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InterPro: IPR011682 Glycosyl hydrolases 38, C-terminal

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942 proteins

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Accession

IPR011682 Glyco_hydro_38_C

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF07748	Glyco_hydro_38C	942
Signatures in BioMart

InterPro Relationships Help

Parent

IPR011013 Glycoside hydrolase-type carbohydrate-binding

GO Term annotation Help

Process

GO:0006013 mannose metabolic process

Function

GO:0015923 mannosidase activity

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 38 GH38 comprises enzymes with only one known activity; alpha-mannosidase (EC:3.2.1.24) (EC:3.2.1.114). This domain is found at the C terminus of glycosyl hydrolases from family 38.

Structural links Help

PDB - click here

SCOP: b.30.5.6

CATH: 2.60.40.1180 , 2.60.40.1360 , 2.70.98.30

Database links Help

Enzyme: EC:3.2.1

PANDIT: PF07748

Pfam Clan: CL0103.8

Taxonomic coverage Help

Example proteins Help

O00754 Lysosomal alpha-mannosidase

O09159 Lysosomal alpha-mannosidase

P22855 Alpha-mannosidase

P54746 Alpha-mannosidase mngB

Q24451 Alpha-mannosidase 2

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR013780	Glycosyl hydrolase, family 13, all-beta
IPR011682	Glycosyl hydrolases 38, C-terminal
IPR015341	Glycoside hydrolase, family 38, central domain
IPR011330	Glycoside hydrolase/deacetylase, beta/alpha-barrel
IPR011013	Glycoside hydrolase-type carbohydrate-binding
IPR000602	Glycoside hydrolase, family 38, core
	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

Additional Reading Open in usermanual
	Kuntz DA, Tarling CA, Withers SG, Rose DR. Structural analysis of Golgi alpha-mannosidase II inhibitors identified from a focused glycosidase inhibitor screen. Biochemistry 47 2008 10058-68 [PubMed: 18759458] http://dx.doi.org/10.1021/bi8010785
	Zhong W, Kuntz DA, Ember B, Singh H, Moremen KW, Rose DR, Boons GJ. Probing the substrate specificity of Golgi alpha-mannosidase II by use of synthetic oligosaccharides and a catalytic nucleophile mutant. J. Am. Chem. Soc. 130 2008 8975-83 [PubMed: 18558690] http://dx.doi.org/10.1021/ja711248y
	Kumar NS, Kuntz DA, Wen X, Pinto BM, Rose DR. Binding of sulfonium-ion analogues of di-epi-swainsonine and 8-epi-lentiginosine to Drosophila Golgi alpha-mannosidase II: the role of water in inhibitor binding. Proteins 71 2008 1484-96 [PubMed: 18076078] http://dx.doi.org/10.1002/prot.21850
	Henrissat B. Glycosidase families. Biochem. Soc. Trans. 26 1998 153-6 [PubMed: 9649738] http://www.biochemsoctrans.org/bst/026/0153/0260153.pdf
	Shah N, Kuntz DA, Rose DR. Golgi alpha-mannosidase II cleaves two sugars sequentially in the same catalytic site. Proc. Natl. Acad. Sci. U.S.A. 105 2008 9570-5 [PubMed: 18599462] http://dx.doi.org/10.1073/pnas.0802206105
	Fiaux H, Kuntz DA, Hoffman D, Janzer RC, Gerber-Lemaire S, Rose DR, Juillerat-Jeanneret L. Functionalized pyrrolidine inhibitors of human type II alpha-mannosidases as anti-cancer agents: optimizing the fit to the active site. Bioorg. Med. Chem. 16 2008 7337-46 [PubMed: 18599296] http://dx.doi.org/10.1016/j.bmc.2008.06.021

InterPro 23.1