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PROSITE documentation PDOC01009

moaA / nifB / pqqE family signature





Description

A number of proteins involved in the biosynthesis of metallo cofactors have been shown [1,2] to be evolutionary related. These proteins are:

  • Bacterial and archebacterial protein moaA, which is involved in the biosynthesis of the molybdenum cofactor (molybdopterin; MPT).
  • Arabidopsis thaliana cnx2, a protein involved in molybdopterin biosynthesis and which is highlys 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.

All these proteins share, in their N-terminal region, a conserved domain that contains three cysteines. In moaA, these cysteines have been shown [1] to be important for the biological activity. They could be inolved in the binding of an iron-sulfur cluster.

Expert(s) to contact by email:

Menendez C.

Last update:

May 2004 / Text revised.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

MOAA_NIFB_PQQE, PS01305; moaA / nifB / pqqE family signature  (PATTERN)


References

1AuthorsMenendez C. Igloi G. Henninger H. Brandsch R.
TitleA pAO1-encoded molybdopterin cofactor gene (moaA) of Arthrobacter nicotinovorans: characterization and site-directed mutagenesis of the encoded protein.
SourceArch. Microbiol. 164:142-151(1995).
PubMed ID8588735

2AuthorsHoff T. Schnorr K.M. Meyer C. Caboche M.
TitleIsolation of two Arabidopsis cDNAs involved in early steps of molybdenum cofactor biosynthesis by functional complementation of Escherichia coli mutants.
SourceJ. Biol. Chem. 270:6100-6107(1995).
PubMed ID7890743



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