EzCatDB: D00460
Related links:    PDB-formatted query search system Fasta-formatted query search system Fasta-formatted query search system

DB codeD00460
RLCP classification1.15.32000.86 : Hydrolysis
CATH domainDomain 13.40.50.1240 : Rossmann foldCatalytic domain
Domain 21.10.910.10
E.C.3.1.3.8

CATH domainRelated DB codes (homologues)
3.40.50.1240 : Rossmann foldS00365,S00363,S00366,D00514

Enzyme Name
UniProtKBKEGG

P34752P34755
Protein name3-phytase A3-phytase B3-phytase
1-phytase
phytase
phytate 1-phosphatase
phytate 6-phosphatase
SynonymsEC 3.1.3.8
3 phytase A
Myo-inositol-hexaphosphate 3-phosphohydrolase A
Myo-inositol hexakisphosphate phosphohydrolase A
EC 3.1.3.8
Myo-inositol-hexaphosphate 3-phosphohydrolase B
pH 2.5 optimum acid phosphatase
PfamPF00328 (His_Phos_2)
[Graphical view]
PF00328 (His_Phos_2)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00562Inositol phosphate metabolism

UniProtKB:Accession NumberP34752P34755
Entry namePHYA_ASPNGPHYB_ASPAW
ActivityMyo-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.
Subunit
Homodimer.
Subcellular locationSecreted.
Cofactor


Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC01204C00001C04563C00009
Compoundmyo-Inositol hexakisphosphateH2OD-myo-Inositol 1,2,4,5,6-pentakisphosphateOrthophosphate
Typecarbohydrate,phosphate group/phosphate ionH2Ocarbohydrate,phosphate group/phosphate ionphosphate group/phosphate ion
ChEBI17401
15377
16507
26078
PubChem
962
22247451

22486802
1004
            
1ihpA01Unbound UnboundUnbound
1qfxAUnbound UnboundUnbound
1qfxBUnbound UnboundUnbound
1ihpA02Unbound UnboundUnbound

Active-site residues
resource
literature [1] & [3]
pdbCatalytic residues
         
1ihpA01HIS 59;ASP 339
1qfxAHIS 63;ASP 319
1qfxBHIS 63;ASP 319
1ihpA02 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[1]p.189
[3]p.970
[4]p.111

references
[1]
CommentsX-ray crystallography (2.5 Angstroms)
PubMed ID9164457
JournalNat Struct Biol
Year1997
Volume4
Pages185-90
AuthorsKostrewa D, Gruninger-Leitch F, D'Arcy A, Broger C, Mitchell D, van Loon AP
TitleCrystal structure of phytase from Aspergillus ficuum at 2.5 A resolution.
Related PDB1ihp
[2]
PubMed ID9925555
JournalAppl Environ Microbiol
Year1999
Volume65
Pages367-73
AuthorsWyss M, Brugger R, Kronenberger A, Remy R, Fimbel R, Oesterhelt G, Lehmann M, van Loon AP
TitleBiochemical characterization of fungal phytases (myo-inositol hexakisphosphate phosphohydrolases): catalytic properties.
[3]
CommentsX-ray crystallography (2.4 Angstroms)
PubMed ID10329192
JournalJ Mol Biol
Year1999
Volume288
Pages965-74
AuthorsKostrewa D, Wyss M, D'Arcy A, van Loon AP
TitleCrystal structure of Aspergillus niger pH 2.5 acid phosphatase at 2. 4 A resolution.
Related PDB1qfx
[4]
PubMed ID10655611
JournalNat Struct Biol
Year2000
Volume7
Pages108-13
AuthorsLim D, Golovan S, Forsberg CW, Jia Z
TitleCrystal structures of Escherichia coli phytase and its complex with phytate.
[5]
PubMed ID10788605
JournalFEBS Lett
Year2000
Volume472
Pages169-72
AuthorsTomschy A, Wyss M, Kostrewa D, Vogel K, Tessier M, Hofer S, Burgin H, Kronenberger A, Remy R, van Loon AP, Pasamontes L
TitleActive site residue 297 of Aspergillus niger phytase critically affects the catalytic properties.
[6]
PubMed ID10933495
JournalProtein Sci
Year2000
Volume9
Pages1304-11
AuthorsTomschy A, Tessier M, Wyss M, Brugger R, Broger C, Schnoebelen L, van Loon AP, Pasamontes L
TitleOptimization of the catalytic properties of Aspergillus fumigatus phytase based on the three-dimensional structure.
[7]
PubMed ID10973795
JournalBiochem Biophys Res Commun
Year2000
Volume275
Pages759-63
AuthorsMullaney EJ, Daly CB, Sethumadhavan K, Rodriquez E, Lei XG, Ullah AH
TitlePhytase activity in Aspergillus fumigatus isolates.
[8]
PubMed ID11051103
JournalArch Biochem Biophys
Year2000
Volume382
Pages105-12
AuthorsRodriguez E, Wood ZA, Karplus PA, Lei XG
TitleSite-directed mutagenesis improves catalytic efficiency and thermostability of Escherichia coli pH 2.5 acid phosphatase/phytase expressed in Pichia pastoris.
[9]
PubMed ID12359257
JournalBiochem Biophys Res Commun
Year2002
Volume297
Pages1016-20
AuthorsMullaney EJ, Daly CB, Kim T, Porres JM, Lei XG, Sethumadhavan K, Ullah AH
TitleSite-directed mutagenesis of Aspergillus niger NRRL 3135 phytase at residue 300 to enhance catalysis at pH 4.0.

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).

createdupdated
2002-07-042009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
© Biotechnology Research Institute for Drug Discovery, AIST, 2015-2016 All Rights Reserved.
© Computational Biology Research Center, AIST, 2004-2016 All Rights Reserved.