CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.10 | Roll |
|
3.10.400 | Sulfate adenylyltransferase |
|
3.10.400.10 | Sulfate adenylyltransferase |
Domain Context
CATH Clusters
| Superfamily | Sulfate adenylyltransferase |
| Functional Family |
Enzyme Information
| 2.7.7.4 |
Sulfate adenylyltransferase.
based on mapping to UniProt O66036
ATP + sulfate = diphosphate + adenylyl sulfate.
-!- The human phosphoadenosine-phosphosulfate synthase (PAPS) system is a bifunctional enzyme: ATP sulfurylase, which catalyzes the formation of adenosine 5'-phosphosulfate (APS) from ATP and inorganic sulfate and the second step is catalyzed by the APS kinase portion of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) synthase, which involves the formation of PAPS from enzyme bound APS and ATP. -!- This is in contrast to what is found in bacteria, yeasts, fungi and plants, where the formation of PAPS is carried out by two individual polypeptides, EC 2.7.7.4 and EC 2.7.1.25.
|
UniProtKB Entries (1)
| O66036 |
SAT_ALLVD
Allochromatium vinosum DSM 180
Sulfate adenylyltransferase
|
PDB Structure
| PDB | 4DNX |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
The crystal structure of the ATP sulfurylase from Allochromatium vinosum in the open state
To be Published
|