InterPro domain: IPR002650

General Information

  • Identifier IPR002650
  • Description Sulphate adenylyltransferase
  • Number of genes 299
  • Gene duplication stats Loading...
  • Associated GO terms GO:0004781   GO:0000103  

Abstract

Sulphate adenylyltransferase or ATP-sulfurylase ( 2.7.7.4 ) forms adenosine 5'-phosphosulphate (APS) from ATP and free sulphate, the first step in the formation of the activated sulphate donor 3'-phosphoadenylylsulphate (PAPS) [ 1 ]. In some cases, it is found in a bifunctional protein in which the other domain, adenosyl phosphosulphate (APS) kinase, catalyses the second and final step, the phosphorylation of APS to PAPS [ 2 ]. The combined ATP sulfurylase/APS kinase may be called PAPS synthase. In some organisms it is used to generate APS from sulfate and ATP, while in others it proceeds in the opposite direction to generate ATP from APS and pyrophosphate. ATP sulfurylase can be a monomer, a homodimer, or a homo-oligomer, depending on the organism. It belongs to a large superfamily of nucleotidyltransferases that includes pantothenate synthetase (PanC), phosphopantetheine adenylyltransferase (PPAT), the amino-acyl tRNA synthetases, and the dissimilatory sulphate adenylyltransferase (sat) of the sulphate reducer Archaeoglobus fulgidus. The enzymes of this family are structurally similar and share a dinucleotide-binding domain. [ 3 , 4 , 5 , 6 , 7 , 8 , 9 , 10 , 11 ].


1. A multifunctional Urechis caupo protein, PAPS synthetase, has both ATP sulfurylase and APS kinase activities. Gene 165, 243-8
2. The isolation and characterization of cDNA encoding the mouse bifunctional ATP sulfurylase-adenosine 5'-phosphosulfate kinase. J. Biol. Chem. 270, 29453-9
3. The complex structures of ATP sulfurylase with thiosulfate, ADP and chlorate reveal new insights in inhibitory effects and the catalytic cycle. J. Mol. Biol. 313, 1117-25
4. Crystal structure of ATP sulfurylase from Penicillium chrysogenum: insights into the allosteric regulation of sulfate assimilation. Biochemistry 40, 6795-804
5. Crystal structure of ATP sulfurylase from the bacterial symbiont of the hydrothermal vent tubeworm Riftia pachyptila. Biochemistry 40, 14509-17
6. Crystal structure of a novel zinc-binding ATP sulfurylase from Thermus thermophilus HB8. Biochemistry 43, 4111-8
7. Sulfate activation and transport in mammals: system components and mechanisms. Chem. Biol. Interact. 109, 143-51
8. Molecular genetics of sulfur assimilation in filamentous fungi and yeast. Annu. Rev. Microbiol. 51, 73-96
9. Enzymology and molecular biology of prokaryotic sulfite oxidation. FEMS Microbiol. Lett. 203, 1-9
10. Activity and stability of recombinant bifunctional rearranged and monofunctional domains of ATP-sulfurylase and adenosine 5'-phosphosulfate kinase. J. Biol. Chem. 274, 10751-7
11. The cytidylyltransferase superfamily: identification of the nucleotide-binding site and fold prediction. Proteins 22, 259-66

Species distribution

Gene table

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