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InterPro: IPR015341 Glycoside hydrolase, family 38, central domain

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886 proteins

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Accession List
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Accession

IPR015341 Glyco_hydro_38_cen_dom

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF09261	Alpha-mann_mid	653
SMART	SM00872	Alpha-mann_mid	865
Signatures in BioMart

GO Term annotation Help

Function

GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008270 zinc ion binding

InterPro annotation

Entry Details in BioMart

Abstract

Members of this entry belong to the glycosyl hydrolase family 38, This domain, which is found in the central region adopts a structure consisting of three alpha helices, in an immunoglobulin/albumin-binding domain-like fold. The domain is predominantly found in the enzyme alpha-mannosidase [1].

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PDB - click here

SCOP: a.8.3.1

CATH: 1.10.287.530 , 1.20.1270.50

Database links Help

Enzyme: EC:3.2.1

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.	Heikinheimo P, Helland R, Leiros HK, Leiros I, Karlsen S, Evjen G, Ravelli R, Schoehn G, Ruigrok R, Tollersrud OK, McSweeney S, Hough E. The structure of bovine lysosomal alpha-mannosidase suggests a novel mechanism for low-pH activation. J. Mol. Biol. 327 631-44 2003 [PubMed: 12634058] http://dx.doi.org/10.1016/S0022-2836(03)00172-4

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
	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