DB code: D00153
| 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. | 3.1.3.25 | |
| CSA | 1ima | |
| M-CSA | 1ima | |
| MACiE | ||
| CATH domain | Related DB codes (homologues) |
|---|---|
| 3.30.540.10 : Fructose-1,6-Bisphosphatase; Chain A, domain 1 | D00148 D00491 T00053 |
| 3.40.190.80 : D-Maltodextrin-Binding Protein; domain 2 | D00148 D00491 T00053 |
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq | Pfam |
|---|---|---|---|---|
| Q57573 |
Inositol-1-monophosphatase
|
IMPase
Inositol-1-phosphatase I-1-Pase EC 3.1.3.25 |
NP_247073.1
(Protein)
NC_000909.1 (DNA/RNA sequence) |
PF00459
(Inositol_P)
[Graphical View] |
| O30298 |
Inositol-1-monophosphatase
|
IMPase
Inositol-1-phosphatase I-1-Pase EC 3.1.3.25 |
NP_071195.1
(Protein)
NC_000917.1 (DNA/RNA sequence) |
PF00459
(Inositol_P)
[Graphical View] |
| P20456 |
Inositol monophosphatase
|
EC
3.1.3.25
Inositol-1(or 4)-monophosphatase IMPase IMP Lithium-sensitive myo-inositol monophosphatase A1 |
NP_776786.1
(Protein)
NM_174361.4 (DNA/RNA sequence) |
PF00459
(Inositol_P)
[Graphical View] |
| P29218 |
Inositol monophosphatase
|
EC
3.1.3.25
Inositol-1(or 4)-monophosphatase IMPase IMP Lithium-sensitive myo-inositol monophosphatase A1 |
NP_001138350.1
(Protein)
NM_001144878.1 (DNA/RNA sequence) NP_001138351.1 (Protein) NM_001144879.1 (DNA/RNA sequence) NP_005527.1 (Protein) NM_005536.3 (DNA/RNA sequence) |
PF00459
(Inositol_P)
[Graphical View] |
| KEGG enzyme name |
|---|
|
inositol-phosphate phosphatase
myo-inositol-1(or 4)-monophosphatase inositol 1-phosphatase L-myo-inositol-1-phosphate phosphatase myo-inositol 1-phosphatase inositol phosphatase inositol monophosphate phosphatase inositol-1(or 4)-monophosphatase myo-inositol-1(or 4)-phosphate phosphohydrolase myo-inositol monophosphatase myo-inositol-1-phosphatase |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| Q57573 | SUHB_METJA | Myo-inositol phosphate + H(2)O = myo-inositol + phosphate. | Homodimer. | Magnesium. | |
| O30298 | SUHB_ARCFU | Myo-inositol phosphate + H(2)O = myo-inositol + phosphate. | Magnesium (By similarity). | ||
| P20456 | IMPA1_BOVIN | Myo-inositol phosphate + H(2)O = myo-inositol + phosphate. | Homodimer. | Cytoplasm. | Magnesium. |
| P29218 | IMPA1_HUMAN | Myo-inositol phosphate + H(2)O = myo-inositol + phosphate. | Homodimer. | Cytoplasm. | Magnesium. |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|---|---|
| MAP00521 | Streptomycin biosynthesis | |
| MAP00562 | Inositol phosphate metabolism | |
| MAP04070 | Phosphatidylinositol signaling system |
| Compound table | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Cofactors | Substrates | Products | Intermediates | |||||||||
| KEGG-id | C00305 | C01177 | C03546 | C00001 | C00137 | C00009 | ||||||
| E.C. | ||||||||||||
| Compound | Magnesium | 1L-myo-Inositol 1-phosphate | myo-Inositol 4-phosphate | H2O | myo-Inositol | Orthophosphate | ||||||
| Type | divalent metal (Ca2+, Mg2+) | carbohydrate,phosphate group/phosphate ion | carbohydrate,phosphate group/phosphate ion | H2O | carbohydrate | phosphate group/phosphate ion | ||||||
| ChEBI |
18420 18420 |
18297 18297 |
18384 18384 |
15377 15377 |
17268 17268 |
26078 26078 |
||||||
| PubChem |
888 888 |
22247451 962 22247451 962 |
1004 22486802 1004 22486802 |
|||||||||
| 1dk4A01 |
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Analogue:3x_ZN | Unbound | Unbound | Unbound | Bound:PO4 | ||
| 1dk4B01 |
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Analogue:3x_ZN | Unbound | Unbound | Unbound | Bound:PO4 | ||
| 1g0hA01 |
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Analogue:2x_CA | Bound:IPD | Unbound | Unbound | Unbound | ||
| 1g0hB01 |
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Analogue:2x_CA | Bound:IPD | Unbound | Unbound | Unbound | ||
| 1g0iA01 |
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Analogue:3x_MN | Unbound | Unbound | Unbound | Bound:PO4 | ||
