F
IPR002650

Sulphate adenylyltransferase

InterPro entry
Short nameSulphate_adenylyltransferase
Overlapping
homologous
superfamilies
 
family relationships

Description

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]
.

References

1.A multifunctional Urechis caupo protein, PAPS synthetase, has both ATP sulfurylase and APS kinase activities. Rosenthal E, Leustek T. Gene 165, 243-8, (1995). View articlePMID: 8522184

2.The isolation and characterization of cDNA encoding the mouse bifunctional ATP sulfurylase-adenosine 5'-phosphosulfate kinase. Li H, Deyrup A, Mensch JR Jr, Domowicz M, Konstantinidis AK, Schwartz NB. J. Biol. Chem. 270, 29453-9, (1995). View articlePMID: 7493984

3.The complex structures of ATP sulfurylase with thiosulfate, ADP and chlorate reveal new insights in inhibitory effects and the catalytic cycle. Ullrich TC, Huber R. J. Mol. Biol. 313, 1117-25, (2001). View articlePMID: 11700067

4.Crystal structure of ATP sulfurylase from Penicillium chrysogenum: insights into the allosteric regulation of sulfate assimilation. MacRae IJ, Segel IH, Fisher AJ. Biochemistry 40, 6795-804, (2001). View articlePMID: 11389593

5.Crystal structure of ATP sulfurylase from the bacterial symbiont of the hydrothermal vent tubeworm Riftia pachyptila. Beynon JD, MacRae IJ, Huston SL, Nelson DC, Segel IH, Fisher AJ. Biochemistry 40, 14509-17, (2001). View articlePMID: 11724564

6.Crystal structure of a novel zinc-binding ATP sulfurylase from Thermus thermophilus HB8. Taguchi Y, Sugishima M, Fukuyama K. Biochemistry 43, 4111-8, (2004). View articlePMID: 15065853

7.Sulfate activation and transport in mammals: system components and mechanisms. Schwartz NB, Lyle S, Ozeran JD, Li H, Deyrup A, Ng K, Westley J. Chem. Biol. Interact. 109, 143-51, (1998). View articlePMID: 9566742

8.Molecular genetics of sulfur assimilation in filamentous fungi and yeast. Marzluf GA. Annu. Rev. Microbiol. 51, 73-96, (1997). View articlePMID: 9343344

9.Enzymology and molecular biology of prokaryotic sulfite oxidation. Kappler U, Dahl C. FEMS Microbiol. Lett. 203, 1-9, (2001). View articlePMID: 11557133

10.Activity and stability of recombinant bifunctional rearranged and monofunctional domains of ATP-sulfurylase and adenosine 5'-phosphosulfate kinase. Deyrup AT, Krishnan S, Singh B, Schwartz NB. J. Biol. Chem. 274, 10751-7, (1999). View articlePMID: 10196147

11.The cytidylyltransferase superfamily: identification of the nucleotide-binding site and fold prediction. Bork P, Holm L, Koonin EV, Sander C. Proteins 22, 259-66, (1995). View articlePMID: 7479698

GO terms

Cross References

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