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) |
---|---|
3.30.540.10 : Fructose-1,6-Bisphosphatase; Chain A, domain 1 | D00148 D00153 T00053 |
3.40.190.80 : D-Maltodextrin-Binding Protein; domain 2 | 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 18420 |
17985 17985 |
17980 17980 |
17816 17816 |
18228 18228 |
15377 15377 |
26078 26078 |
16027 16027 |
17709 17709 |
18384 18384 |
28858 28858 |
||||||
PubChem |
888 888 |
159296 159296 |
10214 10214 |
439455 439455 |
22247451 962 22247451 962 |
1004 22486802 1004 22486802 |
6083 6083 |
10238 10238 |
440211 440211 |
||||||||
1jp4A01 | Bound:3x_MG | Unbound | Unbound | Unbound | Unbound | Bound:PO4 | Unbound | Unbound | Unbound | Unbound | |||||||
1jp4A02 | 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 | 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 | 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, |
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, |
Created | Updated |
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2004-02-19 | 2009-02-26 |