_EC 3.1.3.25 Inositol-phosphate phosphatase. 29 PDB entries  
EC 3.-.-.- Hydrolases. [21,057 PDB entries]
EC 3.1.-.- Acting on ester bonds. [5,979 PDB entries]
EC 3.1.3.- Phosphoric monoester hydrolases. [1,340 PDB entries]
EC 3.1.3.25 Inositol-phosphate phosphatase. [29 PDB entries]    
1awb

Pathway: myo-Inositol Biosynthesis
Reaction: Myo-inositol phosphate + H(2)O = myo-inositol + phosphate.
 

Myo-inositol phosphate
+ H(2)O
=
myo-inositol
+
phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.

Other name(s): Inositol 1-phosphatase. Inositol monophosphate phosphatase. Inositol phosphatase. Inositol-1(or 4)-monophosphatase. L-myo-inositol-1-phosphate phosphatase. Myo-inositol 1-phosphatase. Myo-inositol monophosphatase. Myo-inositol-1(or 4)-monophosphatase. Myo-inositol-1(or 4)-phosphate phosphohydrolase. Myo-inositol-1-phosphatase.
Comments: Acts on five of the six isomers of myo-inositol phosphate, all except myo-inositol 2-phosphate, but does not act on myo-inositol bearing more than one phosphate group. It also acts on adenosine 2'-phosphate (but not the 3'- or 5'-phosphates), sn-glycerol 3-phosphate and glycerol 2-phosphate, but does not act on inositol bisphosphates or more phosphorylated inositols.
Links:   [IntEnz]   [ExPASy]   [KEGG]  

