DB code: S00164

CATH domain 2.120.10.20 : Neuraminidase Catalytic domain
E.C. 3.1.3.8
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam
O66037 3-phytase
EC 3.1.3.8
Phytate 3-phosphatase
Myo-inositol-hexaphosphate 3-phosphohydrolase
PF02333 (Phytase)
[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
O66037 PHYT_BACSD 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
Cofactors Substrates Products Intermediates
KEGG-id C00076 C01204 C00001 C04563 C00009
E.C.
Compound Calcium myo-Inositol hexakisphosphate H2O D-myo-Inositol 1,2,4,5,6-pentakisphosphate Orthophosphate
Type divalent metal (Ca2+, Mg2+) carbohydrate,phosphate group/phosphate ion H2O carbohydrate,phosphate group/phosphate ion phosphate group/phosphate ion
ChEBI 29108
17401
15377
16507
26078
PubChem 271
22247451
962
1004
22486802
1cvmA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:5x_CD,3x_CA Unbound Unbound Unbound
1pooA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:2x_CA Unbound Unbound Unbound
1qlgA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:2x_MG,3x_CA Unbound Unbound Unbound
2pooA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:6x_CA Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [4]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1cvmA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 159;GLU 211;GLU 227;ASP 258;GLU 260;GLN 279(two catalytic Ca2+ binding)
1pooA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 159;GLU 211;GLU 227;ASP 258;GLU 260;GLN 279(two catalytic Ca2+ binding)
1qlgA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 159;GLU 211;GLU 227;ASP 258;GLU 260;GLN 279(two catalytic Ca2+ binding)
2pooA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 159;GLU 211;GLU 227;ASP 258;GLU 260;GLN 279(two catalytic Ca2+ binding)

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[4]
p.149-151

References
[1]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
Medline ID
PubMed ID 10089471
Journal Acta Crystallogr D Biol Crystallogr
Year 1999
Volume 55
Pages 691-3.
Authors Ha NC, Kim YO, Oh TK, Oh BH
Title Preliminary X-ray crystallographic analysis of a novel phytase from a Bacillus amyloliquefaciens strain.
Related PDB 1cvm 2poo
Related UniProtKB O66037
[2]
Resource
Comments
Medline ID
PubMed ID 10475631
Journal Br Poult Sci
Year 1999
Volume 40
Pages 348-52.
Authors Zanini SF, Sazzad MH
Title Effects of microbial phytase on growth and mineral utilisation in broilers fed on maize soyabean-based diets.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 11271819
Journal Folia Microbiol (Praha)
Year 2000
Volume 45
Pages 128-32.
Authors Dvorakova J, Kopecky J, Havlicek V, Kren V
Title Formation of myo-inositol phosphates by Aspergillus niger 3-phytase.
Related PDB
Related UniProtKB
[4]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
Medline ID
PubMed ID 10655618
Journal Nat Struct Biol
Year 2000
Volume 7
Pages 147-53.
Authors Ha NC, Oh BC, Shin S, Kim HJ, Oh TK, Kim YO, Choi KY, Oh BH
Title Crystal structures of a novel, thermostable phytase in partially and fully calcium-loaded states.
Related PDB 1poo 1qlg
Related UniProtKB O66037
[5]
Resource
Comments
Medline ID
PubMed ID 11164958
Journal J Biotechnol
Year 2001
Volume 85
Pages 15-24.
Authors Jermutus L, Tessier M, Pasamontes L, van Loon AP, Lehmann M
Title Structure-based chimeric enzymes as an alternative to directed enzyme evolution: phytase as a test case.
Related PDB
Related UniProtKB

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]).

Created Updated
2004-03-22 2009-04-15