EzCatDB: D00491
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DB codeD00491
RLCP classification1.15.7910.1164 : Hydrolysis
CATH domainDomain 13.30.540.10 : Fructose-1,6-Bisphosphatase; Chain A, domain 1Catalytic domain
Domain 23.40.190.80 : D-Maltodextrin-Binding Protein; domain 2Catalytic domain
E.C.3.1.3.7,3.1.3.57

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

Enzyme Name
UniProtKBKEGG

Q9Z1N4
Protein name3''(2''),5''-bisphosphate nucleotidase 13'(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)

SynonymsEC 3.1.3.7
Bisphosphate 3''-nucleotidase 1
PAP-inositol-1,4-phosphatase
PIP
scHAL2 analogous 3
RefSeqNP_741987.1 (Protein)
NM_171990.2 (DNA/RNA sequence)
PfamPF00459 (Inositol_P)
[Graphical view]

KEGG pathways
MAP codePathwaysE.C.
MAP00562Inositol phosphate metabolism3.1.3.57
MAP00920Sulfur metabolism3.1.3.7
MAP04070Phosphatidylinositol signaling system3.1.3.57

UniProtKB:Accession NumberQ9Z1N4
Entry nameBPNT1_RAT
ActivityAdenosine 3'',5''-bisphosphate + H(2)O = adenosine 5''-phosphate + phosphate.
Subunit
Subcellular location
CofactorMagnesium.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00305C00054C00053C01220C01243C00001C00009C00020C00224C03546C04063
E.C.3.1.3.7,3.1.3.573.1.3.73.1.3.73.1.3.573.1.3.573.1.3.7,3.1.3.573.1.3.7,3.1.3.573.1.3.73.1.3.73.1.3.573.1.3.57
CompoundMagnesiumAdenosine 3',5'-bisphosphate3'-PhosphoadenylylsulfateD-myo-Inositol 1,4-bisphosphate1D-myo-Inositol 1,3,4-trisphosphateH2OOrthophosphateAdenosine 5'-phosphateAdenylylsulfateD-myo-Inositol 4-phosphateD-myo-Inositol 3,4-bisphosphate
Typedivalent metal (Ca2+, Mg2+)amine group,nucleotideamine group,nucleotide,sulfate groupcarbohydrate,phosphate group/phosphate ioncarbohydrate,phosphate group/phosphate ionH2Ophosphate group/phosphate ionamine group,nucleotideamine group,nucleotide,sulfate groupcarbohydrate,phosphate group/phosphate ioncarbohydrate,phosphate group/phosphate ion
ChEBI18420
17985
17980
17816
18228
15377
26078
16027
17709
18384
28858
PubChem888
159296
10214

439455
962
22247451
22486802
1004
6083
10238

440211
                   
1jp4A01Bound:3x_MGUnboundUnboundUnboundUnbound Bound:PO4UnboundUnboundUnboundUnbound
1jp4A02UnboundUnboundUnboundUnboundUnbound UnboundBound:AMPUnboundUnboundUnbound

Active-site residues
resource
PDB;1jp4 & Swiss-prot;Q9Z1N4 & literature [9]
pdbCatalytic residuesCofactor-binding residuesMain-chain involved in catalysis
           
1jp4A01ASP 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 
ASP 247(Magnesium-2)
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[8]Fig.3, p.1092
[9]Fig.5, p.681-682

references
[1]
Medline ID95034747
PubMed ID7947723
JournalBiochemistry
Year1994
Volume33
Pages13164-71
AuthorsYork JD, Ponder JW, Chen ZW, Mathews FS, Majerus PW
TitleCrystal structure of inositol polyphosphate 1-phosphatase at 2.3-A resolution.
[2]
PubMed ID7946962
JournalCell Signal
Year1994
Volume6
Pages355-62
AuthorsLuttrell BM
TitleCellular actions of inositol phosphates and other natural calcium and magnesium chelators.
[3]
PubMed ID8107142
JournalJ Mol Biol
Year1994
Volume236
Pages584-9
AuthorsYork JD, Chen ZW, Ponder JW, Chauhan AK, Mathews FS, Majerus PW
TitleCrystallization and initial X-ray crystallographic characterization of recombinant bovine inositol polyphosphate 1-phosphatase produced in Spodoptera frugiperda cells.
[4]
PubMed ID7493934
JournalJ Biol Chem
Year1995
Volume270
Pages29105-10
AuthorsPeng Z, Verma DP
TitleA 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.
[5]
PubMed ID7761465
JournalProc Natl Acad Sci U S A
Year1995
Volume92
Pages5149-53
AuthorsYork JD, Ponder JW, Majerus PW
TitleDefinition of a metal-dependent/Li(+)-inhibited phosphomonoesterase protein family based upon a conserved three-dimensional core structure.
[6]
PubMed ID9762363
JournalAdv Enzyme Regul
Year1998
Volume38
Pages365-74
AuthorsYork JD, Xiong JP, Spiegelberg B
TitleNuclear inositol signaling: a structural and functional approach.
[7]
Medline ID20123982
PubMed ID10656801
JournalJ Mol Biol
Year2000
Volume295
Pages927-38
AuthorsAlbert A, Yenush L, Gil-Mascarell MR, Rodriguez PL, Patel S, Martinez-Ripoll M, Blundell TL, Serrano R
TitleX-ray structure of yeast Hal2p, a major target of lithium and sodium toxicity, and identification of framework interactions determining cation sensitivity.
[8]
PubMed ID12126627
JournalJ Mol Biol
Year2002
Volume320
Pages1087-94
AuthorsPatel S, Martinez-Ripoll M, Blundell TL, Albert A
TitleStructural enzymology of Li(+)-sensitive/Mg(2+)-dependent phosphatases.
[9]
CommentsX-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 5-308.
PubMed ID11812139
JournalJ Mol Biol
Year2002
Volume315
Pages677-85
AuthorsPatel S, Yenush L, Rodriguez PL, Serrano R, Blundell TL
TitleCrystal structure of an enzyme displaying both inositol-polyphosphate-1-phosphatase and 3'-phosphoadenosine-5'-phosphate phosphatase activities: a novel target of lithium therapy.
Related PDB1jp4
Related UniProtKBQ9Z1N4

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).

createdupdated
2004-02-192009-02-26


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Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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