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InterPro: IPR018366 Carbohydrate-binding type-2, conserved site

Protein matchesHelp
UniProtKB
Matches:
140 proteins
AccessionHelp IPR018366 CBM2_CS
TypeHelp Conserved_site
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR001919 Cellulose-binding domain, family II, bacterial type
IPR008965 Carbohydrate-binding
IPR012291 Cellulose-binding family II/chitobiase, carbohydrate-binding domain
GO Term annotationHelp
Process GO:0005975 carbohydrate metabolic process
Function GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0030246 carbohydrate binding
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

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 linksHelp
SCOP: b.2.2.1
CATH: 2.60.40.290
Database linksHelp
Enzyme: EC:3.2.1

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR018366 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
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

PublicationsHelp
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 ReadingHelp
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
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
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InterPro 23.1