CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.620 | HUPs |
Domain Context
CATH Clusters
| Superfamily | HUPs |
| Functional Family | bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1 |
Enzyme Information
| 2.7.7.4 |
Sulfate adenylyltransferase.
based on mapping to UniProt O43252
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.
|
| 2.7.1.25 |
Adenylyl-sulfate kinase.
based on mapping to UniProt O43252
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.
|
UniProtKB Entries (1)
| O43252 |
PAPS1_HUMAN
Homo sapiens
Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1
|
PDB Structure
| PDB | 1XJQ |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
The crystal structure of human PAPS synthetase 1 reveals asymmetry in substrate binding
J.Mol.Biol.
|
