Catalyzes the phosphorylation of adenosine to adenosine monophosphate (AMP) (PubMed:14594827, PubMed:16511094). Can also catalyze the phosphorylation of the adenosine analog 2-methyladenosine (methyl-Ado) to methyl-AMP, the first step in the metabolism of this compound to an active form that displays antitubercular activity. Is not active on guanosine, inosine, deoxyadenosine, cytidine, uridine, or thymidine. Prefers dGTP and GTP to ATP as phosphate donors in vitro (PubMed:14594827). adenosine + ATP = ADP + AMP + H(+) adenosine + GTP = AMP + GDP + H(+) adenosine + dGTP = AMP + dGDP + H(+) The enzyme is subject to substrate inhibition by adenosine and is competitively inhibited by the adenosine analog iodotubercidin. Unlike other adenosine kinases it is not stimulated by inorganic phosphate. Activity is stimulated in the presence of potassium (PubMed:14594827). Is inhibited by a series of 7-(het)aryl-7-deazaadenine ribonucleosides bearing small and bulky substituents in position 7; some of them display micromolar antimycobacterial activity and low cytotoxicity (PubMed:25259627). Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenosine: step 1/1. Homodimer. Was identified as a high-confidence drug target. Belongs to the carbohydrate kinase PfkB family.