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PROSITE documentation PDOC51662

Beta-propeller phytase (BPP) domain profile





Description

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.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

BP_PHYTASE, PS51662; Beta-propeller phytase (BPP) domain profile  (MATRIX)


References

1AuthorsZhang R. Yang P. Huang H. Yuan T. Shi P. Meng K. Yao B.
TitleMolecular and biochemical characterization of a new alkaline beta-propeller phytase from the insect symbiotic bacterium Janthinobacterium sp. TN115.
SourceAppl. Microbiol. Biotechnol. 92:317-325(2011).
PubMed ID21562981
DOI10.1007/s00253-011-3309-0

2AuthorsZhang R. Yang P. Huang H. Shi P. Yuan T. Yao B.
TitleTwo types of phytases (histidine acid phytase and beta-propeller phytase) in Serratia sp. TN49 from the gut of Batocera horsfieldi (coleoptera) larvae.
SourceCurr. Microbiol. 63:408-415(2011).
PubMed ID21853317
DOI10.1007/s00284-011-9995-0

3AuthorsHa N.-C. Oh B.-C. Shin S. Kim H.-J. Oh T.-K. Kim Y.-O. Choi K.Y. Oh B.-H.
TitleCrystal structures of a novel, thermostable phytase in partially and fully calcium-loaded states.
SourceNat. Struct. Biol. 7:147-153(2000).
PubMed ID10655618
DOI10.1038/72421



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