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 22.214.171.124) (ODC). ODC catalyzes the
transformation of ornithine into putrescine.
Prokaryotic diaminopimelic acid decarboxylase (EC 126.96.36.199) (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 188.8.131.52)
(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Unpublished observations (1993).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.
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