TobZ is involved in the biosynthesis of the 2-deoxystreptamine-containing aminoglycoside antibiotics such as nebramycin 5 and 6-O-carbamoylkanamycin. Catalyzes the hydrolysis of carbamoyl phosphate and its subsequent adenylation by ATP to yield O-carbamoyladenylate. Then it catalyzes the transfer of the carbamoyl moiety from O-carbamoyladenylate to the tobramycin 6-hydroxy group to yield nebramycin 5'. It catalyzes the same reaction with kanamycin A. These reactions are considerably slower in the presence of deoxy-ATP. ATP + carbamoyl phosphate + H2O + tobramycin = AMP + diphosphate + H(+) + nebramycin 5' + phosphate ATP + carbamoyl phosphate + H2O + kanamycin A = 6''-O-carbamoylkanamycin A + AMP + diphosphate + H(+) + phosphate ATP + carbamoyl phosphate + H2O = carbamoyl adenylate + diphosphate + phosphate carbamoyl adenylate + tobramycin = AMP + H(+) + nebramycin 5' carbamoyl adenylate + kanamycin A = 6''-O-carbamoylkanamycin A + AMP + H(+) Binds 1 Fe(2+) ion per subunit. ADP inhibits the formation of nebramycin 5'. Antibiotic biosynthesis; kanamycin biosynthesis. Antibiotic biosynthesis; tobramycin biosynthesis. Consists of two major domains: the N-terminal domain (Kae1-like) is involved in the transfer of carbamoyl from O-carbamoyladenylate to tobramycin or kanamycin; the C-terminal domain (YrdC-like) is involved in the hydrolysis of carbamoyl phosphate and its subsequent adenylation by ATP. Cells lacking this gene accumulate kanamycin. It seems that TobZ plays a solely passive role in the adenylation reaction: all functional groups appear to be provided by the substrates themselves, representing an extreme form of substrate-assisted catalysis. The role of the iron in catalysis remains unclear (PubMed:22383337). Belongs to the NodU/CmcH family.