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O87172 (MALQ_THETH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
4-alpha-glucanotransferase

EC=2.4.1.25
Alternative name(s):
Amylomaltase
Disproportionating enzyme
Short name=D-enzyme
Gene names
Name:malQ
OrganismThermus thermophilus
Taxonomic identifier274 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length500 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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

Cytoplasm By similarity.

Sequence similarities

Belongs to the disproportionating enzyme family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentCytoplasm
   Molecular functionGlycosyltransferase
Transferase
   Technical term3D-structure
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function4-alpha-glucanotransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5005004-alpha-glucanotransferase
PRO_0000170132

Secondary structure

......................................................................................... 500
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O87172 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 6E7175A38E0A5D61

FASTA50057,222
        10         20         30         40         50         60 
MELPRAFGLL LHPTSLPGPY GVGVLGREAR DFLRFLKEAG GRYWQVLPLG PTGYGDSPYQ 

        70         80         90        100        110        120 
SFSAFAGNPY LIDLRPLAER GYVRLEDPGF PQGRVDYGLL YAWKWPALKE AFRGFKEKAS 

       130        140        150        160        170        180 
PEEREAFAAF REREAWWLED YALFMALKGA HGGLPWNRWP LPLRKREEKA LREAKSALAE 

       190        200        210        220        230        240 
EVAFHAFTQW LFFRQWGALK AEAEALGIRI IGDMPIFVAE DSAEVWAHPE WFHLDEEGRP 

       250        260        270        280        290        300 
TVVAGVPPDY FSETGQRWGN PLYRWDVLER EGFSFWIRRL EKALELFHLV RIDHFRGFEA 

       310        320        330        340        350        360 
YWEIPASCPT AVEGRWVKAP GEKLFQKIQE VFGEVPVLAE DLGVITPEVE ALRDRFGLPG 

       370        380        390        400        410        420 
MKVLQFAFDD GMENPFLPHN YPAHGRVVVY TGTHDNDTTL GWYRTATPHE KAFMARYLAD 

       430        440        450        460        470        480 
WGITFREEEE VPWALMHLGM KSVARLAVYP VQDVLALGSE ARMNYPGRPS GNWAWRLLPG 

       490        500 
ELSPEHGARL RAMAEATERL 

« Hide

References

[1]"Cloning, expression and characterization of amylomaltase from Thermus aquaticus ATCC33923."
Terada Y., Fujii K., Takaha T., Okada S.
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 33923 / DSM 674 / AT-62.
[2]"Crystal structure of amylomaltase from Thermus aquaticus, a glycosyltransferase catalysing the production of large cyclic glucans."
Przylas I., Tomoo K., Terada Y., Takaha T., Fujii K., Saenger W., Strater N.
J. Mol. Biol. 296:873-886(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB016244 Genomic DNA. Translation: BAA33728.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CWYX-ray2.00A1-500[»]
1ESWX-ray1.90A1-500[»]
1FP8X-ray2.30A1-500[»]
1FP9X-ray3.10A1-500[»]
2OWCX-ray2.05A1-500[»]
2OWWX-ray2.20A1-500[»]
2OWXX-ray2.50A1-500[»]
ProteinModelPortalO87172.
SMRO87172. Positions 1-500.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING262724.TTC0897.

Protein family/group databases

CAZyGH77. Glycoside Hydrolase Family 77.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR003385. Glyco_hydro_77.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF02446. Glyco_hydro_77. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
TIGRFAMsTIGR00217. malQ. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceO87172.

Entry information

Entry nameMALQ_THETH
AccessionPrimary (citable) accession number: O87172
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references