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InterPro: IPR006103 Glycoside hydrolase family 2, TIM barrel

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UniProtKB

Matches:

2006 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

IPR006103 Glyco_hydro_2_TIM

Secondary

IPR001649

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF02836	Glyco_hydro_2_C	2006
Signatures in BioMart

InterPro Relationships Help

Parent

IPR013781 Glycoside hydrolase, subgroup, catalytic core

Found in

IPR006101 Glycoside hydrolase, family 2

GO Term annotation Help

Process

GO:0005975 carbohydrate metabolic process

Function

GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds

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 2 GH2 comprises enzymes with several known activities; beta-galactosidase (EC:3.2.1.23); beta-mannosidase (EC:3.2.1.25); beta-glucuronidase (EC:3.2.1.31).

These enzymes contain a conserved glutamic acid residue which has been shown [5], in Escherichia coli lacZ (P00722), to be the general acid/base catalyst in the active site of the enzyme.

Beta-galactosidase from E. coli has a TIM-barrel-like core surrounded by four other largely beta domains [6].

Structural links Help

PDB - click here

SCOP: b.1.4.1 , c.1.8.3

CATH: 2.60.40.320 , 3.20.20.80

Database links Help

Enzyme: EC:3.2.1.23

CAZy: GH2

PANDIT: PF02836

Blocks: IPB006103

Pfam Clan: CL0058.12

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR006103

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O18835 Beta-glucuronidase

P00722 Beta-galactosidase

P00723 Beta-galactosidase

P08236 Beta-glucuronidase

P12265 Beta-glucuronidase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR014718	Glycoside hydrolase-type carbohydrate-binding, subgroup
IPR013781	Glycoside hydrolase, subgroup, catalytic core
IPR004199	Glycoside hydrolase, family 42, domain 5
IPR013812	Glycoside hydrolase, family 2/20, immunoglobulin-like beta-sandwich domain
IPR011013	Glycoside hydrolase-type carbohydrate-binding
IPR006101	Glycoside hydrolase, family 2
IPR008979	Galactose-binding domain-like
IPR006104	Glycoside hydrolase family 2, carbohydrate-binding
IPR017853	Glycoside hydrolase, catalytic core
IPR006102	Glycoside hydrolase family 2, immunoglobulin-like beta-sandwich
IPR006103	Glycoside hydrolase family 2, TIM barrel
	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.	Gebler JC, Aebersold R, Withers SG. Glu-537, not Glu-461, is the nucleophile in the active site of (lac Z) beta-galactosidase from Escherichia coli. J. Biol. Chem. 267 11126-30 1992 [PubMed: 1350782] http://intl.jbc.org/cgi/reprint/267/16/11126.pdf
6.	Jacobson RH, Zhang XJ, DuBose RF, Matthews BW. Three-dimensional structure of beta-galactosidase from E. coli. Nature 369 761-6 1994 [PubMed: 8008071] http://dx.doi.org/10.1038/369761a0

Additional Reading Open in usermanual
	Juers DH, Hakda S, Matthews BW, Huber RE. Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase. Biochemistry 42 2003 13505-11 [PubMed: 14621996] http://dx.doi.org/10.1021/bi035506j
	Juers DH, Matthews BW. Reversible lattice repacking illustrates the temperature dependence of macromolecular interactions. J. Mol. Biol. 311 2001 851-62 [PubMed: 11518535] http://dx.doi.org/10.1006/jmbi.2001.4891
	Skalova T, Dohnalek J, Spiwok V, Lipovova P, Vondrackova E, Petrokova H, Duskova J, Strnad H, Kralova B, Hasek J. Cold-active beta-galactosidase from Arthrobacter sp. C2-2 forms compact 660 kDa hexamers: crystal structure at 1.9A resolution. J. Mol. Biol. 353 2005 282-94 [PubMed: 16171818] http://dx.doi.org/10.1016/j.jmb.2005.08.028
	Juers DH, Heightman TD, Vasella A, McCarter JD, Mackenzie L, Withers SG, Matthews BW. A structural view of the action of Escherichia coli (lacZ) beta-galactosidase. Biochemistry 40 2001 14781-94 [PubMed: 11732897] http://dx.doi.org/10.1021/bi011727i
	Juers DH, Jacobson RH, Wigley D, Zhang XJ, Huber RE, Tronrud DE, Matthews BW. High resolution refinement of beta-galactosidase in a new crystal form reveals multiple metal-binding sites and provides a structural basis for alpha-complementation. Protein Sci. 9 2000 1685-99 [PubMed: 11045615] http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=11045615&action=stream&blobtype=pdf

InterPro 23.1