| Primary Identifier | IPR005972 | Type | Family |
| Short Name | Nase_Mo-Fe_asu |
| description | The enzyme responsible for nitrogen fixation, the nitrogenase, shows a high degree of conservation of structure, function, and amino acid sequence across wide phylogenetic ranges. All known Mo-nitrogenases consist of two components, component I (also called dinitrogenase, or Fe-Mo protein), an alpha2beta2 tetramer encoded by the nifD and nifK genes, and component II (dinitrogenase reductase, or Fe protein) a homodimer encoded by the nifH gene [, ]which has an Fe4S4 cluster bound between the subunits and two ATP-binding domains. The Fe protein supplies energy by ATP hydrolysis, and transfers electrons from reduced ferredoxin or flavodoxin to component 1 for the reduction of molecular nitrogen to ammonia [, ]. Nitrogenase contains two unusual rare metal clusters; one of them is the iron molybdenum cofactor (FeMo-co), which is considered to be the site of dinitrogen reduction and whose biosynthesis requires the products of the nifNE operon and of some other nif genes []. It has been proposed that nifNE might serve as a scaffold upon which FeMo-co is built and then inserted into component I [].This entry refers to the alpha subunit of the MoFe protein (component I) of molybdenum (Mo-) nitrogenase, which is encoded by the nifD gene. |
