{PDOC51662}
{PS51662; BP_PHYTASE}
{BEGIN}
***********************************************
* 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>),  beta-propeller phytase (BPP), cysteine
phytase, and purple acid phytase [1,2].

Beta-propeller phytases  are the most abundant and diverse phytases in nature.
So far  all  known  beta-propeller  phytases  are  from  bacteria,  especially
Bacillus spp.  Calcium  plays  an important role in the catalytic activity and
thermostability of beta-propeller phytases [1,2].

The beta-propeller phytase domain is made of six blades (see <PDB:1POO>). Each
blade is  a  highly  curved  sheet composed of four to five antiparallel beta-
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 beta-propeller phytase domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: January 2013 / First entry.

[ 1] Zhang R., Yang P., Huang H., Yuan T., Shi P., Meng K., Yao B.
     "Molecular and biochemical characterization of a new alkaline
     beta-propeller phytase from the insect symbiotic bacterium
     Janthinobacterium sp. TN115."
     Appl. Microbiol. Biotechnol. 92:317-325(2011).
     PubMed=21562981; DOI=10.1007/s00253-011-3309-0
[ 2] Zhang R., Yang P., Huang H., Shi P., Yuan T., Yao B.
     "Two types of phytases (histidine acid phytase and beta-propeller
     phytase) in Serratia sp. TN49 from the gut of Batocera horsfieldi
     (coleoptera) larvae."
     Curr. Microbiol. 63:408-415(2011).
     PubMed=21853317; DOI=10.1007/s00284-011-9995-0
[ 3] Ha N.-C., Oh B.-C., Shin S., Kim H.-J., Oh T.-K., Kim Y.-O., Choi K.Y.,
     Oh B.-H.
     "Crystal structures of a novel, thermostable phytase in partially and
     fully calcium-loaded states."
     Nat. Struct. Biol. 7:147-153(2000).
     PubMed=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 https://prosite.expasy.org/prosite_license.html
--------------------------------------------------------------------------------

{END}