{PDOC00531} {PS00719; GLYCOSYL_HYDROL_F2_1} {PS00608; GLYCOSYL_HYDROL_F2_2} {BEGIN} ******************************************* * Glycosyl hydrolases family 2 signatures * ******************************************* It has been shown [1,2,E1] that the following glycosyl hydrolases can be, on the basis of sequence similarities, classified into a single family: - Beta-galactosidases (EC 3.2.1.23) from bacteria such as Escherichia coli (genes lacZ and ebgA), Clostridium acetobutylicum, Clostridium thermosulfurogenes, Klebsiella pneumoniae, Lactobacillus delbrueckii, or Streptococcus thermophilus and from the fungi Kluyveromyces lactis. - Beta-glucuronidase (EC 3.2.1.31) from Escherichia coli (gene uidA) and from mammals. One of the conserved regions in these enzymes is centered on a conserved glutamic acid residue which has been shown [3], in Escherichia coli lacZ, to be the general acid/base catalyst in the active site of the enzyme. We have used this region as a signature pattern. As a second signature pattern we selected a highly conserved region located some sixty residues upstream from the active site glutamate. -Consensus pattern: N-x-[LIVMFYWD]-R-[STACN](2)-H-Y-P-x(4)-[LIVMFYWS](2)-x(3)- [DN]-x(2)-G-[LIVMFYW](4) -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Consensus pattern: [DENQLF]-[KRVW]-N-[HRY]-[STAPV]-[SAC]-[LIVMFS]-[LIVMFSA]- [LIVMFS]-W-[GSV]-x(2,3)-N-E [E is the active site residue] -Sequences known to belong to this class detected by the pattern: ALL, except for Rhizobium meliloti lacZ. -Other sequence(s) detected in Swiss-Prot: NONE. -Expert(s) to contact by email: Henrissat B.; bernie@afmb.cnrs-mrs.fr -Last update: April 2006 / Pattern revised. [ 1] Henrissat B. "A classification of glycosyl hydrolases based on amino acid sequence similarities." Biochem. J. 280:309-316(1991). PubMed=1747104 [ 2] Schroeder C.J., Robert C., Lenzen G., McKay L.L., Mercenier A. "Analysis of the lacZ sequences from two Streptococcus thermophilus strains: comparison with the Escherichia coli and Lactobacillus bulgaricus beta-galactosidase sequences." J. Gen. Microbiol. 137:369-380(1991). PubMed=1901904 [ 3] Gebler J.C., Aebersold R., Withers S.G. "Glu-537, not Glu-461, is the nucleophile in the active site of (lac Z) beta-galactosidase from Escherichia coli." J. Biol. Chem. 267:11126-11130(1992). PubMed=1350782 [E1] https://www.uniprot.org/docs/glycosid -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}