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InterPro: IPR001919 Cellulose-binding domain, family II, bacterial type

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702 proteins

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Accession

IPR001919 Cellulose-bd_dom_fam2_bac

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00553	CBM_2	687
PROSITE profile	PS51173	CBM2	674
SMART	SM00637	CBD_II	658
Signatures in BioMart

InterPro Relationships Help

Parent

IPR012291 Cellulose-binding family II/chitobiase, carbohydrate-binding domain

Contains

IPR018366 Carbohydrate-binding type-2, conserved site

GO Term annotation Help

Process

GO:0005975 carbohydrate metabolic process

Function

GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0030246 carbohydrate binding

InterPro annotation

Entry Details in BioMart

Abstract

The microbial degradation of cellulose and xylans requires several types of enzyme such as endoglucanases (EC:3.2.1.4), cellobiohydrolases (EC:3.2.1.91) (exoglucanases), or xylanases (EC:3.2.1.8) [1]. Structurally, cellulases and xylanases generally consist of a catalytic domain joined to a cellulose-binding domain (CBD) by a short linker sequence rich in proline and/or hydroxy-amino acids.

The CBD domain is found either at the N-terminal or at the C-terminal extremity of these enzymes. As it is shown in the following schematic representation, there are two conserved cysteines in this CBD domain - one at each extremity of the domain - which have been shown [2] to be involved in a disulphide bond. There are also four conserved tryptophan, two are involved in cellulose binding. The CBD of a number of bacterial cellulases has been shown to consist of about 105 amino acid residues [3, 4].

           +-------------------------------------------------+
           |                                                 |
          xCxxxxWxxxxxNxxxWxxxxxxxWxxxxxxxxWNxxxxxGxxxxxxxxxxCx

'C': conserved cysteine involved in a disulphide bond.

Structural links Help

PDB - click here

SCOP: b.2.2.1

CATH: 2.60.40.290

Database links Help

PDBe-motif: PS00561

Enzyme: EC:3.2.1

PROSITE doc: PDOC00485

PANDIT: PF00553

Blocks: IPB001919

Pfam Clan: CL0203.8

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001919

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P07986 Exoglucanase/xylanase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR008965	Carbohydrate-binding
IPR001000	Glycoside hydrolase, family 10
IPR013781	Glycoside hydrolase, subgroup, catalytic core
IPR012291	Cellulose-binding family II/chitobiase, carbohydrate-binding domain
IPR017853	Glycoside hydrolase, catalytic core
IPR001919	Cellulose-binding domain, family II, bacterial type
IPR018366	Carbohydrate-binding type-2, conserved site
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Gilkes NR, Henrissat B, Kilburn DG, Miller RC Jr, Warren RA. Domains in microbial beta-1, 4-glycanases: sequence conservation, function, and enzyme families. Microbiol. Rev. 55 303-15 1991 [PubMed: 1886523] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=1886523
2.	Gilkes NR, Claeyssens M, Aebersold R, Henrissat B, Meinke A, Morrison HD, Kilburn DG, Warren RA, Miller RC Jr. Structural and functional relationships in two families of beta-1,4-glycanases. Eur. J. Biochem. 202 367-77 1991 [PubMed: 1761039] http://dx.doi.org/10.1111/j.1432-1033.1991.tb16384.x
3.	Meinke A, Gilkes NR, Kilburn DG, Miller RC Jr, Warren RA. Bacterial cellulose-binding domain-like sequences in eucaryotic polypeptides. Protein Seq. Data Anal. 4 349-53 1991 [PubMed: 1812490]
4.	Simpson PJ, Xie H, Bolam DN, Gilbert HJ, Williamson MP. The structural basis for the ligand specificity of family 2 carbohydrate-binding modules. J. Biol. Chem. 275 41137-42 2000 [PubMed: 10973978] http://dx.doi.org/10.1074/jbc.M006948200

Additional Reading Open in usermanual
	Simpson PJ, Bolam DN, Cooper A, Ciruela A, Hazlewood GP, Gilbert HJ, Williamson MP. A family IIb xylan-binding domain has a similar secondary structure to a homologous family IIa cellulose-binding domain but different ligand specificity. Structure 7 1999 853-64 [PubMed: 10425686] http://dx.doi.org/10.1016/S0969-2126(99)80108-7
	Bolam DN, Xie H, White P, Simpson PJ, Hancock SM, Williamson MP, Gilbert HJ. Evidence for synergy between family 2b carbohydrate binding modules in Cellulomonas fimi xylanase 11A. Biochemistry 40 2001 2468-77 [PubMed: 11327868] http://dx.doi.org/10.1021/bi002564l
	Nagy T, Simpson P, Williamson MP, Hazlewood GP, Gilbert HJ, Orosz L. All three surface tryptophans in Type IIa cellulose binding domains play a pivotal role in binding both soluble and insoluble ligands. FEBS Lett. 429 1998 312-6 [PubMed: 9662439] http://dx.doi.org/10.1016/S0014-5793(98)00625-5
	Xu GY, Ong E, Gilkes NR, Kilburn DG, Muhandiram DR, Harris-Brandts M, Carver JP, Kay LE, Harvey TS. Solution structure of a cellulose-binding domain from Cellulomonas fimi by nuclear magnetic resonance spectroscopy. Biochemistry 34 1995 6993-7009 [PubMed: 7766609] http://dx.doi.org/10.1021/bi00021a011

InterPro 23.1