| 1g0iB01 |
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Analogue:3x_MN | Unbound | Unbound | Unbound | Bound:PO4 | ||
| 1lbvA01 |
|
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Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1lbvB01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1lbwA01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1lbwB01 |
|
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Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1lbxA01 |
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Analogue:2x_CA | Bound:IPD | Unbound | Unbound | Unbound | ||
| 1lbxB01 |
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Analogue:2x_CA | Bound:IPD | Unbound | Unbound | Unbound | ||
| 1lbyA01 |
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Analogue:3x_MN | Unbound | Unbound | Unbound | Bound:PO4 | ||
| 1lbyB01 |
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Analogue:3x_MN | Unbound | Unbound | Unbound | Bound:PO4 | ||
| 1lbzA01 |
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Analogue:3x_CA | Analogue:FBP | Unbound | Unbound | Unbound | ||
| 1lbzB01 |
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Analogue:3x_CA | Analogue:FBP | Unbound | Unbound | Unbound | ||
| 2bjiA01 |
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Bound:3x_MG | Unbound | Unbound | Unbound | Unbound | ||
| 2bjiB01 |
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Bound:3x_MG | Unbound | Unbound | Unbound | Unbound | ||
| 1awbA01 |
|
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Analogue:3x_CA | Bound:IPD | Unbound | Unbound | Unbound | ||
| 1awbB01 |
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Analogue:3x_CA | Bound:IPD | Unbound | Unbound | Unbound | ||
| 1imaA01 |
|
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Analogue:_GD | Bound:IPD | Unbound | Unbound | Unbound | ||
| 1imaB01 |
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Analogue:_GD | Bound:IPD | Unbound | Unbound | Unbound | ||
| 1imbA01 |
|
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Analogue:_GD | Bound:LIP | Unbound | Unbound | Unbound | ||
| 1imbB01 |
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Analogue:_GD | Bound:LIP | Unbound | Unbound | Unbound | ||
| 1imcA01 |
|
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Analogue:3x_MN | Unbound | Unbound | Unbound | Unbound | ||
| 1imcB01 |
|
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Analogue:3x_MN | Unbound | Unbound | Unbound | Unbound | ||
| 1imdA01 |
|
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Analogue:2x_MN | Unbound | Unbound | Unbound | Bound:PO4 | ||
| 1imdB01 |
|
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Analogue:2x_MN | Unbound | Unbound | Unbound | Bound:PO4 | ||
| 1imeA01 |
|
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Analogue:_CA | Unbound | Unbound | Unbound | Unbound | ||
| 1imeB01 |
|
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Analogue:_CA | Unbound | Unbound | Unbound | Unbound | ||
| 1imfA01 |
|
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Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 2hhmA01 |
|
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Analogue:_GD | Unbound | Unbound | Unbound | Analogue:SO4 | ||
| 2hhmB01 |
|
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Analogue:_GD | Unbound | Unbound | Unbound | Analogue:SO4 | ||
| 1dk4A02 |
|
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Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1dk4B02 |
|
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Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1g0hA02 |
|
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Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1g0hB02 |
|
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Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1g0iA02 |
|
