S
IPR000385

MoaA/NifB/PqqE, iron-sulphur binding, conserved site

InterPro entry
Short nameMoaA_NifB_PqqE_Fe-S-bd_CS

Description

A number of proteins involved in the biosynthesis of metallo cofactors have been shown
[2, 3]
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
[1]
. 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.

References

1.Crystal structure of the S-adenosylmethionine-dependent enzyme MoaA and its implications for molybdenum cofactor deficiency in humans. Hanzelmann P, Schindelin H. Proc. Natl. Acad. Sci. U.S.A. 101, 12870-5, (2004). View articlePMID: 15317939

2.A pAO1-encoded molybdopterin cofactor gene (moaA) of Arthrobacter nicotinovorans: characterization and site-directed mutagenesis of the encoded protein. Menendez C, Igloi G, Henninger H, Brandsch R. Arch. Microbiol. 164, 142-51, (1995). View articlePMID: 8588735

3.Isolation of two Arabidopsis cDNAs involved in early steps of molybdenum cofactor biosynthesis by functional complementation of Escherichia coli mutants. Hoff T, Schnorr KM, Meyer C, Caboche M. J. Biol. Chem. 270, 6100-7, (1995). View articlePMID: 7890743

GO terms

Cross References

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