Dihydroorotate dehydrogenase, electron transfer subunit, iron-sulphur cluster binding domain (IPR019480)

Short name: Dihydroorotate_DH_Fe-S-bd

Overlapping homologous superfamilies

Domain relationships



Lactococcus lactis is one of the few organisms with two dihydroorotate dehydrogenases (DHODs) A and B [PMID: 11188687]. The B enzyme is typical of DHODs in Gram-positive bacteria that use NAD+ as the second substrate. DHODB is a heterotetramer composed of a central homodimer of PyrDB subunits resembling the DHODA structure and two PyrK subunits along with three different cofactors: FMN, FAD, and a [2Fe-2S] cluster. The [2Fe-2S] iron-sulphur cluster binds to this C-terminal domain of the PyrK subunit, which is at the interface between the flavin and NAD binding domains and contains three beta-strands. The four cysteine residues at the N-terminal part of this domain are the ones that bind, in pairs, to the iron-sulphur cluster. The conformation of the whole molecule means that the iron-sulphur cluster is localized in a well-ordered part of this domain close to the FAD binding site [PMID: 11188687]. The FAD and NAD binding domains are IPR008333 and IPR001433 respectively.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.