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Unbound | Unbound | Unbound | Bound:INS | Unbound | ||
| 1g0iB02 |
|
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Unbound | Unbound | Unbound | Bound:INS | Unbound | ||
| 1lbvA02 |
|
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Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1lbvB02 |
|
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Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1lbwA02 |
|
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Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1lbwB02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1lbxA02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1lbxB02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1lbyA02 |
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Unbound | Unbound | Unbound | Analogue:F6P | Unbound | ||
| 1lbyB02 |
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Unbound | Unbound | Unbound | Analogue:F6P | Unbound | ||
| 1lbzA02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1lbzB02 |
|
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Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 2bjiA02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 2bjiB02 |
|
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Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1awbA02 |
|
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Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1awbB02 |
|
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Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1imaA02 |
|
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Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1imaB02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1imbA02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1imbB02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1imcA02 |
|
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Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1imcB02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1imdA02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1imdB02 |
|
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Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1imeA02 |
|
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Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1imeB02 |
|
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Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1imfA02 |
|
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Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 2hhmA02 |
|
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Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 2hhmB02 |
|
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Unbound | Unbound | Unbound | Unbound | Unbound | ||
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| Swiss-prot;P29218, O30298, Q57573 & Literature [8], [20], [23], [27], [28] | ||
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1dk4A01 |
|
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|
ASP 44;SER 86 | GLU 65(Magnesium-1 & -3);ASP 81(Magnesium-1 & -2);ASP 84(Magnesium-2);ILE 83(Magnesium-1);ASP 38; (Magnesium-3) | GLY 85;SER 86 | ||
| 1dk4B01 |
|
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|
ASP 344;SER 386 | GLU 365(Magnesium-1 & -3);ASP 381(Magnesium-1 & -2);ASP 384(Magnesium-2);ILE 383(Magnesium-1);ASP 338; (Magnesium-3) | GLY 385;SER 386 | ||
| 1g0hA01 |
|
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|
ASP 44;SER 86 | GLU 65(Magnesium-1 & -3);ASP 81(Magnesium-1 & -2);ASP 84(Magnesium-2);ILE 83(Magnesium-1);ASP 38; (Magnesium-3) | GLY 85;SER 86 | ||
| 1g0hB01 |
|
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ASP 344;SER 386 | GLU 365(Magnesium-1 & -3);ASP 381(Magnesium-1 & -2);ASP 384(Magnesium-2);ILE 383(Magnesium-1);ASP 338; (Magnesium-3) | GLY 385;SER 386 | ||
| 1g0iA01 |
|
