To improve security and privacy, we are moving our web pages and services from HTTP to HTTPS. To give users of web services time to transition to HTTPS, we will support separate HTTP and HTTPS services until the end of 2017. From January 2018 most HTTP traffic will be automatically redirected to HTTPS. [more...] View this page in https
Pyridoxal-dependent decarboxylases acting on ornithine, lysine, arginine and
related substrates can be classified into two different families on the basis
of sequence similarities [1,2,3]. The second family consists of:
Eukaryotic ornithine decarboxylase (EC 220.127.116.11) (ODC). ODC catalyzes the
transformation of ornithine into putrescine.
Prokaryotic diaminopimelic acid decarboxylase (EC 18.104.22.168) (DAPDC). DAPDC
catalyzes the conversion of diaminopimelic acid into lysine; the last step
in the biosynthesis of lysine.
Pseudomonas syringae pv. tabaci protein tabA. tabA is probably involved in
the biosynthesis of tabtoxin and is highly similar to DAPDC.
Bacterial and plant biosynthetic arginine decarboxylase (EC 22.214.171.124)
(ADC). ADC catalyzes the transformation of arginine into agmatine, the
first step in the biosynthesis of putrescine from arginine.
The above proteins, while most probably evolutionary related, do not share
extensive regions of sequence similarities. We selected two of the conserved
regions as signature patterns. The first pattern contains a conserved lysine
residue which is known, in mouse ODC , to be the site of attachment of the
pyridoxal-phosphate group. The second pattern contains a stretch of three
consecutive glycine residues and has been proposed to be part of a substrate-binding region .
These enzymes are collectively known as group IV decarboxylases .
April 2006 / Pattern revised.
PROSITE methods (with tools and information) covered by this documentation:
Unpublished observations (1993).
Martin C., Cami B., Yeh P., Stragier P., Parsot C., Patte J.-C.
Mol. Biol. Evol. 5:549-559(1988).
Sandmeier E., Hale T.I., Christen P.
Multiple evolutionary origin of pyridoxal-5'-phosphate-dependent amino acid decarboxylases.
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.