 |
|
| PROSITE documentation PDOC00531 |
Glycosyl hydrolases family 2 signatures
Description
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:
- β-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.
- β-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.
Henrissat B.
April 2006 / Pattern revised.
Technical section
PROSITE methods (with tools and information) covered by this documentation:
| GLYCOSYL_HYDROL_F2_1, PS00719; Glycosyl hydrolases family 2 signature 1 (PATTERN) |
| 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. |
|
|
|
| Matching PDB structures:
1BGL 1BGM 1BHG 1DP0 ... [ALL] |
| GLYCOSYL_HYDROL_F2_2, PS00608; Glycosyl hydrolases family 2 acid/base catalyst (PATTERN) |
| 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. |
|
|
|
| Matching PDB structures:
1BGL 1BGM 1BHG 1DP0 ... [ALL] |
References
| 1 |
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 |
| 2 |
Authors |
Schroeder C.J., Robert C., Lenzen G., McKay L.L., Mercenier A. |
| Title |
Analysis of the lacZ sequences from two Streptococcus thermophilus strains: comparison with the Escherichia coli and Lactobacillus bulgaricus beta-galactosidase sequences. |
| Source |
J. Gen. Microbiol. 137:369-380(1991). |
| PubMed ID |
1901904 |
| 3 |
Authors |
Gebler J.C., Aebersold R., Withers S.G. |
| Title |
Glu-537, not Glu-461, is the nucleophile in the active site of (lac Z) beta-galactosidase from Escherichia coli. |
| Source |
J. Biol. Chem. 267:11126-11130(1992). |
| PubMed ID |
1350782 |
Copyright
PROSITE is copyright. It is produced by the SIB Swiss Institute
Bioinformatics. 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
Prosite License
or
see:
prosite_license.html.
Miscellaneous
View entry in original PROSITE document format
View entry in raw text format (no links)