Leishmaniasis is an illness with a broad spectrum of symptoms caused by parasites of the Leishmania genus, some of which have developed resistance to current treatments, making it necessary to identify new pharmacological targets. The NAD kinase enzyme catalyzes the last reaction of the NADP(H) biosynthesis, an essential molecule in all living beings due to their multiple functions as cofactor in biosynthetic pathways, oxidative defense systems and as precursor of calcium mobilizing molecules. In this study, we identified the NAD kinase in L. braziliensis (LbNADK) by means of bioinformatics and experimental approaches. Predictive structural models revealed conserved characteristics typical of this type of proteins, such as the Rossmann fold, as well as an exclusive N-terminal insertion. The catalytic domain of the enzyme was cloned and expressed as recombinant protein, whose functional identity and kinetic parameters were determined through enzymatic activity assays, indicating differences with the human NMNATs. These findings evidence the involvement of the LbNADK in the biosynthesis of NADP(H) in Leishmania , whose exclusive N-terminal insertion must be characterized as a possible novel pharmacological target.