3.1.12.1	iron-sulfur centre	contains a [4Fe-4S] cluster	726307	
3.1.12.1	iron-sulfur centre	near the active site, each enzyme protomer contains one [4Fe-4S] cluster, which is important for both maintaining the decameric state and nuclease activity	725211	
3.1.12.1	K+	nuclease activity of the enzyme is maximal in the presence of 20-200 mM KCl	725211	
3.1.12.1	Mg2+	cleavage of a 15T DNA oligonucleotide by Sso0001 is observed in the presence of either magnesium or manganese, yielding a cluster of products of around 1–5 nt in size. A 20U RNA oligonucleotide is cleaved in the presence of manganese but not magnesium	726307	
3.1.12.1	Mg2+	nuclease activity of the enzyme is maximal in the presence of Mg2+ or Mn2+ (5 mM)	725211	
3.1.12.1	Mn2+	cleavage of a 15T DNA oligonucleotide by Sso0001 is observed in the presence of either magnesium or manganese, yielding a cluster of products of around 1–5 nt in size. A 20U RNA oligonucleotide is cleaved in the presence of manganese but not magnesium	726307	
3.1.12.1	Mn2+	nuclease activity of the enzyme is maximal in the presence of Mg2+ or Mn2+ (5 mM). Mn2+ is bound in the active site located inside the internal tunnel	725211	
3.1.12.1	additional information	Ca2+ does not support the nuclease activity	725211