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InterPro: IPR000334 Glycoside hydrolase, family 45

Protein matchesHelp
UniProtKB
Matches:
134 proteins
AccessionHelp IPR000334 Glyco_hydro_45
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR014733 Barwin-like endoglucanase
GO Term annotationHelp
Process GO:0005975 carbohydrate metabolic process
Function GO:0008810 cellulase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

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 45 GH45 comprises enzymes with only one known activity; endoglucanase (EC:3.2.1.4).

The microbial degradation of cellulose and xylans requires several types of enzymes such as endoglucanases, cellobiohydrolases (EC:3.2.1.91) (exoglucanases), or xylanases (EC:3.2.1.8) [5, 6]. Fungi and bacteria produce a spectrum of cellulolytic enzymes (cellulases) and xylanases which, on the basis of sequence similarities, can be classified into families. One of these families is known as the cellulase family K or as the glycosyl hydrolases family 45 [7]. The best conserved regions in these enzymes is located in the N-terminal section. It contains an aspartic acid residue which has been shown [8] to act as a nucleophile in the catalytic mechanism. This also has several cysteines that are involved in forming disulphide bridges.

Structural linksHelp
SCOP: b.52.1.1
CATH: 2.40.40.10
Database linksHelp
PDBe-motif: PS01140
Enzyme: EC:3.2.1.4
CAZy: GH45
PROSITE doc: PDOC00877
PANDIT: PF02015
Blocks: IPB000334
Pfam Clan: CL0199.8

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR000334 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O97401 Endoglucanase

P18126 Endoglucanase B

P43316 Endoglucanase-5

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR012291 Cellulose-binding family II/chitobiase, carbohydrate-binding domain
IPR002883 Dockerin cellulose-binding domain
IPR008965 Carbohydrate-binding
IPR000334 Glycoside hydrolase, family 45
IPR001919 Cellulose-binding domain, family II, bacterial type
IPR018366 Carbohydrate-binding type-2, conserved site
IPR009009 Barwin-related endoglucanase
IPR014733 Barwin-like endoglucanase
IPR009031 Type X cellulose-binding domain, CBDX
PDB Chain
ModBase
CATH Domain
SWISS-MODEL
SCOP Domain

PublicationsHelp
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. Beguin P.
Molecular biology of cellulose degradation.
Annu. Rev. Microbiol. 44 219-48 1990 [PubMed: 2252383]
http://dx.doi.org/10.1146/annurev.mi.44.100190.001251
6. 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
7. Henrissat B, Bairoch A.
New families in the classification of glycosyl hydrolases based on amino acid sequence similarities.
Biochem. J. 293 ( Pt 3) 781-8 1993 [PubMed: 8352747]
http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=8352747&action=stream&blobtype=pdf
8. Davies GJ, Dodson GG, Hubbard RE, Tolley SP, Dauter Z, Wilson KS, Hjort C, Mikkelsen JM, Rasmussen G, Schulein M.
Structure and function of endoglucanase V.
Nature 365 362-4 1993 [PubMed: 8377830]
http://dx.doi.org/10.1038/365362a0

Additional ReadingHelp
Valjakka J, Rouvinen J.
Structure of 20K endoglucanase from Melanocarpus albomyces at 1.8 A resolution.
Acta Crystallogr. D Biol. Crystallogr. 59 2003 765-8 [PubMed: 12657806]
http://dx.doi.org/10.1107/S0907444903002051
Davies GJ, Tolley SP, Henrissat B, Hjort C, Schulein M.
Structures of oligosaccharide-bound forms of the endoglucanase V from Humicola insolens at 1.9 A resolution.
Biochemistry 34 1995 16210-20 [PubMed: 8519779]
http://dx.doi.org/10.1021/bi00049a037
Davies GJ, Dodson G, Moore MH, Tolley SP, Dauter Z, Wilson KS, Rasmussen G, Schulein M.
Structure determination and refinement of the Humicola insolens endoglucanase V at 1.5 A resolution.
Acta Crystallogr. D Biol. Crystallogr. 52 1996 7-17 [PubMed: 15299721]
http://dx.doi.org/10.1107/S0907444995009280
Hirvonen M, Papageorgiou AC.
Crystal structure of a family 45 endoglucanase from Melanocarpus albomyces: mechanistic implications based on the free and cellobiose-bound forms.
J. Mol. Biol. 329 2003 403-10 [PubMed: 12767825]
http://dx.doi.org/10.1016/S0022-2836(03)00467-4
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InterPro 23.1