EzCatDB: S00164
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DB codeS00164
CATH domainDomain 12.120.10.20 : NeuraminidaseCatalytic domain
E.C.3.1.3.8


Enzyme Name
UniProtKBKEGG

O66037
Protein name3-phytase3-phytase
1-phytase
phytase
phytate 1-phosphatase
phytate 6-phosphatase
SynonymsEC 3.1.3.8
Phytate 3-phosphatase
Myo-inositol-hexaphosphate 3-phosphohydrolase
PfamPF02333 (Phytase)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00562Inositol phosphate metabolism

UniProtKB:Accession NumberO66037
Entry namePHYT_BACSD
ActivityMyo-inositol hexakisphosphate + H(2)O = 1D- myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate.
Subunit
Subcellular locationSecreted.
Cofactor

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00076C01204C00001C04563C00009
CompoundCalciummyo-Inositol hexakisphosphateH2OD-myo-Inositol 1,2,4,5,6-pentakisphosphateOrthophosphate
Typedivalent metal (Ca2+, Mg2+)carbohydrate,phosphate group/phosphate ionH2Ocarbohydrate,phosphate group/phosphate ionphosphate group/phosphate ion
ChEBI29108
17401
15377
16507
26078
PubChem271

962
22247451

22486802
1004
             
1cvmAAnalogue:5x_CD,3x_CAUnbound UnboundUnbound
1pooABound:2x_CAUnbound UnboundUnbound
1qlgAAnalogue:2x_MG,3x_CAUnbound UnboundUnbound
2pooABound:6x_CAUnbound UnboundUnbound

Active-site residues
resource
literature [4]
pdbCofactor-binding residues
         
1cvmATYR 159;GLU 211;GLU 227;ASP 258;GLU 260;GLN 279(two catalytic Ca2+ binding)
1pooATYR 159;GLU 211;GLU 227;ASP 258;GLU 260;GLN 279(two catalytic Ca2+ binding)
1qlgATYR 159;GLU 211;GLU 227;ASP 258;GLU 260;GLN 279(two catalytic Ca2+ binding)
2pooATYR 159;GLU 211;GLU 227;ASP 258;GLU 260;GLN 279(two catalytic Ca2+ binding)

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[4]p.149-151

references
[1]
CommentsX-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
PubMed ID10089471
JournalActa Crystallogr D Biol Crystallogr
Year1999
Volume55
Pages691-3.
AuthorsHa NC, Kim YO, Oh TK, Oh BH
TitlePreliminary X-ray crystallographic analysis of a novel phytase from a Bacillus amyloliquefaciens strain.
Related PDB1cvm,2poo
Related UniProtKBO66037
[2]
PubMed ID10475631
JournalBr Poult Sci
Year1999
Volume40
Pages348-52.
AuthorsZanini SF, Sazzad MH
TitleEffects of microbial phytase on growth and mineral utilisation in broilers fed on maize soyabean-based diets.
[3]
PubMed ID11271819
JournalFolia Microbiol (Praha)
Year2000
Volume45
Pages128-32.
AuthorsDvorakova J, Kopecky J, Havlicek V, Kren V
TitleFormation of myo-inositol phosphates by Aspergillus niger 3-phytase.
[4]
CommentsX-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
PubMed ID10655618
JournalNat Struct Biol
Year2000
Volume7
Pages147-53.
AuthorsHa NC, Oh BC, Shin S, Kim HJ, Oh TK, Kim YO, Choi KY, Oh BH
TitleCrystal structures of a novel, thermostable phytase in partially and fully calcium-loaded states.
Related PDB1poo,1qlg
Related UniProtKBO66037
[5]
PubMed ID11164958
JournalJ Biotechnol
Year2001
Volume85
Pages15-24.
AuthorsJermutus L, Tessier M, Pasamontes L, van Loon AP, Lehmann M
TitleStructure-based chimeric enzymes as an alternative to directed enzyme evolution: phytase as a test case.

comments
According to the literature [4], there are six calcium-binding sites. Out of six binding sites, three low-affinity calcium-binding sites are located at the active site. In particular, two of the three calcium ions bound at the active site seem to be involved in catalysis, as the coordination geometries of the calcium ions, Ca5 and Ca6, are not complete. They might bind the phosphate groups of the substrate, and stabilize the pentacovalent transition state (see [4]).

createdupdated
2004-03-222009-04-15


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