PROSITE documentation PDOC00646

Glucoamylase active site region signature

Description

Glucoamylase (GA) (EC 3.2.1.3) is an enzyme that catalyzes the release of D-glucose from the non-reducing ends of starch and other oligo- or polysaccharides. Extensive studies of fungal GA have shown [1,E1] that three closely clustered acidic residues play a role in the catalytic mechanism of GA. The region that includes these residues is also conserved in a recently sequenced bacterial GA [2]. We used this region as a signature pattern.

Note:

These proteins belong to family 15 in the classification of glycosyl hydrolases [3,E1].

Note:

A GA from Schwanniomyces occidentalis is not a member of this family but belongs to family 31 (see <PDOC00120>).

Last update:

July 1998 / Text revised.

Technical section

PROSITE method (with tools and information) covered by this documentation:

GLUCOAMYLASE, PS00820Glucoamylase active site region signature  (PATTERN)
Consensus pattern: [STN]-[GP]-x(1,2)-[DE]-x-W-E-E-x(2)-[GS]
All D/E are active site residues
Sequences known to belong to this class detected by the pattern: ALL
Other sequence(s) detected in Swiss-Prot: 1.
• Retrieve an alignment of Swiss-Prot true positive hits:
  Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format
Retrieve the sequence logo from the alignment
Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00820
Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00820
Scan Swiss-Prot/TrEMBL entries against PS00820
view ligand binding statistics
Matching PDB structures: 1AGM 1AYX 1DOG 1GAH ... [ALL]

References

1 Authors Sierks M.R., Ford C., Reilly P.J., Svensson B.
Title Catalytic mechanism of fungal glucoamylase as defined by mutagenesis of Asp176, Glu179 and Glu180 in the enzyme from Aspergillus awamori.
Source Protein Eng. 3:193-198(1990).
PubMed ID 1970434
2 Authors Ohnishi H., Kitamura H., Minowa T., Sakai H., Ohta T.
Title Molecular cloning of a glucoamylase gene from a thermophilic Clostridium and kinetics of the cloned enzyme.
Source Eur. J. Biochem. 207:413-418(1992).
PubMed ID 1633799
3 Authors Henrissat B.
Title A classification of glycosyl hydrolases based on amino acid sequence similarities.
Source Biochem. J. 280:309-316(1991).
PubMed ID 1747104
E1
Source http://www.cazy.org/fam/GH15.html

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