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ASP 44;SER 86 | GLU 65(Magnesium-1 & -3);ASP 81(Magnesium-1 & -2);ASP 84(Magnesium-2);ILE 83(Magnesium-1);ASP 38; (Magnesium-3) | GLY 85;SER 86 | ||
| 1g0iB01 |
|
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ASP 344;SER 386 | GLU 365(Magnesium-1 & -3);ASP 381(Magnesium-1 & -2);ASP 384(Magnesium-2);ILE 383(Magnesium-1);ASP 338; (Magnesium-3) | GLY 385;SER 386 | ||
| 1lbvA01 |
|
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ASP 46;THR 87 | GLU 67(Magnesium-1 & -3);ASP 82(Magnesium-1 & -2);ASP 85(Magnesium-2);LEU 84(Magnesium-1);ASP 38;THR 40(Magnesium-3) | GLY 86;THR 87 | ||
| 1lbvB01 |
|
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ASP 346;THR 387 | GLU 367(Magnesium-1 & -3);ASP 382(Magnesium-1 & -2);ASP 385(Magnesium-2);LEU 384(Magnesium-1);ASP 338;THR 340(Magnesium-3) | GLY 386;THR 387 | ||
| 1lbwA01 |
|
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ASP 46;THR 87 | GLU 67(Magnesium-1 & -3);ASP 82(Magnesium-1 & -2);ASP 85(Magnesium-2);LEU 84(Magnesium-1);ASP 38;THR 40(Magnesium-3) | GLY 86;THR 87 | ||
| 1lbwB01 |
|
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ASP 346;THR 387 | GLU 367(Magnesium-1 & -3);ASP 382(Magnesium-1 & -2);ASP 385(Magnesium-2);LEU 384(Magnesium-1);ASP 338;THR 340(Magnesium-3) | GLY 386;THR 387 | ||
| 1lbxA01 |
|
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ASP 46;THR 87 | GLU 67(Magnesium-1 & -3);ASP 82(Magnesium-1 & -2);ASP 85(Magnesium-2);LEU 84(Magnesium-1);ASP 38;THR 40(Magnesium-3) | GLY 86;THR 87 | ||
| 1lbxB01 |
|
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ASP 346;THR 387 | GLU 367(Magnesium-1 & -3);ASP 382(Magnesium-1 & -2);ASP 385(Magnesium-2);LEU 384(Magnesium-1);ASP 338;THR 340(Magnesium-3) | GLY 386;THR 387 | ||
| 1lbyA01 |
|
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ASP 46;THR 87 | GLU 67(Magnesium-1 & -3);ASP 82(Magnesium-1 & -2);ASP 85(Magnesium-2);LEU 84(Magnesium-1);ASP 38;THR 40(Magnesium-3) | GLY 86;THR 87 | ||
| 1lbyB01 |
|
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ASP 346;THR 387 | GLU 367(Magnesium-1 & -3);ASP 382(Magnesium-1 & -2);ASP 385(Magnesium-2);LEU 384(Magnesium-1);ASP 338;THR 340(Magnesium-3) | GLY 386;THR 387 | ||
| 1lbzA01 |
|
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ASP 46;THR 87 | GLU 67(Magnesium-1 & -3);ASP 82(Magnesium-1 & -2);ASP 85(Magnesium-2);LEU 84(Magnesium-1);ASP 38;THR 40(Magnesium-3) | GLY 86;THR 87 | ||
| 1lbzB01 |
|
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ASP 346;THR 387 | GLU 367(Magnesium-1 & -3);ASP 382(Magnesium-1 & -2);ASP 385(Magnesium-2);LEU 384(Magnesium-1);ASP 338;THR 340(Magnesium-3) | GLY 386;THR 387 | ||
| 2bjiA01 |
|
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ASP 1047;THR 1095 | GLU 1070(Magnesium-1 & -3);ASP 1090(Magnesium-1 & -2);ASP 1093(Magnesium-2);ILE 1092(Magnesium-1);ASP 1041; (Magnesium-3) | GLY 1094;THR 1095 | ||
| 2bjiB01 |
|
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ASP 2047;THR 2095 | GLU 2070(Magnesium-1 & -3);ASP 2090(Magnesium-1 & -2);ASP 2093(Magnesium-2);ILE 2092(Magnesium-1);ASP 2041; (Magnesium-3) | GLY 2094;THR 2095 | ||
| 1awbA01 |
|
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ASP 47;THR 95 | GLU 70(Magnesium-1 & -3);ASP 90(Magnesium-1 & -2);ASP 93(Magnesium-2);ILE 92(Magnesium-1);ASP 41; (Magnesium-3) | GLY 94;THR 95 | ||
| 1awbB01 |
|
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ASP 47;THR 95 | GLU 70(Magnesium-1 & -3);ASP 90(Magnesium-1 & -2);ASP 93(Magnesium-2);ILE 92(Magnesium-1);ASP 41; (Magnesium-3) | GLY 94;THR 95 | ||
| 1imaA01 |
|
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ASP 47;THR 95 | GLU 70(Magnesium-1 & -3);ASP 90(Magnesium-1 & -2);ASP 93(Magnesium-2);ILE 92(Magnesium-1);ASP 41; (Magnesium-3) | GLY 94;THR 95 | ||
| 1imaB01 |
|
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ASP 47;THR 95 | GLU 70(Magnesium-1 & -3);ASP 90(Magnesium-1 & -2);ASP 93(Magnesium-2);ILE 92(Magnesium-1);ASP 41; (Magnesium-3) | GLY 94;THR 95 | ||
