Protein Domain : Sulphate adenylyltransferase IPR002650

Type	Domain
Description	Sulphate adenylyltransferase or ATP-sulfurylase ( ) forms adenosine 5'-phosphosulphate (APS) from ATP and free sulphate, the first step in the formation of the activated sulphate donor 3'-phosphoadenylylsulphate (PAPS) [ ]. 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 [ ]. 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. [, , , , , , , , ].
Short Name	Sulphate_adenylyltransferase