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InterPro: IPR000322 Glycoside hydrolase, family 31

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1885 proteins

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Accession

IPR000322 Glyco_hydro_31

Type

Family

Signatures Help

Database	ID	Name	Proteins
Pfam	PF01055	Glyco_hydro_31	1793
PROSITE pattern	PS00129	GLYCOSYL_HYDROL_F31_1	504
PROSITE pattern	PS00707	GLYCOSYL_HYDROL_F31_2	142
PANTHER	PTHR22762	Glyco_hydro_31	1861
Signatures in BioMart

InterPro Relationships Help

Contains

IPR017853 Glycoside hydrolase, catalytic core

GO Term annotation Help

Process

GO:0005975 carbohydrate metabolic process

Function

GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds

InterPro annotation

Entry Details in BioMart

Abstract

O-Glycosyl hydrolases EC:3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [1, 2, 3]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site [4]. Because the fold of proteins is better conserved than their sequences, some of the families can be grouped in clans.

Glycoside hydrolase family 31 GH31 comprises enzymes with several known activities; alpha-glucosidase (EC:3.2.1.20), alpha-galactosidase (EC:3.2.1.22); glucoamylase (EC:3.2.1.3), sucrase-isomaltase (EC:3.2.1.48) (EC:3.2.1.10); alpha-xylosidase (EC:3.2.1); alpha-glucan lyase (EC:4.2.2.13).

Glycoside hydrolase family 31 groups a number of glycosyl hydrolases on the basis of sequence similarities [5, 6, 7] An aspartic acid has been implicated [8] in the catalytic activity of sucrase, isomaltase, and lysosomal alpha-glucosidase.

Structural links Help

PDB - click here

SCOP: b.150.1.1 , b.30.5.11 , b.71.1.4 , c.1.8.13

Database links Help

PDBe-motif: PS00129 , PS00707

Enzyme: EC:3.2.1

CAZy: GH31

PROSITE doc: PDOC00120

PANDIT: PF01055

Blocks: IPB000322

Pfam Clan: CL0058.12

Taxonomic coverage Help

Example proteins Help

O43451 Maltase-glucoamylase, intestinal

P38138 Glucosidase 2 subunit alpha

P70699 Lysosomal alpha-glucosidase

Q653V7 Probable alpha-glucosidase Os06g0675700

Q9S7Y7 Alpha-xylosidase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR000519	P-type trefoil
IPR017957	P-type trefoil, conserved site
IPR000322	Glycoside hydrolase, family 31
IPR017853	Glycoside hydrolase, catalytic core
	SWISS-MODEL
	PDB Chain
	ModBase

Publications Open in usermanual
1.	Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon JP, Davies G. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc. Natl. Acad. Sci. U.S.A. 92 7090-4 1995 [PubMed: 7624375] http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=7624375&action=stream&blobtype=pdf
2.	Davies G, Henrissat B. Structures and mechanisms of glycosyl hydrolases. Structure 3 853-9 1995 [PubMed: 8535779] http://dx.doi.org/10.1016/S0969-2126(01)00220-9
3.	Bairoch A. Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT. 1999
4.	Henrissat B, Coutinho PM. Carbohydrate-Active Enzymes server. 1999
5.	Henrissat B. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 280 ( Pt 2) 309-16 1991 [PubMed: 1747104] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=1747104
6.	Kinsella BT, Hogan S, Larkin A, Cantwell BA. Primary structure and processing of the Candida tsukubaensis alpha-glucosidase. Homology with the rabbit intestinal sucrase-isomaltase complex and human lysosomal alpha-glucosidase. Eur. J. Biochem. 202 657-64 1991 [PubMed: 1761061] http://dx.doi.org/10.1111/j.1432-1033.1991.tb16420.x
7.	Naim HY, Niermann T, Kleinhans U, Hollenberg CP, Strasser AW. 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. FEBS Lett. 294 109-12 1991 [PubMed: 1743281] http://dx.doi.org/10.1016/0014-5793(91)81353-A
8.	Hermans MM, Kroos MA, van Beeumen J, Oostra BA, Reuser AJ. Human lysosomal alpha-glucosidase. Characterization of the catalytic site. J. Biol. Chem. 266 13507-12 1991 [PubMed: 1856189] http://intl.jbc.org/cgi/reprint/266/21/13507.pdf

Additional Reading Open in usermanual
	Lovering AL, Lee SS, Kim YW, Withers SG, Strynadka NC. Mechanistic and structural analysis of a family 31 alpha-glycosidase and its glycosyl-enzyme intermediate. J. Biol. Chem. 280 2005 2105-15 [PubMed: 15501829] http://dx.doi.org/10.1074/jbc.M410468200
	Henrissat B. Glycosidase families. Biochem. Soc. Trans. 26 1998 153-6 [PubMed: 9649738] http://www.biochemsoctrans.org/bst/026/0153/0260153.pdf
	Kim YW, Lovering AL, Chen H, Kantner T, McIntosh LP, Strynadka NC, Withers SG. Expanding the thioglycoligase strategy to the synthesis of alpha-linked thioglycosides allows structural investigation of the parent enzyme/substrate complex. J. Am. Chem. Soc. 128 2006 2202-3 [PubMed: 16478160] http://dx.doi.org/10.1021/ja057904a

InterPro 23.1