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InterPro: IPR003305 Carbohydrate-binding, CenC-like

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738 proteins

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Accession

IPR003305 CenC_carb_bd

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF02018	CBM_4_9	738
Signatures in BioMart

InterPro Relationships Help

Parent

IPR008979 Galactose-binding domain-like

InterPro annotation

Entry Details in BioMart

Abstract

The 1,4-beta-glucanase CenC from Cellulomonas fimi contains two cellulose-binding domains, CBD(N1) and CBD(N2), arranged in tandem at its N terminus. These homologous CBDs are distinct in their selectivity for binding amorphous and not crystalline cellulose [1]. Multidimensional heteronuclear nuclear magnetic resonance (NMR) spectroscopy was used to determine the tertiary structure of the 152 amino acid N-terminal cellulose-binding domain from C. fimi 1,4-beta-glucanase CenC (CBDN1) [2]. The tertiary structure of CBDN1 is strikingly similar to that of the bacterial 1,3-1,4-beta-glucanases, as well as other sugar-binding proteins with jelly-roll folds.

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SCOP: b.18.1.14 , b.18.1.7

CATH: 2.60.120.260

Database links Help

Enzyme: EC:3.2.1

PANDIT: PF02018

Blocks: IPB003305

Pfam Clan: CL0202.7

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR003305

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P14090 Endoglucanase C

Q18DN4 Halomucin

Q9SG80 Alpha-L-arabinofuranosidase 1

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR003305	Carbohydrate-binding, CenC-like
IPR013784	Carbohydrate-binding-like fold
IPR010720	Alpha-L-arabinofuranosidase, C-terminal
IPR013783	Immunoglobulin-like fold
IPR006626	Parallel beta-helix repeat
IPR011493	GLUG
IPR014756	Immunoglobulin E-set
IPR013098	Immunoglobulin I-set
IPR001304	C-type lectin
IPR008979	Galactose-binding domain-like
IPR017853	Glycoside hydrolase, catalytic core
IPR007110	Immunoglobulin-like
IPR003599	Immunoglobulin subtype
IPR001701	Glycoside hydrolase, family 9
IPR004197	Glycoside hydrolase, family 9, N-terminal, Ig-like
IPR016187	C-type lectin fold
IPR016186	C-type lectin-like
IPR015919	Cadherin-like
IPR008964	Invasin/intimin cell-adhesion
IPR012341	Six-hairpin glycosidase
IPR008928	Six-hairpin glycosidase-like
IPR002126	Cadherin
IPR018221	Glycoside hydrolase, family 9, active site
IPR000601	PKD
	ModBase
	SWISS-MODEL
	PDB Chain
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Brun E, Johnson PE, Creagh AL, Tomme P, Webster P, Haynes CA, McIntosh LP. Structure and binding specificity of the second N-terminal cellulose-binding domain from Cellulomonas fimi endoglucanase C. Biochemistry 39 2445-58 2000 [PubMed: 10704194] http://dx.doi.org/10.1021/bi992079u
2.	Johnson PE, Joshi MD, Tomme P, Kilburn DG, McIntosh LP. Structure of the N-terminal cellulose-binding domain of Cellulomonas fimi CenC determined by nuclear magnetic resonance spectroscopy. Biochemistry 35 14381-94 1996 [PubMed: 8916925] http://dx.doi.org/10.1021/bi961612s

Additional Reading Open in usermanual
	Charnock SJ, Bolam DN, Turkenburg JP, Gilbert HJ, Ferreira LM, Davies GJ, Fontes CM. The X6 "thermostabilizing" domains of xylanases are carbohydrate-binding modules: structure and biochemistry of the Clostridium thermocellum X6b domain. Biochemistry 39 2000 5013-21 [PubMed: 10819965] http://dx.doi.org/10.1021/bi992821q
	Boraston AB, Nurizzo D, Notenboom V, Ducros V, Rose DR, Kilburn DG, Davies GJ. Differential oligosaccharide recognition by evolutionarily-related beta-1,4 and beta-1,3 glucan-binding modules. J. Mol. Biol. 319 2002 1143-56 [PubMed: 12079353] http://dx.doi.org/10.1016/S0022-2836(02)00374-1
	Xie H, Gilbert HJ, Charnock SJ, Davies GJ, Williamson MP, Simpson PJ, Raghothama S, Fontes CM, Dias FM, Ferreira LM, Bolam DN. Clostridium thermocellum Xyn10B carbohydrate-binding module 22-2: the role of conserved amino acids in ligand binding. Biochemistry 40 2001 9167-76 [PubMed: 11478884] http://dx.doi.org/10.1021/bi0106742

InterPro 23.1