AlkJ , an alcohol dehydrogenase from Pseudomonas oleovorans, which
converts aliphatic medium-chain-length alcohols into aldehydes.
Cellobiose dehydrogenase (CDH) (EC 188.8.131.52) from Phanerochaete
This family also includes a lyase:
(R)-mandelonitrile lyase (EC 184.108.40.206) (hydroxynitrile lyase) from plants
, an enzyme involved in cyanogenis, the release of hydrogen cyanide from
These enzymes are proteins of size ranging from 556 (CHD) to 664 (MOX) amino
acid residues which share a number of regions of sequence similarities. One of
these regions, located in the N-terminal section, corresponds to the FAD ADP-binding domain. The function of the other conserved domains is not yet known;
we have selected two of these domains as signature patterns. The first one is
located in the N-terminal section of these enzymes, about 50 residues after
the ADP-binding domain, while the second one is located in the central
May 2008 / Text revised.
PROSITE methods (with tools and information) covered by this documentation:
GMC oxidoreductases. A newly defined family of homologous proteins with diverse catalytic activities.
van Beilen J.B. Eggink G. Enequist H. Bos R. Witholt B.
Mol. Microbiol. 6:3121-3136(1992).
Cheng I.P. Poulton J.E.
Plant Cell Physiol. 34:1139-1143(1993).
PROSITE is copyright. It is produced by the SIB Swiss Institute
Bioinformatics. There are no restrictions on its use by non-profit
institutions as long as its content is in no way modified. Usage by and
for commercial entities requires a license agreement. For information
about the licensing scheme send an email to
or see: prosite_license.html.