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 | Sulfate adenylyltransferase |
Enzyme Information
| 2.7.7.4 |
Sulfate adenylyltransferase.
based on mapping to UniProt P08536
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)
| P08536 |
MET3_YEAST
Saccharomyces cerevisiae S288C
Sulfate adenylyltransferase
|
PDB Structure
| PDB | 1R6X |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structural and functional analysis of a truncated form of Saccharomyces cerevisiae ATP sulfurylase: C-terminal domain essential for oligomer formation but not for activity
Protein Eng.
|