| 1imbA01 |
|
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ASP 47;THR 95 | GLU 70(Magnesium-1 & -3);ASP 90(Magnesium-1 & -2);ASP 93(Magnesium-2);ILE 92(Magnesium-1);ASP 41; (Magnesium-3) | GLY 94;THR 95 | ||
| 1imbB01 |
|
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ASP 47;THR 95 | GLU 70(Magnesium-1 & -3);ASP 90(Magnesium-1 & -2);ASP 93(Magnesium-2);ILE 92(Magnesium-1);ASP 41; (Magnesium-3) | GLY 94;THR 95 | ||
| 1imcA01 |
|
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ASP 47;THR 95 | GLU 70(Magnesium-1 & -3);ASP 90(Magnesium-1 & -2);ASP 93(Magnesium-2);ILE 92(Magnesium-1);ASP 41; (Magnesium-3) | GLY 94;THR 95 | ||
| 1imcB01 |
|
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ASP 47;THR 95 | GLU 70(Magnesium-1 & -3);ASP 90(Magnesium-1 & -2);ASP 93(Magnesium-2);ILE 92(Magnesium-1);ASP 41; (Magnesium-3) | GLY 94;THR 95 | ||
| 1imdA01 |
|
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ASP 47;THR 95 | GLU 70(Magnesium-1 & -3);ASP 90(Magnesium-1 & -2);ASP 93(Magnesium-2);ILE 92(Magnesium-1);ASP 41; (Magnesium-3) | GLY 94;THR 95 | ||
| 1imdB01 |
|
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ASP 47;THR 95 | GLU 70(Magnesium-1 & -3);ASP 90(Magnesium-1 & -2);ASP 93(Magnesium-2);ILE 92(Magnesium-1);ASP 41; (Magnesium-3) | GLY 94;THR 95 | ||
| 1imeA01 |
|
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ASP 47;THR 95 | GLU 70(Magnesium-1 & -3);ASP 90(Magnesium-1 & -2);ASP 93(Magnesium-2);ILE 92(Magnesium-1);ASP 41; (Magnesium-3) | GLY 94;THR 95 | ||
| 1imeB01 |
|
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|
ASP 47;THR 95 | GLU 70(Magnesium-1 & -3);ASP 90(Magnesium-1 & -2);ASP 93(Magnesium-2);ILE 92(Magnesium-1);ASP 41; (Magnesium-3) | GLY 94;THR 95 | ||
| 1imfA01 |
|
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ASP 47;THR 95 | GLU 70(Magnesium-1 & -3);ASP 90(Magnesium-1 & -2);ASP 93(Magnesium-2);ILE 92(Magnesium-1);ASP 41; (Magnesium-3) | GLY 94;THR 95 | ||
| 2hhmA01 |
|
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ASP 47;THR 95 | GLU 70(Magnesium-1 & -3);ASP 90(Magnesium-1 & -2);ASP 93(Magnesium-2);ILE 92(Magnesium-1);ASP 41; (Magnesium-3) | GLY 94;THR 95 | ||
| 2hhmB01 |
|
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ASP 47;THR 95 | GLU 70(Magnesium-1 & -3);ASP 90(Magnesium-1 & -2);ASP 93(Magnesium-2);ILE 92(Magnesium-1);ASP 41; (Magnesium-3) | GLY 94;THR 95 | ||
| 1dk4A02 |
|
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ASP 201(Magnesium-2) | ||||
| 1dk4B02 |
|
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ASP 501(Magnesium-2) | ||||
| 1g0hA02 |
|
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ASP 201(Magnesium-2) | ||||
| 1g0hB02 |
|
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ASP 501(Magnesium-2) | ||||
| 1g0iA02 |
|
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ASP 201(Magnesium-2) | ||||
| 1g0iB02 |
|
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ASP 501(Magnesium-2) | ||||
| 1lbvA02 |
|
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ASP 200(Magnesium-2) | ||||
| 1lbvB02 |
|
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ASP 500(Magnesium-2) | ||||
| 1lbwA02 |
|
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ASP 200(Magnesium-2) | ||||
| 1lbwB02 |
|
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ASP 500(Magnesium-2) | ||||
| 1lbxA02 |
|
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ASP 200(Magnesium-2) | ||||
| 1lbxB02 |
|
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ASP 500(Magnesium-2) | ||||
| 1lbyA02 |
|
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ASP 200(Magnesium-2) | ||||
| 1lbyB02 |
|
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ASP 500(Magnesium-2) | ||||
| 1lbzA02 |
|
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ASP 200(Magnesium-2) | ||||
| 1lbzB02 |
|
