CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.950 | Maf protein |
|
3.90.950.10 |
Domain Context
CATH Clusters
| Superfamily | 3.90.950.10 |
| Functional Family | Probable bifunctional dTTP/UTP pyrophosphatase/methyltransferase protein |
Enzyme Information
| 2.1.1.- |
Methyltransferases.
based on mapping to UniProt O95671
|
| 3.6.1.9 |
Nucleotide diphosphatase.
based on mapping to UniProt O95671
A nucleoside triphosphate + H(2)O = a nucleotide + diphosphate.
-!- The enzyme preferentially hydrolyzes ATP, but can also hydrolyze other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates. -!- In vitro the enzyme also acts as a nucleotidohydrolase on ADP, NAD(+), NADP(+), FAD, and CoA. -!- Formerly EC 3.6.1.19.
|
UniProtKB Entries (1)
| O95671 |
ASML_HUMAN
Homo sapiens
Probable bifunctional dTTP/UTP pyrophosphatase/methyltransferase protein
|
PDB Structure
| PDB | 2P5X |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Biochemical and structural studies of conserved maf proteins revealed nucleotide pyrophosphatases with a preference for modified nucleotides.
Chem.Biol.
|