DB code: D00460

RLCP classification 1.15.32000.86 : Hydrolysis
CATH domain 3.40.50.1240 : Rossmann fold Catalytic domain
1.10.910.10 :
E.C. 3.1.3.8
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.40.50.1240 : Rossmann fold S00365 S00363 S00366 D00514

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam
P34752 3-phytase A
EC 3.1.3.8
3 phytase A
Myo-inositol hexakisphosphate phosphohydrolase A
Myo-inositol-hexaphosphate 3-phosphohydrolase A
PF00328 (His_Phos_2)
[Graphical View]
P34755 3-phytase B
EC 3.1.3.8
Myo-inositol-hexaphosphate 3-phosphohydrolase B
pH 2.5 optimum acid phosphatase
PF00328 (His_Phos_2)
[Graphical View]

KEGG enzyme name
3-phytase
1-phytase
phytase
phytate 1-phosphatase
phytate 6-phosphatase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P34755 PHYB_ASPAW Myo-inositol hexakisphosphate + H(2)O = 1D- myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate. Homodimer.
P34752 PHYA_ASPNG Myo-inositol hexakisphosphate + H(2)O = 1D- myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate. Secreted.

KEGG Pathways
Map code Pathways E.C.
MAP00562 Inositol phosphate metabolism

Compound table
Substrates Products Intermediates
KEGG-id C01204 C00001 C04563 C00009
E.C.
Compound myo-Inositol hexakisphosphate H2O D-myo-Inositol 1,2,4,5,6-pentakisphosphate Orthophosphate
Type carbohydrate,phosphate group/phosphate ion H2O carbohydrate,phosphate group/phosphate ion phosphate group/phosphate ion
ChEBI 17401
15377
16507
26078
PubChem 22247451
962
1004
22486802
1ihpA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1qfxA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1qfxB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1ihpA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [1] & [3]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1ihpA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 59;ASP 339
1qfxA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 63;ASP 319
1qfxB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 63;ASP 319
1ihpA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[1]
p.189
[3]
p.970
[4]
p.111

References
[1]
Resource
Comments X-ray crystallography (2.5 Angstroms)
Medline ID
PubMed ID 9164457
Journal Nat Struct Biol
Year 1997
Volume 4
Pages 185-90
Authors Kostrewa D, Gruninger-Leitch F, D'Arcy A, Broger C, Mitchell D, van Loon AP
Title Crystal structure of phytase from Aspergillus ficuum at 2.5 A resolution.
Related PDB 1ihp
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 9925555
Journal Appl Environ Microbiol
Year 1999
Volume 65
Pages 367-73
Authors Wyss M, Brugger R, Kronenberger A, Remy R, Fimbel R, Oesterhelt G, Lehmann M, van Loon AP
Title Biochemical characterization of fungal phytases (myo-inositol hexakisphosphate phosphohydrolases): catalytic properties.
Related PDB
Related UniProtKB
[3]
Resource
Comments X-ray crystallography (2.4 Angstroms)
Medline ID
PubMed ID 10329192
Journal J Mol Biol
Year 1999
Volume 288
Pages 965-74
Authors Kostrewa D, Wyss M, D'Arcy A, van Loon AP
Title Crystal structure of Aspergillus niger pH 2.5 acid phosphatase at 2. 4 A resolution.
Related PDB 1qfx
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 10655611
Journal Nat Struct Biol
Year 2000
Volume 7
Pages 108-13
Authors Lim D, Golovan S, Forsberg CW, Jia Z
Title Crystal structures of Escherichia coli phytase and its complex with phytate.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 10788605
Journal FEBS Lett
Year 2000
Volume 472
Pages 169-72
Authors Tomschy A, Wyss M, Kostrewa D, Vogel K, Tessier M, Hofer S, Burgin H, Kronenberger A, Remy R, van Loon AP, Pasamontes L
Title Active site residue 297 of Aspergillus niger phytase critically affects the catalytic properties.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 10933495
Journal Protein Sci
Year 2000
Volume 9
Pages 1304-11
Authors Tomschy A, Tessier M, Wyss M, Brugger R, Broger C, Schnoebelen L, van Loon AP, Pasamontes L
Title Optimization of the catalytic properties of Aspergillus fumigatus phytase based on the three-dimensional structure.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 10973795
Journal Biochem Biophys Res Commun
Year 2000
Volume 275
Pages 759-63
Authors Mullaney EJ, Daly CB, Sethumadhavan K, Rodriquez E, Lei XG, Ullah AH
Title Phytase activity in Aspergillus fumigatus isolates.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 11051103
Journal Arch Biochem Biophys
Year 2000
Volume 382
Pages 105-12
Authors Rodriguez E, Wood ZA, Karplus PA, Lei XG
Title Site-directed mutagenesis improves catalytic efficiency and thermostability of Escherichia coli pH 2.5 acid phosphatase/phytase expressed in Pichia pastoris.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 12359257
Journal Biochem Biophys Res Commun
Year 2002
Volume 297
Pages 1016-20
Authors Mullaney EJ, Daly CB, Kim T, Porres JM, Lei XG, Sethumadhavan K, Ullah AH
Title Site-directed mutagenesis of Aspergillus niger NRRL 3135 phytase at residue 300 to enhance catalysis at pH 4.0.
Related PDB
Related UniProtKB

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).

Created Updated
2002-07-04 2009-02-26