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ASP 500(Magnesium-2) | ||||
| 2bjiA02 |
|
|
|
|
|
ASP 1220(Magnesium-2) | ||||
| 2bjiB02 |
|
|
|
|
|
ASP 2220(Magnesium-2) | ||||
| 1awbA02 |
|
|
|
|
|
ASP 220(Magnesium-2) | ||||
| 1awbB02 |
|
|
|
|
|
ASP 220(Magnesium-2) | ||||
| 1imaA02 |
|
|
|
|
|
ASP 220(Magnesium-2) | ||||
| 1imaB02 |
|
|
|
|
|
ASP 220(Magnesium-2) | ||||
| 1imbA02 |
|
|
|
|
|
ASP 220(Magnesium-2) | ||||
| 1imbB02 |
|
|
|
|
|
ASP 220(Magnesium-2) | ||||
| 1imcA02 |
|
|
|
|
|
ASP 220(Magnesium-2) | ||||
| 1imcB02 |
|
|
|
|
|
ASP 220(Magnesium-2) | ||||
| 1imdA02 |
|
|
|
|
|
ASP 220(Magnesium-2) | ||||
| 1imdB02 |
|
|
|
|
|
ASP 220(Magnesium-2) | ||||
| 1imeA02 |
|
|
|
|
|
ASP 220(Magnesium-2) | ||||
| 1imeB02 |
|
|
|
|
|
ASP 220(Magnesium-2) | ||||
| 1imfA02 |
|
|
|
|
|
ASP 220(Magnesium-2) | ||||
| 2hhmA02 |
|
|
|
|
|
ASP 220(Magnesium-2) | ||||
| 2hhmB02 |
|
|
|
|
|
ASP 220(Magnesium-2) | ||||
| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
|
[7]
|
p.9474-9475 | |
|
[8]
|
Fig.5, p.9466 | |
|
[10]
|
Fig.4, p.5-6 | |
|
[16]
|
||
|
[20]
|
Fig.2, Fig.5, p.268-269 | |
|
[27]
|
Fig.5, p.681-682 | |
|
[28]
|
Fig.5, p.553 | |
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 1665957 |
| Journal | Anal Biochem |
| Year | 1991 |
| Volume | 198 |
| Pages | 375-8 |
| Authors | Churchich JE, Kwok F |
| Title | Assay of 1L-myo-inositol-1-phosphatase using a fluorometric method. |
| Related PDB | |
| Related UniProtKB | |
| [2] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 1333077 |
| Journal | Pharm Res |
| Year | 1992 |
| Volume | 9 |
| Pages | 1370-3 |
| Authors | Harrold MW, Sriburi A, Caimano P, Qi H, Seybert D, Lin FT |
| Title |
Inhibition of myo-inositol 1-phosphatase by cis-1,2,3-cyclohexanetriol 1-phosphate, |
| Related PDB | |
| Related UniProtKB | |
| [3] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) |
| Medline ID | 93066173 |
| PubMed ID | 1332026 |
| Journal | Proc Natl Acad Sci U S A |
| Year | 1992 |
| Volume | 89 |
| Pages | 10031-5 |
| Authors | Bone R, Springer JP, Atack JR |
| Title |
Structure of inositol monophosphatase, |
| Related PDB | 2hhm |
| Related UniProtKB | P29218 |
| [4] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8382485 |
| Journal | Biochem Biophys Res Commun |
| Year | 1993 |
| Volume | 190 |
| Pages | 1080-3 |
| Authors | Zhang Y, Liang JY, Lipscomb WN |
| Title | Structural similarities between fructose-1,6-bisphosphatase and inositol monophosphatase. |
| Related PDB | |
| Related UniProtKB | |
| [5] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8223565 |
| Journal | Eur J Biochem |
| Year | 1993 |
| Volume | 217 |
| Pages | 281-7 |
| Authors | Pollack SJ, Knowles MR, Atack JR, Broughton HB, Ragan CI, Osborne S, McAllister G |
| Title | Probing the role of metal ions in the mechanism of inositol monophosphatase by site-directed mutagenesis. |
| Related PDB | |
| Related UniProtKB | |
| [6] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8019438 |
| Journal | Biochem Mol Biol Int |
| Year | 1994 |
| Volume | 32 |
| Pages | 325-30 |
| Authors | Kwok F, Lo SC, Churchich JE |
| Title | Brain myo-inositol monophosphatase: activity of the single subunit in a dimeric enzyme. |
| Related PDB | |
| Related UniProtKB | |
| [7] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH SUBSTRATE. |
| Medline ID | |
| PubMed ID | 8068621 |
| Journal | Biochemistry |
| Year | 1994 |
| Volume | 33 |
| Pages | 9468-76 |
| Authors | Bone R, Frank L, Springer JP, Atack JR |
| Title | Structural studies of metal binding by inositol monophosphatase: evidence for two-metal ion catalysis. |
| Related PDB | 1imc 1imd 1ime 1imf |
| Related UniProtKB | |
| [8] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 8068620 |
| Journal | Biochemistry |
| Year | 1994 |
| Volume | 33 |
| Pages | 9460-7 |
| Authors | Bone R, Frank L, Springer JP, Pollack SJ, Osborne SA, Atack JR, Knowles MR, McAllister G, Ragan CI, Broughton HB, et al |
