2.7.9.5	ATP + alpha-glucan + H2O	dikinases use ATP as a dual phosphate donor and transfer the beta- and gamma-phosphate groups to two distinct acceptor molecules, a glucan and water. A conserved histidine residue within this domain is capable of accepting the beta-phosphate group of ATP following nucleotide binding and hydrolysis. The phosphoramidate bond is acid labile, but rather stable under alkaline conditions. The gamma-phosphate group is transferred to water	
2.7.9.5	ATP + [phospho-alpha-glucan]	the enzyme phosphorylates granular starch that has previously been phosphorylated by EC 2.7.9.4, alpha-glucan, water dikinase	
2.7.9.5	ATP + [phospho-alpha-glucan] + H2O	important enzymes of starch metabolism. Catalyzes the addition of phosphate groups to amylopectin chains at the surface of starch granules, changing its physicochemical properties	
2.7.9.5	ATP + [phospho-alpha-glucan] + H2O	the enzyme is involved in starch phosphorylation, a key step in starch degradation