PROSITE documentation PDOC00787

Glycosyl hydrolases family 39 putative active site

Description:

It has been shown [1,E1] that the following glycosyl hydrolases can be classified into a single family on the basis of sequence similarities:

  • Mammalian lysosomal α-L-iduronidase (EC 3.2.1.76).
  • Caldocellum saccharolyticum and Thermoanaerobacter saccharolyticum β- xylosidase (EC 3.2.1.37) (gene xynB).

The best conserved regions in these enzymes is located in the N-terminal section. It contains a glutamic acid residue which, on the basis of similarities with other families of glycosyl hydrolases [2], probably acts as the proton donor in the catalytic mechanism. We use this region as a signature pattern.

Expert(s) to contact by email:

Henrissat B.

Last update:

May 2004 / Text revised.

Technical section:

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

GLYCOSYL_HYDROL_F39, PS01027Glycosyl hydrolases family 39 active site  (PATTERN)
Consensus pattern: W-x-F-E-x-W-N-E-P-[DN]
The second E may be the active site residue
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:
  Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format
Retrieve the sequence logo from the alignment
Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS01027
Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS01027
Scan Swiss-Prot/TrEMBL entries against PS01027
view ligand binding statistics
Matching PDB structures: 1PX8 1UHV 1W91 1Y24 ... [ALL]

References:

1 AuthorsHenrissat B., Bairoch A.
TitleNew families in the classification of glycosyl hydrolases based on amino acid sequence similarities.
SourceBiochem. J. 293:781-788(1993).
PubMed ID8352747
2 AuthorsHenrissat B., Callebaut I., Fabrega S., Lehn P., Mornon J.-P., Davies G.
TitleConserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.
SourceProc. Natl. Acad. Sci. U.S.A. 92:7090-7094(1995).
PubMed ID7624375
E1
Sourcehttp://www.expasy.org/cgi-bin/lists?glycosid.txt

Copyright:

PROSITE is copyright. It is produced by the Swiss Institute of Bioinformatics (SIB). There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to license@isb-sib.ch or see: http://www.expasy.org/prosite/prosite_license.htm.

Miscellaneous:

View entry in original PROSITE document format
View entry in raw text format (no links)