MoaA/NifB/PqqE, iron-sulphur binding, conserved site
Short name | MoaA_NifB_PqqE_Fe-S-bd_CS |
Description
* 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.
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
biological process
- None
molecular function
cellular component
- None
Cross References
Contributing Member Database Entry
- PROSITE patterns:PS01305