A53-576[»]
ProteinModelPortaliQ06801.
SMRiQ06801.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ06801.

Family & Domainsi

Sequence similaritiesi

Belongs to the disproportionating enzyme family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410IFXE. Eukaryota.
COG1640. LUCA.
InParanoidiQ06801.
KOiK00705.

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.

Q06801-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIHTCFSLI PSSFSSPKLP YPKNTTFQSP IPKLSRPTFM FDRKGSFQNG
60 70 80 90 100
TAAVPAVGED FPIDYADWLP KRDPNDRRRA GILLHPTSFP GPYGIGDLGP
110 120 130 140 150
QAFKFLDWLH LAGCSLWQVL PLVPPGKRGN EDGSPYSGQD ANCGNTLLIS
160 170 180 190 200
LEELVDDGLL KMEELPEPLP TDRVNYSTIS EIKDPLITKA AKRLLSSEGE
210 220 230 240 250
LKDQLENFRR DPNISSWLED AAYFAAIDNS VNTISWYDWP EPLKNRHLAA
260 270 280 290 300
LEEVYQSEKD FIDIFIAQQF LFQRQWKKVR DYARSKGISI MGDMPIYVGY
310 320 330 340 350
HSADVWANKK QFLLNRKGFP LIVSGVPPDA FSETGQLWGS PLYDWKAMEK
360 370 380 390 400
DGFSWWVRRI QRATDLFDEF RIDHFRGFAG FWAVPSEEKI AILGRWKVGP
410 420 430 440 450
GKPLFDAILQ AVGKINIIAE DLGVITEDVV QLRKSIEAPG MAVLQFAFGS
460 470 480 490 500
DAENPHLPHN HEQNQVVYTG THDNDTIRGW WDTLPQEEKS NVLKYLSNIE
510 520 530 540 550
EEEISRGLIE GAVSSVARIA IIPMQDVLGL GSDSRMNIPA TQFGNWSWRI
560 570
PSSTSFDNLD AEAKKLRDIL ATYGRL
Length:576
Mass (Da):64,951
Last modified:June 1, 1994 - v1
Checksum:iA0D16F3A546307BB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68664 mRNA. Translation: CAA48630.1.
PIRiA45049.
RefSeqiNP_001274781.1. NM_001287852.1.
UniGeneiStu.18047.

Genome annotation databases

GeneIDi102595076.
KEGGisot:102595076.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68664 mRNA. Translation: CAA48630.1.
PIRiA45049.
RefSeqiNP_001274781.1. NM_001287852.1.
UniGeneiStu.18047.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1X1NX-ray1.80A53-576[»]
ProteinModelPortaliQ06801.
SMRiQ06801.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4113.PGSC0003DMT400042739.

Protein family/group databases

CAZyiGH77. Glycoside Hydrolase Family 77.

Proteomic databases

PRIDEiQ06801.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi102595076.
KEGGisot:102595076.

Phylogenomic databases

eggNOGiENOG410IFXE. Eukaryota.
COG1640. LUCA.
InParanoidiQ06801.
KOiK00705.

Enzyme and pathway databases

BRENDAi2.4.1.25. 5757.

Miscellaneous databases

EvolutionaryTraceiQ06801.

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 nameiDPEP_SOLTU
AccessioniPrimary (citable) accession number: Q06801
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 2, 2016
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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.