There are 29 PDB entries in enzyme class E.C.3.1.3.25

  PDB code Protein
1awb
Human myo-inositol monophosphatase in complex with d- inositol-1-phosphate and calcium
Source: Homo sapiens. Human. Organism_taxid: 9606. Cell_line: bl21. Organ: brain. Cellular_location: cytoplasm. Gene: impa. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (272 residues) CATH domains: 3.30.540.10 3.40.190.80
Bound ligand:   Het Group IPD is 75.00% similar to enzyme product Myo-inositol
1dk4
Crystal structure of mj0109 gene product inositol monophosphatase
Source: Methanocaldococcus jannaschii. Organism_taxid: 2190. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (252 residues) CATH domains: 3.30.540.10 3.40.190.80
1g0h
Crystal structure of mj0109 gene product inositol monophosphatase-fructose 1,6 bisphosphatase
Source: Methanocaldococcus jannaschii. Organism_taxid: 2190. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (252 residues) CATH domains: 3.30.540.10 3.40.190.80
1g0i
Crystal structure of mj0109 gene product inositol monophosphatase-fructose 1,6 bisphosphatase
Source: Methanocaldococcus jannaschii. Organism_taxid: 2190. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (252 residues) CATH domains: 3.30.540.10 3.40.190.80
1ima
Structural analysis of inositol monophosphatase complexes wi substrates
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: brain. Gene: cdna
Chains: A, B (273 residues) CATH domains: 3.30.540.10 3.40.190.80
Bound ligand:   Het Group IPD is 75.00% similar to enzyme product Myo-inositol
1imb
Structural analysis of inositol monophosphatase complexes wi substrates
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: brain. Gene: cdna
Chains: A, B (273 residues) CATH domains: 3.30.540.10 3.40.190.80
Bound ligand:   Het Group LIP is 75.00% similar to enzyme product Myo-inositol
1imc
Structural studies of metal binding by inositol monophosphatase: evidence for two-metal ion catalysis
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: brain. Gene: cdna
Chains: A, B (267 residues) CATH domains: 3.30.540.10 3.40.190.80
1imd
Structural studies of metal binding by inositol monophosphatase: evidence for two-metal ion catalysis
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: brain. Gene: cdna
Chains: A, B (267 residues) CATH domains: 3.30.540.10 3.40.190.80
Bound ligand:   Het Group PO4 corresponds to enzyme product phosphate
1ime
Structural studies of metal binding by inositol monophosphatase: evidence for two-metal ion catalysis
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: brain. Gene: cdna
Chains: A, B (273 residues) CATH domains: 3.30.540.10 3.40.190.80
1imf
Structural studies of metal binding by inositol monophosphat evidence for two-metal ion catalysis
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: brain. Gene: cdna
Chain: A (264 residues) CATH domains: 3.30.540.10 3.40.190.80
1lbv
Crystal structure of apo-form (p21) of dual activity fbpase/impase (af2372) from archaeoglobus fulgidus
Source: Archaeoglobus fulgidus. Organism_taxid: 2234. Gene: af2372. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (252 residues) CATH domains: 3.30.540.10 3.40.190.80
1lbw
Crystal structure of apo-form (p32) of dual activity fbpase/impase (af2372) from archaeoglobus fulgidus
Source: Archaeoglobus fulgidus. Organism_taxid: 2234. Gene: af2372. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (252 residues) CATH domains: 3.30.540.10 3.40.190.80
1lbx
Crystal structure of a ternary complex of dual activity fbpase/impase (af2372) from archaeoglobus fulgidus with calcium ions and d-myo-inositol-1-phosphate
Source: Archaeoglobus fulgidus. Organism_taxid: 2234. Gene: af2372. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (252 residues) CATH domains: 3.30.540.10 3.40.190.80
1lby
Crystal structure of a complex (p32 crystal form) of dual activity fbpase/impase (af2372) from archaeoglobus fulgidus with 3 manganese ions, fructose-6-phosphate, and phosphate ion
Source: Archaeoglobus fulgidus. Organism_taxid: 2234. Gene: af2372. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (252 residues) CATH domains: 3.30.540.10 3.40.190.80
1lbz
Crystal structure of a complex (p32 crystal form) of dual activity fbpase/impase (af2372) from archaeoglobus fulgidus with 3 calcium ions and fructose-1,6 bisphosphate
Source: Archaeoglobus fulgidus. Organism_taxid: 2234. Gene: af2372. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (252 residues) CATH domains: 3.30.540.10 3.40.190.80
2bji
High resolution structure of myo-inositol monophosphatase, the target of lithium therapy
Source: Bos taurus. Bovine. Organism_taxid: 9913. Organ: brain. Expressed in: escherichia coli. Expression_system_taxid: 511693. Expression_system_cell_line: de3.
Chains: A, B (275 residues) CATH domains: 3.30.540.10 3.40.190.80
2czh
Crystal structure of human myo-inositol monophosphatase 2 (impa2) with phosphate ion (orthorhombic form)
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: impa2. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (254 residues) CATH domains: 3.30.540.10 3.40.190.80
Bound ligand:   Het Group PO4 corresponds to enzyme product phosphate
2czi
Crystal structure of human myo-inositol monophosphatase 2 (impa2) with calcium and phosphate ions
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: impa2. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (259 residues) CATH domains: 3.30.540.10 3.40.190.80
Bound ligand:   Het Group PO4 corresponds to enzyme product phosphate
2czk
Crystal structure of human myo-inositol monophosphatase 2 (i (trigonal form)
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: impa2. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (253 residues) CATH domains: 3.30.540.10 3.40.190.80
2ddk
Crystal structure of human myo-inositol monophosphatase 2 (impa2) (orthorhombic form)
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: impa2, imp.18p. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (258 residues) CATH domains: 3.30.540.10 3.40.190.80
2fvz
Human inositol monophosphosphatase 2
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: impa2, imp.18p. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B, C, D (244 residues) CATH domains: 3.30.540.10 3.40.190.80
2hhm
Structure of inositol monophosphatase, the putative target of lithium therapy
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: brain
Chains: A, B (272 residues) CATH domains: 3.30.540.10 3.40.190.80
2p3n
Thermotoga maritima impase tm1415
Source: Thermotoga maritima. Organism_taxid: 243274. Strain: msb8. Gene: suhb. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
Chains: A, B, C, D (256 residues) CATH domains: 3.30.540.10 3.40.190.80
2p3v
Thermotoga maritima impase tm1415
Source: Thermotoga maritima. Organism_taxid: 243274. Strain: msb8. Gene: suhb. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
Chains: A, B, C, D (254 residues) CATH domains: 3.30.540.10 3.40.190.80
2pcr
Crystal structure of myo-inositol-1(or 4)-monophosphatase (a from aquifex aeolicus vf5
Source: Aquifex aeolicus. Organism_taxid: 224324. Strain: vf5. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (238 residues) CATH domains: 3.30.540.10 3.40.190.80
2q74
Mycobacterium tuberculosis suhb
Source: Mycobacterium tuberculosis. Organism_taxid: 83332. Strain: h37rv. Gene: suhb. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C (245 residues) CATH domains: 3.30.540.10 3.40.190.80
2qfl
Structure of suhb: inositol monophosphatase and extragenic suppressor from e. Coli
Source: Escherichia coli. Organism_taxid: 562. Gene: suhb, ssya. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
Chain: A (262 residues) CATH domains: 3.30.540.10 3.40.190.80
4as4
Structure of human inositol monophosphatase 1
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: plyss.
Chains: A, B (274 residues) CATH domains: 3.30.540.10 3.40.190.80
Bound ligands:   Het Group GOL is 50.00% similar to enzyme product Myo-inositol
  Het Group PO4 corresponds to enzyme product phosphate
4as5
Structure of mouse inositol monophosphatase 1
Source: Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_variant: plyss.
Chains: A, B, C, D (274 residues) CATH domains: 3.30.540.10 3.40.190.80
Bound ligands:   Het Group GOL is 50.00% similar to enzyme product Myo-inositol
  Het Group PO4 corresponds to enzyme product phosphate