| Title | Structural analysis of inositol monophosphatase complexes with substrates. |
| Related PDB | 1ima 1imb |
| Related UniProtKB | |
| [9] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8276805 |
| Journal | J Biol Chem |
| Year | 1994 |
| Volume | 269 |
| Pages | 266-71 |
| Authors | Kwon OS, Churchich JE |
| Title | Interaction of 70-kDA heat shock cognate protein with peptides and myo-inositol monophosphatase. |
| Related PDB | |
| Related UniProtKB | |
| [10] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 7890024 |
| Journal | FEBS Lett |
| Year | 1995 |
| Volume | 361 |
| Pages | 1-7 |
| Authors | Atack JR, Broughton HB, Pollack SJ |
| Title | Structure and mechanism of inositol monophosphatase. |
| Related PDB | |
| Related UniProtKB | |
| [11] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 7568043 |
| Journal | Proc Natl Acad Sci U S A |
| Year | 1995 |
| Volume | 92 |
| Pages | 8916-20 |
| Authors | Villeret V, Huang S, Fromm HJ, Lipscomb WN |
| Title |
Crystallographic evidence for the action of potassium, |
| Related PDB | |
| Related UniProtKB | |
| [12] | |
| 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 | |
| [13] | |
| Resource | |
| Comments |
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT GLN-36, |
| Medline ID | |
| PubMed ID | 8718889 |
| Journal | Biochemistry |
| Year | 1996 |
| Volume | 35 |
| Pages | 10957-66 |
| Authors | Ganzhorn AJ, Lepage P, Pelton PD, Strasser F, Vincendon P, Rondeau JM |
| Title | The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase. |
| Related PDB | |
| Related UniProtKB | P29218 |
| [14] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8925839 |
| Journal | Eur J Biochem |
| Year | 1996 |
| Volume | 240 |
| Pages | 288-91 |
| Authors | Saudek V, Vincendon P, Do QT, Atkinson RA, Sklenar V, Pelton PD, Piriou F, Ganzhorn AJ |
| Title | 7Li nuclear-magnetic-resonance study of lithium binding to myo-inositolmonophosphatase. |
| Related PDB | |
| Related UniProtKB | |
| [15] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9435892 |
| Journal | J Med Chem |
| Year | 1997 |
| Volume | 40 |
| Pages | 4208-21 |
| Authors | Piettre SR, Andre C, Chanal MC, Ducep JB, Lesur B, Piriou F, Raboisson P, Rondeau JM, Schelcher C, Zimmermann P, Ganzhorn AJ |
| Title | Monoaryl- and bisaryldihydroxytropolones as potent inhibitors of inositol monophosphatase. |
| Related PDB | |
| Related UniProtKB | |
| [16] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) |
| Medline ID | |
| PubMed ID | |
| Journal | PRotein Eng |
| Year | 1997 |
| Volume | 10 |
| Pages | 61 |
| Authors | Ganzhorn AJ, Rondeau JM |
| Title | Structure of an enzyme-substrate complex and the catalytic mechanism of human brain myo-inositol monophosphatase. |
| Related PDB | 1awb |
| Related UniProtKB | P29218 |
| [17] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9647837 |
| Journal | Appl Environ Microbiol |
| Year | 1998 |
| Volume | 64 |
| Pages | 2609-15 |
| Authors | Chen L, Roberts MF |
| Title | Cloning and expression of the inositol monophosphatase gene from Methanococcus jannaschii and characterization of the enzyme. |
| Related PDB | |
| Related UniProtKB | |
| [18] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9853417 |
| Journal | Biol Pharm Bull |
| Year | 1998 |
| Volume | 21 |
| Pages | 1218-21 |
| Authors | Tsuda J, Kimura T, Tanino H, Shimohama S, Fujimoto S |
| Title | Characterization of high- and low-molecular weight zinc-dependent acid phosphatases in bovine liver. |
| Related PDB | |
| Related UniProtKB | |
| [19] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9988525 |
| Journal | J Protein Chem |
| Year | 1998 |
| Volume | 17 |
| Pages | 789-97 |
| Authors | Lau CK, Lo SC, Li W, Churchich DR, Kwok F, Churchich JE |
| Title | Partially folded conformations of inositol monophosphatase endowed with catalytic activity. |
| Related PDB | |
