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
IPPase
IPP
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.
MAP00562 Inositol phosphate metabolism
MAP04070 Phosphatidylinositol signaling system

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
 18420
 		17816
 17816
 		15377
 15377
 		18228
 18228
 		18384
 18384
 		26078
 26078
 		28858
 28858
PubChem 888
 888
 		22247451
 962
 22247451
 962
 		439455
 439455
 		1004
 22486802
 1004
 22486802
 		440211
 440211
1inpA01 Unbound Unbound Unbound Unbound Unbound Unbound
1inpA02 Bound:2x_MG Unbound Unbound Unbound Unbound Unbound
1inpA03 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
1inpA02 ASP 54;THR 158 ASP 153;ASP 156(Magnesium-1 binding);GLU 79;ASP 153;ILE 155(Magnesium-2 binding)
1inpA03 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