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| PROSITE documentation PDOC00375 [for PROSITE entry PS00364] |
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 1.1.99.8), from methylotrophs.
- Ethanol dehydrogenases from Acetobacter aceti [3].
- Glucose dehydrogenase (EC 1.1.5.2) 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.
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PROSITE methods (with tools and information) covered by this documentation:
| 1 | Authors | Duine J.A. Jongejan J.A. |
| Title | Quinoproteins, enzymes with pyrrolo-quinoline quinone as cofactor. | |
| Source | Annu. Rev. Biochem. 58:403-426(1989). | |
| PubMed ID | 2549854 | |
| DOI | 10.1146/annurev.bi.58.070189.002155 |
| 2 | Authors | Gallop P.M. Paz M.A. Flueckiger R. Kagan H.M. |
| Title | PQQ, the elusive coenzyme. | |
| Source | Trends Biochem. Sci. 14:343-346(1989). | |
| PubMed ID | 2572081 |
| 3 | Authors | Inoue T. Sunagawa M. Mori A. Imai C. Fukuda M. Takagi M. Yano K. |
| Title | Cloning and sequencing of the gene encoding the 72-kilodalton dehydrogenase subunit of alcohol dehydrogenase from Acetobacter aceti. | |
| Source | J. Bacteriol. 171:3115-3122(1989). | |
| PubMed ID | 2722742 |
| 4 | Authors | Cleton-Jansen A.-M. Dekker S. van de Putte P. Goosen N. |
| Source | Mol. Gen. Genet. 229:206-212(1991). |
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