For enhancement of cis,cis-muconate productivity from benzoate, catechol 1,2-dioxygenase (C12O) which catalyzes the rate-limiting step (catechol conversion to cis,cis-muconate) was cloned and expressed in recombinant Pseudomonas putida BCM114. At higher benzoate concentrations (more than 15 mM), cis,cis-muconate productivity gradually decreased and unconverted catechol was accumulated up to 10 mM in the case of wildtype P. putida BM014, whereas cis,cis-muconate productivity continuously increased and catechol was completely transformed to cis,cis-muconate for P. putida BCM114. Specific C120 activity of P. putida BCM114 was about three times higher than that of P. putida BM014, and productivity was enhanced more than two times.