EC Number |
General Information |
Reference |
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3.1.3.8 | evolution |
dual-domain beta-propeller phytases have succeeded evolutionarily because they can increase the amount of available phosphate by interacting together |
-, 714987 |
3.1.3.8 | evolution |
enzyme rStPhy belongs to the histidine acid phosphatase (HAP) phytases family |
750839 |
3.1.3.8 | evolution |
molecular modeling of PHY US42 indicates that this phytase belongs to the group of beta-propeller phytases that are usually calcium-dependent |
-, 750984 |
3.1.3.8 | evolution |
on the basis of the site at which phytate dephosphorization begins, phytases can be grouped into three classes: 3-phytases (EC 3.1.3.8), 6-phytases (EC 3.1.3.26), and 5-phytases (EC 3.1.3.72). The fungal phytases are included in the 3-phytases class, in which the dephosphorization starts at the third phosphate group. Because of their catalytic mechanism, the fungal phytases belong to the histidine acid phosphatase class |
749619 |
3.1.3.8 | evolution |
the consensus sequence RHGXRXP and HD, typical of histidine acid phosphatases |
-, 751491 |
3.1.3.8 | evolution |
the enzyme AgpP from Pantoea sp. 3.5.1. belongs to the Agp subfamily of histidine acid phosphatases with 3-phytase specificity. The amino acid sequence of the Pantoea sp. 3.5.1 AgpP phytase harbors an N-terminal RHNLRAP motif (where the italicized residues are variable) and a C-terminal HD motif, which are the structural hallmarks of the highly conserved catalytic core of histidine acid phosphatases (HAPs) [consensus sequence RH(G/N)XRXP/HD, where the slash separates the N- and C-terminal sequences] |
749654 |
3.1.3.8 | evolution |
the enzyme belongs to the histidine acid phosphatase (HAP) family |
-, 751302, 751544 |
3.1.3.8 | evolution |
the enzyme belongs to the histidine acid phosphatase (HAP) family phytases present in insect-cultivated fungus gardens |
749682 |
3.1.3.8 | evolution |
the enzyme belongs to the histidine acid phosphatase (HAP) family, it possesses typical conserved motifs of HAP phytases: RHGERFP in AA125-131 and HD in AA394-395 |
-, 751308 |
3.1.3.8 | evolution |
the enzyme belongs to the histidine acid phosphatase family, it contains the active-site motif RHGXRXP |
-, 752009 |