cd01997

The C-terminal domain of GMP synthetase. It contains two subdomains; the ATP pyrophosphatase domain which closes to the N-termial and the dimerization domain at C-terminal end. The ATP-PPase is a twisted, five-stranded parallel beta-sheet sandwiched between helical layers. It has a signature nucleotide-binding motif, or P-loop, at the end of the first-beta strand.The dimerization domain formed by the C-terminal 115 amino acid for prokaryotic proteins. It is adjacent to teh ATP-binding site of the ATP-PPase subdomain. The largest difference between the primary sequence of prokaryotic and eukaryotic GMP synthetase map to the dimerization domain.Eukaryotic GMP synthetase has several large insertions relative to prokaryotes.