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AAA family ATPase
Adenylate kinase, active site lid
Comparisons of adenylate kinases have revealed a particular divergence in the active site lid. In some organisms, particularly the Gram-positive bacteria, residues in the lid domain have been mutated to cysteines and these cysteine residues are responsible for the binding of a zinc ion. The bound zinc ion in the lid domain, is clearly structurally homologous to Zinc-finger domains. However, it is unclear whether the adenylate kinase lid is a novel zinc-finger DNA/RNA binding domain, or that the lid bound zinc serves a purely structural function [1]. [1]. 9715904. Crystal structures of Bacillus stearothermophilus adenylate kinase with bound Ap5A, Mg2+ Ap5A, and Mn2+ Ap5A reveal an intermediate lid position and six coordinate octahedral geometry for bound Mg2+ and Mn2+. Berry MB, Phillips GN Jr;. Proteins 1998;32:276-288. (from Pfam)
nucleoside monophosphate kinase
adenylate kinase
Members of this family have adenylate kinase activity (EC 2.7.4.3), interconverting ATP + AMP with 2 ADP, although for some members, that activity falls within the broader activity of EC 2.7.4.10 (NTP + AMP = NDP + ADP).
nucleoside monophosphate kinase catalyzes the transfer of the terminal phosphoryl group from a nucleoside triphosphate, usually ATP, to a nucleoside monophosphate
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