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 Q12650
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)
Q12650 |
MET3_PENCH
Penicillium chrysogenum
Sulfate adenylyltransferase
|
PDB Structure
PDB | 1M8P |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | Escherichia |
Primary Citation |
Allosteric Inhibition via R-State Destabilization in
ATP Sulfurylase from Penicillium chrysogenum
Nat.Struct.Biol.
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