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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
ProteomesiUP000011115 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)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5252Chloroplast1 PublicationAdd
BLAST
Chaini53 – 5765244-alpha-glucanotransferase, chloroplastic/amyloplasticPRO_0000018550Add
BLAST

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

1
576
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi65 – 673Combined sources
Helixi74 – 763Combined sources
Beta strandi79 – 835Combined sources
Helixi86 – 883Combined sources
Helixi100 – 11213Combined sources
Beta strandi116 – 1183Combined sources
Beta strandi128 – 1303Combined sources
Beta strandi137 – 1393Combined sources
Beta strandi141 – 1433Combined sources
Helixi146 – 1483Combined sources
Helixi151 – 1566Combined sources
Helixi162 – 1643Combined sources
Turni176 – 1783Combined sources
Helixi179 – 19618Combined sources
Helixi200 – 21011Combined sources
Helixi212 – 23120Combined sources
Helixi236 – 2383Combined sources
Helixi241 – 2444Combined sources
Helixi248 – 25710Combined sources
Helixi259 – 28527Combined sources
Beta strandi289 – 2979Combined sources
Beta strandi300 – 3023Combined sources
Helixi303 – 3064Combined sources
Helixi309 – 3113Combined sources
Beta strandi320 – 3267Combined sources
Beta strandi329 – 3335Combined sources
Helixi345 – 3506Combined sources
Helixi354 – 36613Combined sources
Beta strandi368 – 3736Combined sources
Helixi375 – 3784Combined sources
Beta strandi380 – 3856Combined sources
Beta strandi389 – 3935Combined sources
Beta strandi395 – 3984Combined sources
Helixi402 – 41211Combined sources
Beta strandi416 – 4194Combined sources
Helixi427 – 4359Combined sources
Beta strandi440 – 4434Combined sources
Helixi444 – 4463Combined sources
Beta strandi447 – 4504Combined sources
Helixi458 – 4603Combined sources
Beta strandi463 – 4697Combined sources
Helixi477 – 4826Combined sources
Helixi486 – 49510Combined sources
Helixi501 – 5033Combined sources
Helixi504 – 51310Combined sources
Beta strandi518 – 5236Combined sources
Helixi524 – 5274Combined sources
Helixi532 – 5343Combined sources
Beta strandi542 – 5443Combined sources
Helixi556 – 5583Combined sources
Helixi560 – 57213Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X1NX-ray1.80A53-576[»]
ProteinModelPortaliQ06801.
SMRiQ06801. Positions 54-576.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ06801.

Family & Domainsi

Sequence similaritiesi

Belongs to the disproportionating enzyme family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1X1NX-ray1.80A53-576[»]
ProteinModelPortaliQ06801.
SMRiQ06801. Positions 54-576.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4113.PGSC0003DMT400042739.

Protein family/group databases

CAZyiGH77. Glycoside Hydrolase Family 77.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi102595076.
KEGGisot:102595076.

Phylogenomic databases

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...

Publicationsi

  1. "Disproportionating enzyme (4-alpha-glucanotransferase; EC 2.4.1.25) of potato. Purification, molecular cloning, and potential role in starch metabolism."
    Takaha T., Yanase M., Okada S., Smith S.M.
    J. Biol. Chem. 268:1391-1396(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 53-57; 174-183 AND 247-259.
    Strain: cv. May Queen.
    Tissue: Tuber.
  2. "Structure determination and refinement at 1.8 A resolution of disproportionating enzyme from potato."
    Imamura K., Matsuura T., Takaha T., Fujii K., Nakagawa A., Kusunoki M., Nitta Y.
    Submitted (APR-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 53-576.

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: June 24, 2015
This is version 84 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

External Data

Dasty 3

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 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.