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Enzyme Name | UniProtKB | KEGG |
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| P34752 | P34755 |
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Protein name | 3-phytase A | 3-phytase B | 3-phytase1-phytasephytasephytate 1-phosphatasephytate 6-phosphatase |
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Synonyms | EC 3.1.3.83 phytase AMyo-inositol hexakisphosphate phosphohydrolase AMyo-inositol-hexaphosphate 3-phosphohydrolase A | EC 3.1.3.8Myo-inositol-hexaphosphate 3-phosphohydrolase BpH 2.5 optimum acid phosphatase |
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Pfam | PF00328 (His_Phos_2) [Graphical view]
| PF00328 (His_Phos_2) [Graphical view]
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KEGG pathways | MAP code | Pathways |
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MAP00562 | Inositol phosphate metabolism |
UniProtKB:Accession Number | P34752 | P34755 |
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Entry name | PHYA_ASPNG | PHYB_ASPAW |
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Activity | Myo-inositol hexakisphosphate + H(2)O = 1D- myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate. | Myo-inositol hexakisphosphate + H(2)O = 1D- myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate. |
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Subunit |
| Homodimer. |
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Subcellular location | Secreted. |
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Cofactor |
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Compound table: links to PDB-related databases & PoSSuM |
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| Substrates | Products |
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KEGG-id | C01204 | C00001 | C04563 | C00009 |
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Compound | myo-Inositol hexakisphosphate | H2O | D-myo-Inositol 1,2,4,5,6-pentakisphosphate | Orthophosphate |
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Type | carbohydrate,phosphate group/phosphate ion | H2O | carbohydrate,phosphate group/phosphate ion | phosphate group/phosphate ion |
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ChEBI | 17401
| 15377
| 16507
| 26078
|
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PubChem |
| 22247451 962
|
| 1004 22486802
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| | | | | | | | | | | |
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1ihpA01 |  |  |  |  |  |  |  | Unbound | | Unbound | Unbound |
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1qfxA |  |  |  |  |  |  |  | Unbound | | Unbound | Unbound |
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1qfxB |  |  |  |  |  |  |  | Unbound | | Unbound | Unbound |
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1ihpA02 |  |  |  |  |  |  |  | Unbound | | Unbound | Unbound |
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References for Catalytic Mechanism | References | Sections | No. of steps in catalysis |
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[1] | p.189 |
| [3] | p.970 |
| [4] | p.111 |
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references | [1] |
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Comments | X-ray crystallography (2.5 Angstroms) |
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PubMed ID | 9164457 |
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Journal | Nat Struct Biol |
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Year | 1997 |
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Volume | 4 |
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Pages | 185-90 |
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Authors | Kostrewa D, Gruninger-Leitch F, D'Arcy A, Broger C, Mitchell D, van Loon AP |
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Title | Crystal structure of phytase from Aspergillus ficuum at 2.5 A resolution. |
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Related PDB | 1ihp |
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[2] |
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PubMed ID | 9925555 |
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Journal | Appl Environ Microbiol |
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Year | 1999 |
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Volume | 65 |
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Pages | 367-73 |
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Authors | Wyss M, Brugger R, Kronenberger A, Remy R, Fimbel R, Oesterhelt G, Lehmann M, van Loon AP |
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Title | Biochemical characterization of fungal phytases (myo-inositol hexakisphosphate phosphohydrolases): catalytic properties. |
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[3] |
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Comments | X-ray crystallography (2.4 Angstroms) |
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PubMed ID | 10329192 |
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Journal | J Mol Biol |
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Year | 1999 |
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Volume | 288 |
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Pages | 965-74 |
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Authors | Kostrewa D, Wyss M, D'Arcy A, van Loon AP |
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Title | Crystal structure of Aspergillus niger pH 2.5 acid phosphatase at 2. 4 A resolution. |
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Related PDB | 1qfx |
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[4] |
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PubMed ID | 10655611 |
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Journal | Nat Struct Biol |
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Year | 2000 |
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Volume | 7 |
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Pages | 108-13 |
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Authors | Lim D, Golovan S, Forsberg CW, Jia Z |
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Title | Crystal structures of Escherichia coli phytase and its complex with phytate. |
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[5] |
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PubMed ID | 10788605 |
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Journal | FEBS Lett |
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Year | 2000 |
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Volume | 472 |
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Pages | 169-72 |
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Authors | Tomschy A, Wyss M, Kostrewa D, Vogel K, Tessier M, Hofer S, Burgin H, Kronenberger A, Remy R, van Loon AP, Pasamontes L |
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Title | Active site residue 297 of Aspergillus niger phytase critically affects the catalytic properties. |
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[6] |
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PubMed ID | 10933495 |
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Journal | Protein Sci |
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Year | 2000 |
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Volume | 9 |
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Pages | 1304-11 |
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Authors | Tomschy A, Tessier M, Wyss M, Brugger R, Broger C, Schnoebelen L, van Loon AP, Pasamontes L |
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Title | Optimization of the catalytic properties of Aspergillus fumigatus phytase based on the three-dimensional structure. |
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[7] |
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PubMed ID | 10973795 |
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Journal | Biochem Biophys Res Commun |
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Year | 2000 |
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Volume | 275 |
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Pages | 759-63 |
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Authors | Mullaney EJ, Daly CB, Sethumadhavan K, Rodriquez E, Lei XG, Ullah AH |
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Title | Phytase activity in Aspergillus fumigatus isolates. |
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[8] |
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PubMed ID | 11051103 |
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Journal | Arch Biochem Biophys |
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Year | 2000 |
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Volume | 382 |
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Pages | 105-12 |
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Authors | Rodriguez E, Wood ZA, Karplus PA, Lei XG |
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Title | Site-directed mutagenesis improves catalytic efficiency and thermostability of Escherichia coli pH 2.5 acid phosphatase/phytase expressed in Pichia pastoris. |
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[9] |
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PubMed ID | 12359257 |
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Journal | Biochem Biophys Res Commun |
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Year | 2002 |
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Volume | 297 |
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Pages | 1016-20 |
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Authors | Mullaney EJ, Daly CB, Kim T, Porres JM, Lei XG, Sethumadhavan K, Ullah AH |
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Title | Site-directed mutagenesis of Aspergillus niger NRRL 3135 phytase at residue 300 to enhance catalysis at pH 4.0. |
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comments | According to the literature [1] & [3], His59 (PDB; 1ihp) makes the nucleophilic attack on the phosphorous atom to form a phosphohistidine intermediate. In the next step, the phosphohistidine is hydrolyzed by a water molecule. During the hydrolysis, the leaving group is protonated by a general acid, Asp339 (PDB; 1ihp).
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created | updated |
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2002-07-04 | 2009-02-26 |
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