DB code: D00491

RLCP classification 1.15.7910.1164 : Hydrolysis
CATH domain 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. 3.1.3.7 3.1.3.57
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.40.190.80 : D-Maltodextrin-Binding Protein; domain 2 D00148 D00153 T00053
3.30.540.10 : Fructose-1,6-Bisphosphatase; Chain A, domain 1 D00148 D00153 T00053

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
Q9Z1N4 3''(2''),5''-bisphosphate nucleotidase 1
EC 3.1.3.7
Bisphosphate 3''-nucleotidase 1
PAP-inositol 1,4-phosphatase
PIP
scHAL2 analogous 3
NP_741987.1 (Protein)
NM_171990.2 (DNA/RNA sequence)
PF00459 (Inositol_P)
[Graphical View]

KEGG enzyme name
3'(2'),5'-bisphosphate nucleotidase
(EC 3.1.3.7 )
phosphoadenylate 3'-nucleotidase
(EC 3.1.3.7 )
3'-phosphoadenylylsulfate 3'-phosphatase
(EC 3.1.3.7 )
phosphoadenylate 3'-nucleotidase
(EC 3.1.3.7 )
3'(2'),5'-bisphosphonucleoside 3'(2')-phosphohydrolase
(EC 3.1.3.7 )
inositol-1,4-bisphosphate 1-phosphatase
(EC 3.1.3.57 )
inositol-polyphosphate 1-phosphatase
(EC 3.1.3.57 )

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
Q9Z1N4 BPNT1_RAT Adenosine 3'',5''-bisphosphate + H(2)O = adenosine 5''-phosphate + phosphate. Magnesium.

KEGG Pathways
Map code Pathways E.C.
MAP00562 Inositol phosphate metabolism 3.1.3.57
MAP00920 Sulfur metabolism 3.1.3.7
MAP04070 Phosphatidylinositol signaling system 3.1.3.57

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00305 C00054 C00053 C01220 C01243 C00001 C00009 C00020 C00224 C03546 C04063
E.C. 3.1.3.7
3.1.3.57
3.1.3.7
3.1.3.7
3.1.3.57
3.1.3.57
3.1.3.7
3.1.3.57
3.1.3.7
3.1.3.57
3.1.3.7
3.1.3.7
3.1.3.57
3.1.3.57
Compound Magnesium Adenosine 3',5'-bisphosphate 3'-Phosphoadenylylsulfate D-myo-Inositol 1,4-bisphosphate 1D-myo-Inositol 1,3,4-trisphosphate H2O Orthophosphate Adenosine 5'-phosphate Adenylylsulfate D-myo-Inositol 4-phosphate D-myo-Inositol 3,4-bisphosphate
Type divalent metal (Ca2+, Mg2+) amine group,nucleotide amine group,nucleotide ,sulfate group carbohydrate,phosphate group/phosphate ion carbohydrate,phosphate group/phosphate ion H2O phosphate group/phosphate ion amine group,nucleotide amine group,nucleotide ,sulfate group carbohydrate,phosphate group/phosphate ion carbohydrate,phosphate group/phosphate ion
ChEBI 18420
17985
17980
17816
18228
15377
26078
16027
17709
18384
28858
PubChem 888
159296
10214
439455
22247451
962
1004
22486802
6083
10238
440211
1jp4A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:3x_MG Unbound Unbound Unbound Unbound Bound:PO4 Unbound Unbound Unbound Unbound
1jp4A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Bound:AMP Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
PDB;1jp4 & Swiss-prot;Q9Z1N4 & literature [9]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1jp4A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 51;THR 122 GLU 74(Magnesium-1 & -3);ASP 117(Magnesium-1 & -2);VAL 119(Magnesium-1);ASP 120(Magnesium-2) GLY 121;THR 122
1jp4A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 247(Magnesium-2)

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[8]
Fig.3, p.1092
[9]
Fig.5, p.681-682

References
[1]
Resource
Comments
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
Related UniProtKB
[2]
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
[3]
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
[4]
Resource
Comments
Medline ID
PubMed ID 7493934
Journal J Biol Chem
Year 1995
Volume 270
Pages 29105-10
Authors Peng Z, Verma DP
Title A rice HAL2-like gene encodes a Ca(2+)-sensitive 3'(2'),5'-diphosphonucleoside 3'(2')-phosphohydrolase and complements yeast met22 and Escherichia coli cysQ mutations.
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 20123982
PubMed ID 10656801
Journal J Mol Biol
Year 2000
Volume 295
Pages 927-38
Authors Albert A, Yenush L, Gil-Mascarell MR, Rodriguez PL, Patel S, Martinez-Ripoll M, Blundell TL, Serrano R
Title X-ray structure of yeast Hal2p, a major target of lithium and sodium toxicity, and identification of framework interactions determining cation sensitivity.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 12126627
Journal J Mol Biol
Year 2002
Volume 320
Pages 1087-94
Authors Patel S, Martinez-Ripoll M, Blundell TL, Albert A
Title Structural enzymology of Li(+)-sensitive/Mg(2+)-dependent phosphatases.
Related PDB
Related UniProtKB
[9]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 5-308.
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 1jp4
Related UniProtKB Q9Z1N4

Comments
This enzyme belongs to the inositol monophosphatase family.
This enzyme has got both the catalytic activities of phosphoadenylate 3'-nucleotidase (PAPase; EC 3.1.3.7) and inositol-polyphosphate 1-phosphatase (IPPase;EC 3.1.3.57).
This enzyme binds three magnesium ions, according to the literature [9]. The mechanism of this enzyme is similar to that of its homologous enzymes (D00148, D00153 & T00053 in EzCatDB).

Created Updated
2004-02-19 2009-02-26