PROSITE documentation PDOC00375
Bacterial quinoprotein dehydrogenases signatures


Pyrrolo-quinoline quinone (PQQ) is redox coenzyme, which serves as a cofactor for a number of enzymes (quinoproteins) and particularly for some bacterial dehydrogenases [1,2]. A number of these bacterial quinoproteins are clearly evolutionary related. These proteins are listed below.

  • Methanol dehydrogenases (MDH) (EC, from methylotrophs.
  • Ethanol dehydrogenases from Acetobacter aceti [3].
  • Glucose dehydrogenase (EC from Acinetobacter calcoaceticus, Escherichia coli, and Gluconobacter oxydans [4].

These dehydrogenases all have from 600 to 800 amino acids. We developed two signature patterns for these proteins using sequence data from well conserved regions: the first one is located in the N-terminal half while the second one is from the C-terminal half.

Last update:

December 2004 / Patterns and text revised.


Technical section

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

BACTERIAL_PQQ_1, PS00363; Bacterial quinoprotein dehydrogenases signature 1  (PATTERN)

BACTERIAL_PQQ_2, PS00364; Bacterial quinoprotein dehydrogenases signature 2  (PATTERN)


1AuthorsDuine J.A. Jongejan J.A.
TitleQuinoproteins, enzymes with pyrrolo-quinoline quinone as cofactor.
SourceAnnu. Rev. Biochem. 58:403-426(1989).
PubMed ID2549854

2AuthorsGallop P.M. Paz M.A. Flueckiger R. Kagan H.M.
TitlePQQ, the elusive coenzyme.
SourceTrends Biochem. Sci. 14:343-346(1989).
PubMed ID2572081

3AuthorsInoue T. Sunagawa M. Mori A. Imai C. Fukuda M. Takagi M. Yano K.
TitleCloning and sequencing of the gene encoding the 72-kilodalton dehydrogenase subunit of alcohol dehydrogenase from Acetobacter aceti.
SourceJ. Bacteriol. 171:3115-3122(1989).
PubMed ID2722742

4AuthorsCleton-Jansen A.-M. Dekker S. van de Putte P. Goosen N.
SourceMol. Gen. Genet. 229:206-212(1991).

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