An FAD-requiring monooxygenase active on tetracycline antibiotic and some of its derivatives, which leads to their inactivation (PubMed:26097034). Expression in E.coli confers high resistance to oxytetracycline, slightly less resistance to tetracycline, moderate resistance to minocycline but no resistance to tigecycline. Degrades tetracycline and oxytetracycline; the reaction requires NADPH (PubMed:26097034). Degrades and confers resistance to chlortetracycline (PubMed:28481346). 7-chlorotetracycline + H(+) + NADPH + O2 = (1S,10S,10aS)-3-(CONH2)-9-Cl-1-(Me2N)-3,3a,4,10-(HO)4-10-Me-2,5-dioxo-1H,10aH,11H,11aH-cyclopenta[b]anthracen-6-olate + CO + H2O + NADP(+) a tetracycline + H(+) + NADPH + O2 = a (1S,10aS)-3-(CONH2)-1-(Me2N)-3,3a,4,6-(HO)4-2,5-dioxo-1H,10aH,11H,11aH-cyclopenta[b]anthracene + CO + H2O + NADP(+) Binds 1 FAD per subunit. Inhibited by anhydrotetracycline. Consists of an N-terminal FAD-binding domain with a Rossman fold, a substrate-binding domain and a C-terminal helix that bridges the 2 domains close to the antibiotic-binding site. This last helix is flexible, is not found in TetX of Bacteroides species, and may contribute to their different substrate specificities. Isolated from an agricultural soil sample. Tetracycline antibiotics bind to the ribosomal acceptor site (A-site), preventing binding of the aminoacyl-tRNA to the A-site. The hydrophilic side of tetracycline makes many hydrogen-bonding interactions with oxygen atoms of the ribosome's phosphate backbone. Belongs to the aromatic-ring hydroxylase family.