Biofilm formation is the most effective pathway for electron transfer to anodes in bioelectrochemical systems. However, the mechanisms triggering biofilm formation under anoxic conditions, as well as the architectural and compositional factors that positively influence current generation, are not well understood. Recent findings have shown that riboflavin can function similarly to a quorum sensing molecule in the γ-proteobacterium Shewanella oneidensis. Enhanced biofilm formation induced by riboflavin correlates with increased current densities. Only a limited number of candidate proteins were found to have altered concentrations due to this quorum sensing mechanism. This study demonstrates that the catalytic functions of the UDP-N-acetylglucosamine C4 epimerase WbpP and UDP-N-acetyl-D-glucosamine 6-dehydrogenase WbpA affect biofilm formation and lead to increased current density. Using optical coherence tomography, we found that the expression of each protein individually causes specific, quantifiable changes in biofilm architecture, including biovolume, height, and porosity. However, the current density did not significantly differ when these proteins were expressed alone compared to the control. In contrast, co-expression of WbpP and WbpA resulted in a doubling of current density, closely resembling the increases observed with riboflavin-mediated quorum sensing. We hypothesize that riboflavin-based quorum sensing may lead, through several intermediary steps, to the overproduction of WbpA and WbpP, resulting in better attachment to graphite anodes and thus higher current densities.