PROSITE documentation PDOC00484
Eukaryotic molybdopterin oxidoreductases signature


A number of different eukaryotic oxidoreductases that require and bind a molybdopterin cofactor have been shown [1] to share a few regions of sequence similarity. These enzymes are:

  • Xanthine dehydrogenase (EC, which catalyzes the oxidation of xanthine to uric acid with the concomitant reduction of NAD. Structurally, this enzyme of about 1300 amino acids consists of at least three distinct domains: an N-terminal 2Fe-2S ferredoxin-like iron-sulfur binding domain (see <PDOC00175>), a central FAD/NAD-binding domain and a C-terminal Mo- pterin domain.
  • Aldehyde oxidase (EC, which catalyzes the oxidation aldehydes into acids. Aldehyde oxidase is highly similar to xanthine dehydrogenase in its sequence and domain structure.
  • Nitrate reductase (EC, which catalyzes the reduction of nitrate to nitrite. Structurally, this enzyme of about 900 amino acids consists of an N-terminal Mo-pterin domain, a central cytochrome b5-type heme-binding domain (see <PDOC00170>) and a C-terminal FAD/NAD-binding cytochrome reductase domain.
  • Sulfite oxidase (EC, which catalyzes the oxidation of sulfite to sulfate. Structurally, this enzyme of about 460 amino acids consists of an N-terminal cytochrome b5-binding domain followed by a Mo-pterin domain.

There are a few conserved regions in the sequence of the molybdopterin-binding domain of these enzymes. The pattern we use to detect these proteins is based on one of them. It contains a cysteine residue which could be involved in binding the molybdopterin cofactor.

Last update:

April 2006 / Pattern revised.


Technical section

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

MOLYBDOPTERIN_EUK, PS00559; Eukaryotic molybdopterin oxidoreductases signature  (PATTERN)


1AuthorsWootton J.C. Nicolson R.E. Cock J.M. Walters D.E. Burke J.F. Doyle W.A. Bray R.C.
TitleEnzymes depending on the pterin molybdenum cofactor: sequence families, spectroscopic properties of molybdenum and possible cofactor-binding domains.
SourceBiochim. Biophys. Acta 1057:157-185(1991).
PubMed ID2015248

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