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 | Probable bifunctional SAT/APS kinase |
Enzyme Information
| 2.7.1.25 |
Adenylyl-sulfate kinase.
based on mapping to UniProt O67174
ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl 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.
|
| 2.7.7.4 |
Sulfate adenylyltransferase.
based on mapping to UniProt O67174
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)
| O67174 |
SATC_AQUAE
Aquifex aeolicus VF5
Probable bifunctional SAT/APS kinase
|
PDB Structure
| PDB | 2GKS |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structure of the bifunctional ATP sulfurylase-APS kinase from the chemolithotrophic thermophile Aquifex aeolicus.
J.Mol.Biol.
|