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| 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.
Henrissat B.
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. |
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| 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 |
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