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Reviewed, UniProtKB/Swiss-Prot O87172 (MALQ_THETH)

Last modified June 16, 2009. Version 56. 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
    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 lineageBacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus

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Protein attributes

Sequence length500 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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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.

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Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

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

Chain1 – 5005004-alpha-glucanotransferase
PRO_0000170132

Secondary structure

1 ...................................................................................... 500
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
O87172-1 [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

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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: 10677288] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+Additional computationally mapped references.

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Cross-references

Sequence databases

AB016244 Genomic DNA. Translation: BAA33728.1.

3D structure databases

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[»]
ModBaseSearch...

Protein family/group databases

CAZyGH77. Glycoside Hydrolase Family 77.

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 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: June 16, 2009
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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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