The NifA protein is responsible for transcription activation of nif genes in the endophytic diazotroph Herbaspirillum seropedicae. When expressed in Escherichia coli this NifA protein is unable to activate the transcription of a Klebsiella pneumoniae nifH::lacZ fusion. However, a form of NifA lacking the N-terminal domain did activate transcription and its activity was not inhibited by ammonium. In this work we show that when expressed separately, the N-terminal domain of H. seropedicae NifA protein can restore ammonium control of the N-truncated NifA activity in E. coli. This effect is dependent on the relative concentrations of the N-terminal domain and the N-truncated protein and suggests that the N-terminal domain behaves in this respect in a manner similar to that of NifL of the gamma proteobacteria.