CATH Classification

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
Lalor, D.J., Schnyder, T., Saridakis, V., Pilloff, D.E., Dong, A., Tang, H., Leyh, T.S., Pai, E.F.
Protein Eng.