Component of the dicamba O-demethylase multicomponent enzyme system involved in the degradation of the herbicide dicamba (PubMed:15855162, PubMed:15820213, PubMed:16535584). In vitro, catalyzes the O-demethylation of 2-methoxy-3,6-dichlorobenzoic acid (dicamba) to yield 3,6-dichlorosalicylic acid (DCSA) via an exocyclic monooxygenation (PubMed:15855162, PubMed:15820213, PubMed:16535584, PubMed:19616009). 3,6-dichloro-2-methoxybenzoate + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = 3,6-dichlorosalicylate + formaldehyde + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] Binds 1 [2Fe-2S] cluster per subunit. Activity enhanced by Fe(2+) and Mg(2+) ions. Optimum pH is between 6.5-7.5. Optimum temperature is 30 degrees Celsius. Homotrimer (PubMed:15820213, PubMed:19616009, PubMed:19616011). The dicamba O-demethylase multicomponent enzyme system is composed of an oxygenase component (DdmC) and an electron transfer component formed by a ferredoxin reductase (DdmA) and a ferredoxin (DdmB) (PubMed:15855162, PubMed:15820213, PubMed:16535584). In vitro, dicamba O-demethylase assays in which DdmA2 is substituted for DdmA1 demonstrate that the two enzymes possess nearly identical activities (PubMed:15855162).