PROSITE documentation PDOC51662 [for PROSITE entry PS51662]Beta-propeller phytase (BPP) domain profile
Phytic acid (myo-inositol hexakisphosphate or phytate when in salt form) is the major storage form of organic phosphorus in nature. Phytases (myo-inositol hexakisphosphate phosphohydrolases; EC 3.1.3.8 or 3.1.3.26) hydrolyze phytic acid to less phosphorylated myo-inositol derivatives and inorganic phosphate. According to their three-dimensional structures and catalytic mechanisms, phytases are classified into four subfamilies: histidine acid phosphatase (HAP) (see <PDOC00538>), β-propeller phytase (BPP), cysteine phytase, and purple acid phytase [1,2].
β-propeller phytases are the most abundant and diverse phytases in nature. So far all known β-propeller phytases are from bacteria, especially Bacillus spp. Calcium plays an important role in the catalytic activity and thermostability of β-propeller phytases [1,2].
The β-propeller phytase domain is made of six blades (see <PDB:1POO>). Each blade is a highly curved sheet composed of four to five antiparallel β-strands that are connected to each other in a topologically identical manner. The fourth strand of each blade is connected across the top of the molecule to the first strand of the next blade. The six blades are aligned along the shaft of the propeller, which is a distinct central channel filled with many well-bound water molecules. Between the blades, extensive hydrophobic interactions are observed [3].
The profile we developed covers the entire β-propeller phytase domain.
Last update:January 2013 / First entry.
-------------------------------------------------------------------------------
PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Zhang R. Yang P. Huang H. Yuan T. Shi P. Meng K. Yao B. |
| Title | Molecular and biochemical characterization of a new alkaline beta-propeller phytase from the insect symbiotic bacterium Janthinobacterium sp. TN115. | |
| Source | Appl. Microbiol. Biotechnol. 92:317-325(2011). | |
| PubMed ID | 21562981 | |
| DOI | 10.1007/s00253-011-3309-0 |
| 2 | Authors | Zhang R. Yang P. Huang H. Shi P. Yuan T. Yao B. |
| Title | Two types of phytases (histidine acid phytase and beta-propeller phytase) in Serratia sp. TN49 from the gut of Batocera horsfieldi (coleoptera) larvae. | |
| Source | Curr. Microbiol. 63:408-415(2011). | |
| PubMed ID | 21853317 | |
| DOI | 10.1007/s00284-011-9995-0 |
| 3 | Authors | Ha N.-C. Oh B.-C. Shin S. Kim H.-J. Oh T.-K. Kim Y.-O. Choi K.Y. |
| Title | Oh B.-H. Crystal structures of a novel, thermostable phytase in partially and fully calcium-loaded states. | |
| Source | Nat. Struct. Biol. 7:147-153(2000). | |
| PubMed ID | 10655618 | |
| DOI | 10.1038/72421 |
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 prosite_license.html.
View entry in original PROSITE document format
View entry in raw text format (no links)