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It has been shown [1,2,3,E1] that the following glycosyl hydrolases can be, on the basis of sequence similarities, classified into a single family:

• Lysosomal α-glucosidase (EC 3.2.1.20) (acid maltase) is a vertebrate glycosidase active at low pH, which hydrolyzes α(1->4) and α(1->6) linkages in glycogen, maltose, and isomaltose.
• α-glucosidase (EC 3.2.1.20) from the yeast Candida tsukunbaensis.
• α-glucosidase (EC 3.2.1.20) (gene malA) from the archebacteria Sulfolobus solfataricus.
• Intestinal sucrase-isomaltase (EC 3.2.1.48 / EC 3.2.1.10) is a vertebrate membrane-bound, multifunctional enzyme complex which hydrolyzes sucrose, maltose and isomaltose. The sucrase and isomaltase domains of the enzyme are homologous (41% of amino acid identity) and have most probably evolved by duplication.
• Glucoamylase 1 (EC 3.2.1.3) (glucan 1,4-α-glucosidase) from various fungal species.
• Yeast hypothetical protein YBR229c.
• Fission yeast hypothetical protein SpAC30D11.01c.

An aspartic acid has been implicated [4] in the catalytic activity of sucrase, isomaltase, and lysosomal α-glucosidase. The region around this active residue is highly conserved and can be used as a signature pattern. We have used a second region, which contains two conserved cysteines, as an additional signature pattern.

Henrissat B.

April 2006 / Pattern revised.

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

GLYCOSYL_HYDROL_F31_1, PS00129; Glycosyl hydrolases family 31 active site  (PATTERN)

Consensus pattern: [GFY]-[LIVMF]-W-x-D-M-[NSA]-E D is the active site residue Sequences known to belong to this class detected by the pattern: ALL, except for SpAC30D11.01c Other sequence(s) detected in Swiss-Prot: NONE.

• 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 PS00129 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00129 • Scan Swiss-Prot/TrEMBL entries against PS00129 • view ligand binding statistics

Matching PDB structures: 2G3M 2G3N 2QLY 2QMJ ... [ALL]

GLYCOSYL_HYDROL_F31_2, PS00707; Glycosyl hydrolases family 31 signature 2  (PATTERN)

Consensus pattern: G-[AVP]-[DT]-[LIVMTAS]-[CG]-G-[FY]-x(3)-[STP]-x(3)-L-[CL]-x-R-W-x(2)-[LVMI]-[GSA]-[SA]-[FY]-x-P-[FY]-x-R-[DNA] Sequences known to belong to this class detected by the pattern: ALL, except for YBR229c which lacks the two cysteines, rat sucrase-isomaltase and malA Other sequence(s) detected in Swiss-Prot: NONE.

• 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 PS00707 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00707 • Scan Swiss-Prot/TrEMBL entries against PS00707 • view ligand binding statistics

Matching PDB structures: 2QLY 2QMJ 3CTT 3L4T ... [ALL]

1	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

2	Authors	Kinsella B.T., Hogan S., Larkin A., Cantwell B.A.
	Title	Primary structure and processing of the Candida tsukubaensis alpha-glucosidase. Homology with the rabbit intestinal sucrase-isomaltase complex and human lysosomal alpha-glucosidase.
	Source	Eur. J. Biochem. 202:657-664(1991).
	PubMed ID	1761061

3	Authors	Naim H.Y., Niermann T., Kleinhans U., Hollenberg C.P., Strasser A.W.M.
	Title	Striking structural and functional similarities suggest that intestinal sucrase-isomaltase, human lysosomal alpha-glucosidase and Schwanniomyces occidentalis glucoamylase are derived from a common ancestral gene.
	Source	FEBS Lett. 294:109-112(1991).
	PubMed ID	1743281

4	Authors	Hermans M.M.P., Kroos M.A., van Beeumen J., Oostra B.A., Reuser A.J.
	Title	Human lysosomal alpha-glucosidase. Characterization of the catalytic site.
	Source	J. Biol. Chem. 266:13507-13512(1991).
	PubMed ID	1856189

E1
Source	http://www.uniprot.org/docs/glycosid

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