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-hexaphosphate 3-phosphohydrolase A
Myo-inositol hexakisphosphate 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
P34752 PHYA_ASPNG Myo-inositol hexakisphosphate + H(2)O = 1D- myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate. Secreted.
P34755 PHYB_ASPAW Myo-inositol hexakisphosphate + H(2)O = 1D- myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate. Homodimer.

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
 17401
 		15377
 15377
 		16507
 16507
 		26078
 26078
PubChem 22247451
 962
 22247451
 962
 		1004
 22486802
 1004
 22486802
1ihpA01 Unbound Unbound Unbound
1qfxA Unbound Unbound Unbound
1qfxB Unbound Unbound Unbound
1ihpA02 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 HIS 59;ASP 339
1qfxA HIS 63;ASP 319
1qfxB HIS 63;ASP 319
1ihpA02

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