PROSITE documentation PDOC00737

Glycosyl hydrolases family 25 active sites signature

Description

It has been shown [1,2] that a number of cell-wall lytic enzymes (EC 3.2.1.17) are evolutionary related and can be classified into a single family:

  • Lysozymes (lysin) from Streptococcus pneumoniae bacteriophages of the Cp family.
  • Lysozyme (endolysin) from Lactococcus delbrueckii phage mv1.
  • Autolytic lysozyme from Clostridium acetobutylicum.
  • Lysozyme M1 from Streptomyces globisporus.
  • N,O-diacetylmuramidase (lysozyme ch) from the fungus Chalaropsis.

Two residues, an aspartate and a glutamate, have been shown [3] 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 and can be used as a signature pattern.

Expert(s) to contact by email:

Henrissat B.

Last update:

December 2004 / Pattern and text revised.

Technical section

PROSITE method (with tools and information) covered by this documentation:

GLYCOSYL_HYDROL_F25, PS00953; Glycosyl hydrolases family 25 active sites signature  (PATTERN)
Consensus pattern: D-[LIVM]-x(3)-[NQ]-[PGE]-x(9,15)-[GR]-x(4)-[LIVMFY](2)-K-x-[ST]-E-[GS]-x(2)-[FYL]-x-[DN]
D and E are active site residues
Sequences known to belong to this class detected by the pattern: ALL
Other sequence(s) detected in Swiss-Prot: NONE.
• Retrieve an alignment of Swiss-Prot true positive hits:
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• Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00953
• Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00953
• Scan Swiss-Prot/TrEMBL entries against PS00953
• view ligand binding statistics
Matching PDB structures: 1H09 1JFX 1OBA 2IXU ... [ALL]

References

1 Authors Croux C., Garcia J.L.
Title Sequence of the lyc gene encoding the autolytic lysozyme of Clostridium acetobutylicum ATCC824: comparison with other lytic enzymes.
Source Gene 104:25-31(1991).
PubMed ID 1916274
2 Authors Henrissat B.
Title A classification of glycosyl hydrolases based on amino acid sequence similarities.
Source Biochem. J. 280:309-316(1991).
PubMed ID 1747104
3 Authors Fouche P.B., Hash J.H.
Title The N,O-diacetylmuramidase of Chalaropsis species. Identificaiton of aspartyl and glutamyl residues in the active site.
Source J. Biol. Chem. 253:6787-6793(1978).
PubMed ID 567645

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