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InterPro: IPR001382 Glycoside hydrolase, family 47

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850 proteins

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Accession

IPR001382 Glyco_hydro_47

Type

Family

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:1.50.10.50	Glyco_hydro_47	749
Pfam	PF01532	Glyco_hydro_47	741
PRINTS	PR00747	GLYHDRLASE47	713
PANTHER	PTHR11742	Glyco_hydro_47	829
SuperFamily	SSF48225	Glyco_hydro_47	758
Signatures in BioMart

GO Term annotation Help

Function

GO:0004571 mannosyl-oligosaccharide 1,2-alpha-mannosidase activity
GO:0005509 calcium ion binding

Component

GO:0016020 membrane

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 47 GH47 comprises enzymes with only one known activity; alpha-mannosidase (EC:3.2.1.113).

Alpha-mannosidase is involved in the maturation of Asn-linked oligo-saccharides [5]. The enzyme hydrolyses terminal 1,2-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide man(9)(glcnac)(2) in a calcium-dependent manner. The mannose residues are trimmed away to produce, first, man(8)glcnac(2), then a man(5)(glcnac)(2) structure.

Structural links Help

PDB - click here

SCOP: a.102.2.1

CATH: 1.50.10.50

Database links Help

CAZy: GH47

PANDIT: PF01532

Blocks: IPB001382

Taxonomic coverage Help

Example proteins Help

P32906 Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase

P45700 Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA

P53624 Mannosyl-oligosaccharide alpha-1,2-mannosidase isoform A

Q18788 Mannosyl-oligosaccharide 1,2-alpha-mannosidase C52E4.5

Q9UKM7 Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR001382	Glycoside hydrolase, family 47
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

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.	Lal A, Schutzbach JS, Forsee WT, Neame PJ, Moremen KW. Isolation and expression of murine and rabbit cDNAs encoding an alpha 1,2-mannosidase involved in the processing of asparagine-linked oligosaccharides. J. Biol. Chem. 269 9872-81 1994 [PubMed: 8144580] http://intl.jbc.org/cgi/content/abstract/269/13/9872

Additional Reading Open in usermanual
	Lobsanov YD, Yoshida T, Desmet T, Nerinckx W, Yip P, Claeyssens M, Herscovics A, Howell PL. Modulation of activity by Arg407: structure of a fungal alpha-1,2-mannosidase in complex with a substrate analogue. Acta Crystallogr. D Biol. Crystallogr. 64 2008 227-36 [PubMed: 18323617] http://dx.doi.org/10.1107/S0907444907065572
	Tempel W, Karaveg K, Liu ZJ, Rose J, Wang BC, Moremen KW. Structure of mouse Golgi alpha-mannosidase IA reveals the molecular basis for substrate specificity among class 1 (family 47 glycosylhydrolase) alpha1,2-mannosidases. J. Biol. Chem. 279 2004 29774-86 [PubMed: 15102839] http://dx.doi.org/10.1074/jbc.M403065200
	Karaveg K, Siriwardena A, Tempel W, Liu ZJ, Glushka J, Wang BC, Moremen KW. Mechanism of class 1 (glycosylhydrolase family 47) {alpha}-mannosidases involved in N-glycan processing and endoplasmic reticulum quality control. J. Biol. Chem. 280 2005 16197-207 [PubMed: 15713668] http://dx.doi.org/10.1074/jbc.M500119200
	Van Petegem F, Contreras H, Contreras R, Van Beeumen J. Trichoderma reesei alpha-1,2-mannosidase: structural basis for the cleavage of four consecutive mannose residues. J. Mol. Biol. 312 2001 157-65 [PubMed: 11545593] http://dx.doi.org/10.1006/jmbi.2001.4946
	Lobsanov YD, Vallee F, Imberty A, Yoshida T, Yip P, Herscovics A, Howell PL. Structure of Penicillium citrinum alpha 1,2-mannosidase reveals the basis for differences in specificity of the endoplasmic reticulum and Golgi class I enzymes. J. Biol. Chem. 277 2002 5620-30 [PubMed: 11714724] http://dx.doi.org/10.1074/jbc.M110243200

InterPro 23.1