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InterPro: IPR002053 Glycoside hydrolase, family 25

Protein matchesHelp
UniProtKB
Matches:
1405 proteins
AccessionHelp IPR002053 Glyco_hydro_25
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR013781 Glycoside hydrolase, subgroup, catalytic core
Children IPR018077 Glycoside hydrolase, family 25 subgroup
Contains IPR008270 Glycoside hydrolase, family 25, active site
GO Term annotationHelp
Process GO:0009253 peptidoglycan catabolic process
GO:0016998 cell wall macromolecule catabolic process
Function GO:0003796 lysozyme 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 25 GH25 comprises enzymes with only one known activity; lysozyme (EC:3.2.1.17).

It has been shown [5, 6] that a number of cell-wall lytic enzymes are evolutionary related and can be classified into a single family. Two residues, an aspartate and a glutamate, have been shown [7] to be important for the catalytic activity of the Charalopsis enzyme. These residues as well as some others in their vicinity are conserved in all proteins from this family.

Structural linksHelp
SCOP: c.1.8.8
CATH: 3.20.20.80
Database linksHelp
Enzyme: EC:3.2.1
CAZy: GH25
PANDIT: PF01183
Blocks: IPB002053
Pfam Clan: CL0058.12

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR002053 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P00721 N,O-diacetylmuramidase

P15057 Lysozyme

P25310 Lysozyme M1

Q27650 Lysozyme

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR002479 Putative cell wall binding repeat
IPR008270 Glycoside hydrolase, family 25, active site
IPR013781 Glycoside hydrolase, subgroup, catalytic core
IPR017853 Glycoside hydrolase, catalytic core
IPR018337 Cell wall/choline-binding repeat
IPR002053 Glycoside hydrolase, family 25
IPR018077 Glycoside hydrolase, family 25 subgroup
SWISS-MODEL
PDB Chain
ModBase
SCOP Domain
CATH 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. Croux C, Garcia JL.
Sequence of the lyc gene encoding the autolytic lysozyme of Clostridium acetobutylicum ATCC824: comparison with other lytic enzymes.
Gene 104 25-31 1991 [PubMed: 1916274]
http://dx.doi.org/10.1016/0378-1119(91)90460-S
6. Henrissat B.
A classification of glycosyl hydrolases based on amino acid sequence similarities.
Biochem. J. 280 ( Pt 2) 309-16 1991 [PubMed: 1747104]
http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=1747104
7. Fouche PB, Hash JH.
The N,O-diacetylmuramidase of Chalaropsis species. Identificaiton of aspartyl and glutamyl residues in the active site.
J. Biol. Chem. 253 6787-93 1978 [PubMed: 567645]
http://intl.jbc.org/cgi/reprint/253/19/6787.pdf

Additional ReadingHelp
Monterroso B, Albert A, Martinez-Ripoll M, Garcia P, Garcia JL, Menendez M, Hermoso JA.
Crystallization and preliminary X-ray diffraction studies of the complete modular endolysin from Cp-1, a phage infecting Streptococcus pneumoniae.
Acta Crystallogr. D Biol. Crystallogr. 58 2002 1487-9 [PubMed: 12198311]
http://dx.doi.org/10.1107/S0907444902011563
Hermoso JA, Monterroso B, Albert A, Galan B, Ahrazem O, Garcia P, Martinez-Ripoll M, Garcia JL, Menendez M.
Structural basis for selective recognition of pneumococcal cell wall by modular endolysin from phage Cp-1.
Structure 11 2003 1239-49 [PubMed: 14527392]
http://dx.doi.org/10.1016/j.str.2003.09.005
Perez-Dorado I, Campillo NE, Monterroso B, Hesek D, Lee M, Paez JA, Garcia P, Martinez-Ripoll M, Garcia JL, Mobashery S, Menendez M, Hermoso JA.
Elucidation of the molecular recognition of bacterial cell wall by modular pneumococcal phage endolysin CPL-1.
J. Biol. Chem. 282 2007 24990-9 [PubMed: 17581815]
http://dx.doi.org/10.1074/jbc.M704317200
Rau A, Hogg T, Marquardt R, Hilgenfeld R.
A new lysozyme fold. Crystal structure of the muramidase from Streptomyces coelicolor at 1.65 A resolution.
J. Biol. Chem. 276 2001 31994-9 [PubMed: 11427528]
http://dx.doi.org/10.1074/jbc.M102591200
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InterPro 23.1