DB code: T00053

RLCP classification 1.15.7910.1164 : Hydrolysis
CATH domain 4.10.460.10 : Inositol Polyphosphate 1-phosphatase; domain 1
3.30.540.10 : Fructose-1,6-Bisphosphatase; Chain A, domain 1 Catalytic domain
3.40.190.80 : D-Maltodextrin-Binding Protein; domain 2 Catalytic domain
E.C. 3.1.3.57
CSA 1inp
M-CSA 1inp
MACiE

CATH domain Related DB codes (homologues)
3.30.540.10 : Fructose-1,6-Bisphosphatase; Chain A, domain 1 D00148 D00153 D00491
3.40.190.80 : D-Maltodextrin-Binding Protein; domain 2 D00148 D00153 D00491

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P21327 Inositol polyphosphate 1-phosphatase
IPP
IPPase
EC 3.1.3.57
NP_776789.1 (Protein)
NM_174364.2 (DNA/RNA sequence)
PF00459 (Inositol_P)
[Graphical View]

KEGG enzyme name
inositol-1,4-bisphosphate 1-phosphatase
inositol-polyphosphate 1-phosphatase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P21327 INPP_BOVIN 1D-myo-inositol 1,4-bisphosphate + H(2)O = 1D- myo-inositol 4-phosphate + phosphate. Monomer. Magnesium.

KEGG Pathways
Map code Pathways E.C.
MAP04070 Phosphatidylinositol signaling system
MAP00562 Inositol phosphate metabolism

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00305 C01220 C00001 C01243 C03546 C00009 C04063
E.C.
Compound Magnesium D-myo-Inositol 1,4-bisphosphate H2O 1D-myo-Inositol 1,3,4-trisphosphate D-myo-Inositol 4-phosphate Orthophosphate D-myo-Inositol 3,4-bisphosphate
Type divalent metal (Ca2+, Mg2+) carbohydrate,phosphate group/phosphate ion H2O carbohydrate,phosphate group/phosphate ion carbohydrate,phosphate group/phosphate ion phosphate group/phosphate ion carbohydrate,phosphate group/phosphate ion
ChEBI 18420
17816
15377
18228
18384
26078
28858
PubChem 888
22247451
962
439455
1004
22486802
440211
1inpA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1inpA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:2x_MG Unbound Unbound Unbound Unbound Unbound
1inpA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
PDB;1inp & Swiss-prot;P21327 & literature [2], [7]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1inpA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1inpA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 54;THR 158 ASP 153;ASP 156(Magnesium-1 binding);GLU 79;ASP 153;ILE 155(Magnesium-2 binding)
1inpA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 317(Magnesium-1 binding)

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[2]
[3]
[7]
Fig.5, p.683

References
[1]
Resource
Comments
Medline ID
PubMed ID 2537096
Journal Biochim Biophys Acta
Year 1989
Volume 1001
Pages 134-44
Authors Hansen CA, Inubushi T, Williamson MT, Williamson JR
Title Partial purification of inositol polyphosphate 1-phosphomonoesterase with characterization of its substrates and products by nuclear magnetic resonance spectroscopy.
Related PDB
Related UniProtKB
[2]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Medline ID 95034747
PubMed ID 7947723
Journal Biochemistry
Year 1994
Volume 33
Pages 13164-71
Authors York JD, Ponder JW, Chen ZW, Mathews FS, Majerus PW
Title Crystal structure of inositol polyphosphate 1-phosphatase at 2.3-A resolution.
Related PDB 1inp
Related UniProtKB P21327
[3]
Resource
Comments
Medline ID
PubMed ID 7946962
Journal Cell Signal
Year 1994
Volume 6
Pages 355-62
Authors Luttrell BM
Title Cellular actions of inositol phosphates and other natural calcium and magnesium chelators.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 8107142
Journal J Mol Biol
Year 1994
Volume 236
Pages 584-9
Authors York JD, Chen ZW, Ponder JW, Chauhan AK, Mathews FS, Majerus PW
Title Crystallization and initial X-ray crystallographic characterization of recombinant bovine inositol polyphosphate 1-phosphatase produced in Spodoptera frugiperda cells.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 7761465
Journal Proc Natl Acad Sci U S A
Year 1995
Volume 92
Pages 5149-53
Authors York JD, Ponder JW, Majerus PW
Title Definition of a metal-dependent/Li(+)-inhibited phosphomonoesterase protein family based upon a conserved three-dimensional core structure.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 9762363
Journal Adv Enzyme Regul
Year 1998
Volume 38
Pages 365-74
Authors York JD, Xiong JP, Spiegelberg B
Title Nuclear inositol signaling: a structural and functional approach.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 11812139
Journal J Mol Biol
Year 2002
Volume 315
Pages 677-85
Authors Patel S, Yenush L, Rodriguez PL, Serrano R, Blundell TL
Title Crystal structure of an enzyme displaying both inositol-polyphosphate-1-phosphatase and 3'-phosphoadenosine-5'-phosphate phosphatase activities: a novel target of lithium therapy.
Related PDB
Related UniProtKB

Comments
This enzyme is homologous to PIPase(DB code;D00491) with a similar active site, suggesting that it has a similar mechanism to that of the homologous enzyme.

Created Updated
2005-09-06 2009-02-26