EBI Databases InterPro	Search Open in usermanual InterPro:
Jump to: InterProScan Databases Documentation FTP site Help Click on the icon for context sensitive help from the user manual. Advanced search

InterPro: IPR006104 Glycoside hydrolase family 2, carbohydrate-binding

Protein matches Help

UniProtKB

Matches:

2720 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
Matches in BioMart

Accession

IPR006104 Glyco_hydro_2_carb-bd

Secondary

IPR001649

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF02837	Glyco_hydro_2_N	2720
Signatures in BioMart

InterPro Relationships Help

Parent

IPR008979 Galactose-binding domain-like

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.

The sugar binding domain has a jelly-roll fold [6].

Structural links Help

PDB - click here

SCOP: b.18.1.5

CATH: 2.60.120.260

Database links Help

Enzyme: EC:3.2.1.23

CAZy: GH2

PANDIT: PF02837

Blocks: IPB006104

Pfam Clan: CL0202.7

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR006104

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P00722 Beta-galactosidase

P08236 Beta-glucuronidase

P12265 Beta-glucuronidase

Q75W54 Mannosylglycoprotein endo-beta-mannosidase

Q93324 Probable beta-mannosidase

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
	Tailford LE, Offen WA, Smith NL, Dumon C, Morland C, Gratien J, Heck MP, Stick RV, Bleriot Y, Vasella A, Gilbert HJ, Davies GJ. Structural and biochemical evidence for a boat-like transition state in beta-mannosidases. Nat. Chem. Biol. 4 2008 306-12 [PubMed: 18408714] http://dx.doi.org/10.1038/nchembio.81
	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
	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
	Tailford LE, Money VA, Smith NL, Dumon C, Davies GJ, Gilbert HJ. Mannose foraging by Bacteroides thetaiotaomicron: structure and specificity of the beta-mannosidase, BtMan2A. J. Biol. Chem. 282 2007 11291-9 [PubMed: 17287210] http://dx.doi.org/10.1074/jbc.M610964200

InterPro 23.1