CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.540 | Fructose-1,6-Bisphosphatase; Chain A, domain 1 |
|
3.30.540.10 | Fructose-1,6-Bisphosphatase, subunit A, domain 1 |
Domain Context
CATH Clusters
| Superfamily | Fructose-1,6-Bisphosphatase, subunit A, domain 1 |
| Functional Family | Inositol-1-monophosphatase |
Enzyme Information
| 3.1.3.94 |
D-galactose 1-phosphate phosphatase.
based on mapping to UniProt P29218
Alpha-D-galactose 1-phosphate + H(2)O = D-galactose + phosphate.
-!- The human enzyme also has the activity of EC 3.1.3.25. -!- The enzyme has very low activity with L-galactose 1-phosphate (cf. EC 3.1.3.93).
|
| 3.1.3.25 |
Inositol-phosphate phosphatase.
based on mapping to UniProt P29218
Myo-inositol phosphate + H(2)O = myo-inositol + phosphate.
-!- Acts on five of the six isomers of myo-inositol phosphate, all except myo-inositol 2-phosphate, but does not act on myo-inositol bearing more than one phosphate group. -!- It also acts on adenosine 2'-phosphate (but not the 3'- or 5'-phosphates), sn-glycerol 3-phosphate and glycerol 2-phosphate, but does not act on inositol bisphosphates or more phosphorylated inositols.
|
UniProtKB Entries (1)
| P29218 |
IMPA1_HUMAN
Homo sapiens
Inositol monophosphatase 1
|
PDB Structure
| PDB | 1IMD |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural studies of metal binding by inositol monophosphatase: evidence for two-metal ion catalysis.
Biochemistry
|
