Conserved Site

MoaA/nifB/pqqE, iron-sulphur binding, conserved site (IPR000385)

Short name: MoaA_NifB_PqqE_Fe-S-bd_CS


A number of proteins involved in the biosynthesis of metallo cofactors have been shown [PMID: 8588735, PMID: 7890743] to be evolutionary related. These include:

  • Bacterial and archebacterial protein moaA, which is involved in the biosynthesis of the molybdenum cofactor (molybdopterin; MPT).
  • Arabidopsis thaliana (Mouse-ear cress) cnx2, a protein involved in molybdopterin biosynthesis and which is highly similar to moaA.
  • Bacillus subtilis narA, which seems to be the moaA ortholog in that bacteria.
  • Bacterial protein nifB (or fixZ) which is involved in the biosynthesis of the nitrogenase iron-molybdenum cofactor.
  • Bacterial protein pqqE which is involved in the biosynthesis of the cofactor pyrrolo-quinoline-quinone (PQQ).
  • Pyrococcus furiosus cmo, a protein involved in the synthesis of a molybdopterin-based tungsten cofactor.
  • Caenorhabditis elegans hypothetical protein F49E2.1.
These proteins share, in their N-terminal region, a conserved domain that contains three cysteines. In moaA, these cysteines have been shown to be important for biological activity by binding a [4Fe-4S] cluster [PMID: 15317939]. The three cysteines each coordinate one Fe, while S-adenosylmethionine is the fourth ligand to the cluster and binds to its unique Fe as an N/O chelate.

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0051539 4 iron, 4 sulfur cluster binding
GO:0003824 catalytic activity
GO:0046872 metal ion binding

Cellular Component

No terms assigned in this category.

Contributing signatures

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