This entry contains cytosolic Fe-S cluster assembling factors NBP35 and CFD1. The NBP35-CFD1 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins. Nucleotide binding and hydrolysis seems to be critical for loading of Fe-S clusters onto CFD1 and NBP35 [, , ]. In higher eukaryotes NBP35 and CFD1 are known as NUBP1 and NUBP2, and NUBP1 is also involved in iron regulation [].Bacterial homologues ApbC and MRP (Multiple Resistance and pH adaptation in E. coli) have been shown to contain an ATP-binding domain at the N terminus and have ATPase activity. MRP is a membrane-spanning protein and functions as a Na+/H+ antiporter [, ]. Archaeal homologues function as iron-sulfur cluster carriers [].