| Related UniProtKB | |
| [20] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11828418 |
| Journal | Chembiochem |
| Year | 2000 |
| Volume | 1 |
| Pages | 262-71 |
| Authors | Miller DJ, Beaton MW, Wilkie J, Gani D |
| Title | The 6-OH group of D-inositol 1-phosphate serves as an H-bond donor in the catalytic hydrolysis of the phosphate ester by inositol monophosphatase. |
| Related PDB | |
| Related UniProtKB | |
| [21] | |
| Resource | |
| Comments | |
| Medline ID | |
| 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 | |
| [22] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND METAL IONS. |
| Medline ID | |
| PubMed ID | 11062561 |
| Journal | Nat Struct Biol |
| Year | 2000 |
| Volume | 7 |
| Pages | 1046-50 |
| Authors | Stec B, Yang H, Johnson KA, Chen L, Roberts MF |
| Title | MJ0109 is an enzyme that is both an inositol monophosphatase and the 'missing' archaeal fructose-1,6-bisphosphatase. |
| Related PDB | 1dk4 |
| Related UniProtKB | Q57573 |
| [23] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). |
| Medline ID | |
| PubMed ID | 11170378 |
| Journal | Biochemistry |
| Year | 2001 |
| Volume | 40 |
| Pages | 618-30 |
| Authors | Johnson KA, Chen L, Yang H, Roberts MF, Stec B |
| Title | Crystal structure and catalytic mechanism of the MJ0109 gene product: a bifunctional enzyme with inositol monophosphatase and fructose 1,6-bisphosphatase activities. |
| Related PDB | 1g0h 1g0i |
| Related UniProtKB | Q57573 |
| [24] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11914086 |
| Journal | Biochemistry |
| Year | 2002 |
| Volume | 41 |
| Pages | 4392-8 |
| Authors | Nigou J, Dover LG, Besra GS |
| Title |
Purification and biochemical characterization of Mycobacterium tuberculosis SuhB, |
| Related PDB | |
| Related UniProtKB | |
| [25] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND METAL IONS. |
| Medline ID | |
| PubMed ID | 11940584 |
| Journal | J Biol Chem |
| Year | 2002 |
| Volume | 277 |
| Pages | 22863-74 |
| Authors | Stieglitz KA, Johnson KA, Yang H, Roberts MF, Seaton BA, Head JF, Stec B |
| Title |
Crystal structure of a dual activity IMPase/FBPase (AF2372) from Archaeoglobus fulgidus. |
| Related PDB | 1lbv 1lbw 1lbx 1lby 1lbz |
| Related UniProtKB | O30298 |
| [26] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11882005 |
| Journal | J Med Chem |
| Year | 2002 |
| Volume | 45 |
| Pages | 1363-73 |
| Authors | Fauroux CM, Lee M, Cullis PM, Douglas KT, Gore MG, Freeman S |
| Title | Stereochemistry at phosphorus of the reaction catalyzed by myo-inositol monophosphatase. |
| Related PDB | |
| Related UniProtKB | |
| [27] | |
| 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 | |
| [28] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 15858264 |
| Journal | Acta Crystallogr D Biol Crystallogr |
| Year | 2005 |
| Volume | 61 |
| Pages | 545-55 |
| Authors | Gill R, Mohammed F, Badyal R, Coates L, Erskine P, Thompson D, Cooper J, Gore M, Wood S |
| Title |
High-resolution structure of myo-inositol monophosphatase, |
| Related PDB | 2bji |
| Related UniProtKB | |
| [29] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 15715947 |
| Journal | J Biochem Mol Biol |
| Year | 2005 |
| Volume | 38 |
| Pages | 58-64 |
| Authors | Kim DW, Hong JW, Eum WS, Choi HS, Choi SH, Kim SY, Lee BR, An JJ, Lee SH, Lee SR, Kwon OS, Kwon HY, Cho SW, Lee KS, Park J, Choi SY |
| Title | Inactivation of brain myo-inositol monophosphate phosphatase by pyridoxal-5'-phosphate. |
| Related PDB | |
| Related UniProtKB | |
| Comments |
|---|
|
This enzyme belongs to the inositol monophosphatase family. According to the literature [7], (1) Asp47 (of 1awb) acts as the general base to activate a water through Thr95 (probably acting as a proton shuttle). (2) The activated water makes a nucleophilic attack on the phosphate group, (3) The target bond, (4) Another water, |
| Created | Updated |
|---|---|
| 2005-08-05 | 2009-02-26 |