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InterPro: IPR006047 Glycosyl hydrolase, family 13, catalytic domain

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UniProtKB

Matches:

10738 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR006047 Glyco_hydro_13_cat_dom

Secondary

IPR000461

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00128	Alpha-amylase	10738
Signatures in BioMart

InterPro Relationships Help

Parent

IPR013781 Glycoside hydrolase, subgroup, catalytic core

Children

IPR006589 Glycosyl hydrolase, family 13, subfamily, catalytic domain

Found in

IPR006407 1,4-alpha-glucan branching enzyme, core region
IPR011837 Glycogen debranching enzyme GlgX
IPR011838 Pullulanase, extracellular
IPR011839 Alpha-1,6-glucosidases, pullulanase-type
IPR011840 Pullulanase, type I
IPR012767 Malto-oligosyltrehalose synthase
IPR012768 Malto-oligosyltrehalose trehalohydrolase
IPR013776 Alpha-amylase, thermostable
IPR016377 Sucrose phosphorylase

GO Term annotation Help

Process

GO:0005975 carbohydrate metabolic process

Function

GO:0003824 catalytic activity
GO:0043169 cation binding

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.

Enzymes containing this domain, such as alpha-amylase, belong to family 13 (GH13) of the glycosyl hydrolases. The maltogenic alpha-amylase is an enzyme which catalyses hydrolysis of (1-4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive alpha-maltose residues from the non-reducing ends of the chains in the conversion of starch to maltose. Other enzymes include neopullulanase, which hydrolyses pullulan to panose, and cyclomaltodextrinase, which hydrolyses cyclodextrins.

This entry represents the catalytic domain found in several protein members of this family. It has a structure consisting of an 8 stranded alpha/beta barrel that contains the active site, interrupted by a ~70 amino acid calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain [5].

More information about this protein can be found at Protein of the Month: alpha-Amylase [6].

Structural links Help

PDB - click here

SCOP: b.71.1.1 , c.1.8.1

CATH: 2.60.40.1180 , 3.20.20.80 , 3.30.1590.10 , 3.90.400.10

Database links Help

CAZy: GH13

PANDIT: PF00128

Pfam Clan: CL0058.12

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR006047

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O04196 Isoamylase 1, chloroplastic

O18408 Alpha-amylase-related protein

P00687 Alpha-amylase 1

P04745 Alpha-amylase 1

P07265 Alpha-glucosidase MAL62

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR013781	Glycoside hydrolase, subgroup, catalytic core
IPR013780	Glycosyl hydrolase, family 13, all-beta
IPR013783	Immunoglobulin-like fold
IPR006589	Glycosyl hydrolase, family 13, subfamily, catalytic domain
IPR006046	Glycoside hydrolase family 13
IPR006047	Glycosyl hydrolase, family 13, catalytic domain
IPR006048	Alpha-amylase, C-terminal all beta
IPR014756	Immunoglobulin E-set
IPR004193	Glycoside hydrolase, family 13, N-terminal
IPR017853	Glycoside hydrolase, catalytic core
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP 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.	Abe A, Yoshida H, Tonozuka T, Sakano Y, Kamitori S. Complexes of Thermoactinomyces vulgaris R-47 alpha-amylase 1 and pullulan model oligossacharides provide new insight into the mechanism for recognizing substrates with alpha-(1,6) glycosidic linkages. FEBS J. 272 6145-53 2005 [PubMed: 16302977] http://dx.doi.org/10.1111/j.1742-4658.2005.05013.x
6.	McDowall J. Protein of the Month ? alpha-Amylase. 2006

Additional Reading Open in usermanual
	Larson SB, Greenwood A, Cascio D, Day J, McPherson A. Refined molecular structure of pig pancreatic alpha-amylase at 2.1 A resolution. J. Mol. Biol. 235 1994 1560-84 [PubMed: 8107092] http://dx.doi.org/10.1006/jmbi.1994.1107
	Maurus R, Begum A, Williams LK, Fredriksen JR, Zhang R, Withers SG, Brayer GD. Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity. Biochemistry 47 2008 3332-44 [PubMed: 18284212] http://dx.doi.org/10.1021/bi701652t
	Strobl S, Maskos K, Betz M, Wiegand G, Huber R, Gomis-Ruth FX, Glockshuber R. Crystal structure of yellow meal worm alpha-amylase at 1.64 A resolution. J. Mol. Biol. 278 1998 617-28 [PubMed: 9600843] http://dx.doi.org/10.1006/jmbi.1998.1667
	Kelly RM, Leemhuis H, Rozeboom HJ, van Oosterwijk N, Dijkstra BW, Dijkhuizen L. Elimination of competing hydrolysis and coupling side reactions of a cyclodextrin glucanotransferase by directed evolution. Biochem. J. 413 2008 517-25 [PubMed: 18422488] http://dx.doi.org/10.1042/BJ20080353
	Bozonnet S, Jensen MT, Nielsen MM, Aghajari N, Jensen MH, Kramhoft B, Willemoes M, Tranier S, Haser R, Svensson B. The 'pair of sugar tongs' site on the non-catalytic domain C of barley alpha-amylase participates in substrate binding and activity. FEBS J. 274 2007 5055-67 [PubMed: 17803687] http://dx.doi.org/10.1111/j.1742-4658.2007.06024.x
	Nielsen MM, Seo ES, Bozonnet S, Aghajari N, Robert X, Haser R, Svensson B. Multi-site substrate binding and interplay in barley alpha-amylase 1. FEBS Lett. 582 2008 2567-71 [PubMed: 18588886] http://dx.doi.org/10.1016/j.febslet.2008.06.027
	Ravaud S, Robert X, Watzlawick H, Haser R, Mattes R, Aghajari N. Trehalulose synthase native and carbohydrate complexed structures provide insights into sucrose isomerization. J. Biol. Chem. 282 2007 28126-36 [PubMed: 17597061] http://dx.doi.org/10.1074/jbc.M704515200

InterPro 23.1