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| PROSITE documentation PDOC51166 |
CBM20 (carbohydrate binding type-20) domain profile
Description
Carbohydrate-binding modules (CBM) have been classified into more than 40
families according to sequence homology [E1]. Several amylolytic enzymes share
a conserved region of 90-130 amino acid residues, the CBM20 domain. It is
mainly found C-terminal to the catalytic domain and has been shown to bind
granular starch [1,2].
The crystal structure of CBM20 has been solved (see <PDB:1CGT>) [3]. It
consists of seven β-stands forming an open-sided distorted β-barrel.
Several aromatics, especially the well-conserved Trp and Tyr residues,
participates in granular starch binding. Starch consists of glucose units
mainly in the form of amylose and amylopectin, which are arranged in
semicrystalline arrays of double-helical strands to form large irregular
granules. The two starch strands are bound to the CBM20 domain in a
perpendicular orientation. This may be functionally important, as it may force
starch strands apart thus increasing the hydrolyzable surface [4].
Some proteins known to contain a CBM20 domain are listed below:
- Mammalian genethonin 1 protein.
- Mammalian laforin protein, a dual specificity protein phosphatase that may
be involved in the control of glycogen metabolism.
- Human hypothetical protein KIAA1434.
- Fungi glucoamylase (EC 3.2.1.3).
- Bacterial cyclomaltodextrin glucanotransferase (EC 2.4.1.19).
- Bacterial α-amylase (EC 3.2.1.1).
- Pseudomonas glucan 1,4-α-maltotetraohydrolase precursor (EC 3.2.1.60).
- Thermoanaerobacterium amylopullulanase (α-amylase/pullulanase).
- Bacillus maltogenic α-amylase (EC 3.2.1.133).
The profile we developed covers the whole CBM20 domain.
The CBM20 domain is also known as the starch-binding domain.
November 2005 / First entry.
Technical section
PROSITE method (with tools and information) covered by this documentation:
| CBM20, PS51166; CBM20 (carbohydrate binding type-20) domain profile (MATRIX) |
| Sequences known to belong to this class detected by the profile: |
ALL |
| Other sequence(s) detected in Swiss-Prot: |
NONE. |
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| Matching PDB structures:
1A47 1AC0 1ACZ 1B90 ... [ALL] |
References
| 1 |
Authors |
Goto M., Semimaru T., Furukawa K., Hayashida S. |
| Title |
Analysis of the raw starch-binding domain by mutation of a glucoamylase from Aspergillus awamori var. kawachi expressed in Saccharomyces cerevisiae. |
| Source |
Appl. Environ. Microbiol. 60:3926-3930(1994). |
| PubMed ID |
7993082 |
| 2 |
Authors |
Chen L., Coutinho P.M., Nikolov Z., Ford C. |
| Title |
Deletion analysis of the starch-binding domain of Aspergillus glucoamylase. |
| Source |
Protein Eng. 8:1049-1055(1995). |
| PubMed ID |
8771186 |
| 3 |
Authors |
Klein C., Schulz G.E. |
| Title |
Structure of cyclodextrin glycosyltransferase refined at 2.0 A resolution. |
| Source |
J. Mol. Biol. 217:737-750(1991). |
| PubMed ID |
1826034 |
| 4 |
Authors |
Sorimachi K., Le Gal-Coeffet M.F., Williamson G., Archer D.B., Williamson M.P. |
| Title |
Solution structure of the granular starch binding domain of Aspergillus niger glucoamylase bound to beta-cyclodextrin. |
| Source |
Structure 5:647-661(1997). |
| PubMed ID |
9195884 |
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