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InterPro: IPR013780 Glycosyl hydrolase, family 13, all-beta

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UniProtKB

Matches:

4263 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
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
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Accession

IPR013780 Glyco_hydro_13_b

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:2.60.40.1180	Glyco_hydro_13_b	4263
Signatures in BioMart

InterPro Relationships Help

Children

IPR006048 Alpha-amylase, C-terminal all beta
IPR015156 Malto-oligosyltrehalose trehalohydrolase, C-terminal
IPR015165 Domain of unknown function DUF1921
IPR015167 Domain of unknown function DUF1923
IPR015261 4-alpha-glucanotransferase, C-terminal
IPR015279 Malto-oligosyltrehalose synthase, C-terminal
IPR015340 Alpha-amylase, domain of unknown function DUF1966, C-terminal
IPR019492 Cyclo-malto-dextrinase, C-terminal

Found in

IPR011837 Glycogen debranching enzyme GlgX
IPR011840 Pullulanase, type I
IPR012769 Alpha,alpha-phosphotrehalase
IPR012810 Trehalose synthase/alpha-amylase, N-terminal
IPR013777 Alpha-amylase, fungi

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.

This entry represents the all-beta domain that is found in several members of the glycosyl hydrolase family 13. It is usually located C-terminal to the catalytic beta/alpha barrel domain. This structure of this domain has been found to be a Greek key beta-sheet fold [5, 6, 7, 8].

More information about this protein can be found at Protein of the Month: alpha-Amylase [9].

Structural links Help

PDB - click here

SCOP: b.30.5.6 , b.71.1.1 , b.71.1.3 , c.1.8.1

CATH: 2.60.40.1180

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR013780

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P00687 Alpha-amylase 1

P04745 Alpha-amylase 1

P07265 Alpha-glucosidase MAL62

Q24451 Alpha-mannosidase 2

Q9M0S5 Isoamylase 3, chloroplastic

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
IPR011330	Glycoside hydrolase/deacetylase, beta/alpha-barrel
IPR006048	Alpha-amylase, C-terminal all beta
IPR014756	Immunoglobulin E-set
IPR004193	Glycoside hydrolase, family 13, N-terminal
IPR011013	Glycoside hydrolase-type carbohydrate-binding
IPR011682	Glycosyl hydrolases 38, C-terminal
IPR015341	Glycoside hydrolase, family 38, central domain
IPR017853	Glycoside hydrolase, catalytic core
IPR000602	Glycoside hydrolase, family 38, 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.	Machius M, Wiegand G, Huber R. Crystal structure of calcium-depleted Bacillus licheniformis alpha-amylase at 2.2 A resolution. J. Mol. Biol. 246 545-59 1995 [PubMed: 7877175] http://dx.doi.org/10.1006/jmbi.1994.0106
6.	Hondoh H, Kuriki T, Matsuura Y. Three-dimensional structure and substrate binding of Bacillus stearothermophilus neopullulanase. J. Mol. Biol. 326 177-88 2003 [PubMed: 12547200] http://dx.doi.org/10.1016/S0022-2836(02)01402-X
7.	Jensen MH, Mirza O, Albenne C, Remaud-Simeon M, Monsan P, Gajhede M, Skov LK. Crystal structure of the covalent intermediate of amylosucrase from Neisseria polysaccharea. Biochemistry 43 3104-10 2004 [PubMed: 15023061] http://dx.doi.org/10.1021/bi0357762
8.	Garman SC, Garboczi DN. The molecular defect leading to Fabry disease: structure of human alpha-galactosidase. J. Mol. Biol. 337 319-35 2004 [PubMed: 15003450] http://dx.doi.org/10.1016/j.jmb.2004.01.035
9.	Mcdowall A. Protein of the Month ? alpha-Amylase. 2006

Additional Reading Open in usermanual
	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
	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
	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
	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
	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

InterPro 23.1