Component of the chloroacetanilide N-alkylformylase multicomponent enzyme system involved in the degradation of chloroacetanilide herbicides (N-alkoxyalkyl-N-chloroacetyl-substituted aniline derivatives). In vitro, catalyzes the N-dealkylation of butachlor, alachlor and acetochlor to yield 2-chloro-N-(2,6-diethylphenyl)acetamide (CDEPA) (for alachlor and butachlor) and 2-chloro-N-(2-methyl-6-ethylphenyl)acetamide (CMEPA) (for acetochlor). butachlor + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = butyl formate + H2O + N-(2,6-diethylphenyl)-2-chloroacetamide + 2 oxidized [2Fe-2S]-[ferredoxin] alachlor + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = H2O + methyl formate + N-(2,6-diethylphenyl)-2-chloroacetamide + 2 oxidized [2Fe-2S]-[ferredoxin] acetochlor + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = ethyl formate + H2O + N-(2-ethyl-6-methylphenyl)-2-chloroacetamide + 2 oxidized [2Fe-2S]-[ferredoxin] Binds 1 [2Fe-2S] cluster per subunit. Activity enhanced by Fe(2+) and Mg(2+) ions. Divalent cations such as Ca(2+), Cr(2+), Co(2+), and Mn(2+) show moderate inhibition of the enzyme, whereas heavy metal ions such as Ag(+), Cu(2+), Pb(2+), Hg(2+), Ni(2+) and Zn(2+) severely inhibit the activity. Optimum pH is 7. Optimum temperature is 35 degrees Celsius. The chloroacetanilide N-alkylformylase multicomponent enzyme system is composed of an oxygenase component (CndA) and an electron transfer component formed by a ferredoxin reductase (CndC1) and a ferredoxin (CndB1). In vitro, chloroacetanilide N-alkylformylase assays in which CndB1 is substituted for CndB2 demonstrate that the two enzymes possess nearly identical activities.