 |
|
| PROSITE documentation PDOC00532 |
Glycosyl hydrolases family 32 active site
Description:
It has been shown [1,2] that the following glycosyl hydrolases can be
classified into a single family on the basis of sequence similarities:
- Inulinase (EC 3.2.1.7) (or inulase) from the fungi Kluyveromyces marxianus.
- β-fructofuranosidase (EC 3.2.1.26), commonly known as invertase in fungi
and plants and as sucrase in bacteria (gene sacA or scrB).
- Raffinose invertase (EC 3.2.1.26) (gene rafD) from Escherichia coli plasmid
pRSD2.
- Levanase (EC 3.2.1.65) (gene sacC) from Bacillus subtilis.
One of the conserved regions in these enzymes is located in the N-terminal
section and contains an aspartic acid residue which has been shown [3], in
yeast invertase to be important for the catalytic mechanism. We have used this
region as a signature pattern.
Expert(s) to contact by email:
Henrissat B.
Last update:
April 2006 / Pattern revised.
Technical section:
PROSITE method (with tools and information) covered by this documentation:
| GLYCOSYL_HYDROL_F32, PS00609; Glycosyl hydrolases family 32 active site (PATTERN) |
| Consensus pattern: |
H-x(2)-[PV]-x(4)-[LIVMA]-N-D-P-N-[GA]
D is the active site residue |
| Sequences known to belong to this class detected by the pattern: |
ALL |
| Other sequence(s) detected in Swiss-Prot: |
NONE. |
|
|
|
| Matching PDB structures:
1UYP 1W2T 2AC1 2OXB ... [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 | Gunasekaran P., Karunakaran T., Cami B., Mukundan A.G., Preziosi L., Baratti J. |
| Title | Cloning and sequencing of the sacA gene: characterization of a sucrase from Zymomonas mobilis. |
| Source | J. Bacteriol. 172:6727-6735(1990). |
| PubMed ID | 2254250 |
| 3 |
Authors | Reddy V.A., Maley F. |
| Title | Identification of an active-site residue in yeast invertase by affinity labeling and site-directed mutagenesis. |
| Source | J. Biol. Chem. 265:10817-10820(1990). |
| PubMed ID | 2113524 |
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)