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Reviewed, UniProtKB/Swiss-Prot Q06801 (DPEP_SOLTU)

Last modified June 16, 2009. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    4-alpha-glucanotransferase, chloroplastic/amyloplastic
    EC=2.4.1.25
Alternative name(s):
    Amylomaltase
    Disproportionating enzyme
      Short name=D-enzyme
Gene names
Name: DPEP
OrganismSolanum tuberosum (Potato)
Taxonomic identifier4113 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum

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Protein attributes

Sequence length576 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

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 activity

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.

Subcellular location

Plastid › chloroplast. Plastid › amyloplast.

Tissue specificity

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

Sequence similarities

Belongs to the disproportionating enzyme family.

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Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentAmyloplast
Chloroplast
Plastid
   DomainTransit peptide
   Molecular functionGlycosyltransferase
Transferase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentamyloplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

chloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function4-alpha-glucanotransferase activity

Inferred from electronic annotation. Source: EC

cation binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5252Chloroplast Ref.1
Chain53 – 5765244-alpha-glucanotransferase, chloroplastic/amyloplastic
PRO_0000018550

Secondary structure

1 ................................................................................................. 576
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q06801-1 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: A0D16F3A546307BB

FASTA57664,951
        10         20         30         40         50         60 
MAIHTCFSLI PSSFSSPKLP YPKNTTFQSP IPKLSRPTFM FDRKGSFQNG TAAVPAVGED 

        70         80         90        100        110        120 
FPIDYADWLP KRDPNDRRRA GILLHPTSFP GPYGIGDLGP QAFKFLDWLH LAGCSLWQVL 

       130        140        150        160        170        180 
PLVPPGKRGN EDGSPYSGQD ANCGNTLLIS LEELVDDGLL KMEELPEPLP TDRVNYSTIS 

       190        200        210        220        230        240 
EIKDPLITKA AKRLLSSEGE LKDQLENFRR DPNISSWLED AAYFAAIDNS VNTISWYDWP 

       250        260        270        280        290        300 
EPLKNRHLAA LEEVYQSEKD FIDIFIAQQF LFQRQWKKVR DYARSKGISI MGDMPIYVGY 

       310        320        330        340        350        360 
HSADVWANKK QFLLNRKGFP LIVSGVPPDA FSETGQLWGS PLYDWKAMEK DGFSWWVRRI 

       370        380        390        400        410        420 
QRATDLFDEF RIDHFRGFAG FWAVPSEEKI AILGRWKVGP GKPLFDAILQ AVGKINIIAE 

       430        440        450        460        470        480 
DLGVITEDVV QLRKSIEAPG MAVLQFAFGS DAENPHLPHN HEQNQVVYTG THDNDTIRGW 

       490        500        510        520        530        540 
WDTLPQEEKS NVLKYLSNIE EEEISRGLIE GAVSSVARIA IIPMQDVLGL GSDSRMNIPA 

       550        560        570 
TQFGNWSWRI PSSTSFDNLD AEAKKLRDIL ATYGRL

« Hide

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References

[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: 7678257] [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.

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Cross-references

Sequence databases

X68664 mRNA. Translation: CAA48630.1.
PIRA45049.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1X1NX-ray1.80A53-576[»]
ModBaseSearch...

Protein family/group databases

CAZyGH77. Glycoside Hydrolase Family 77.

Enzyme and pathway databases

BRENDA2.4.1.25. 296.

Family and domain databases

InterProIPR003385. Glyco_hydro_77.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF02446. Glyco_hydro_77. 1 hit.
[Graphical view]
TIGRFAMsTIGR00217. malQ. 1 hit.
ProtoNetSearch...

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Entry information

Entry nameDPEP_SOLTU
AccessionPrimary (citable) accession number: Q06801
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: June 16, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents