Protein Domain : TorD-like superfamily IPR036411

Type	Homologous_superfamily
Description	This superfamily is represented by TorD. TorD is involved in the maturation of the the trimethylamine N-oxide reductase TorA (a DMSO reductase family member) in Escherichia coli [ ]. TorA is a molybdenum-containing enzyme which requires the the insertion of a bis(molybdopterin guanine dinucleotide) molybdenum (bis(MGD)Mo) cofactor in its catalytic site to be active and translocated to the periplasm. TorD acts as a chaperone, binding to apoTorA and promoting efficient incorporation of the cofactor into the protein. This superfamily also includes DmsD, which could be required for the biogenesis of DMSO reductase rather than for the targeting of DmsA to the inner membrane [ , , ]. TorD and DmsD have a number of common features suggesting they function by using similar mechanisms. A major structural difference is that TorD is a domain-swapped dimer, while DmsD exists as a monomer [].
Short Name	TorD-like_sf