1. MARTIN, C., CAMI, B., YEH, P., STRAGIER, P., PARSOT, C. AND PATTE, J.-C.
Pseudomonas aeruginosa diaminopimelate decarboxylase: evolutionary
relationship with other amino acid decarboxylases.
MOL.BIOL.EVOL. 5 549-559 (1988).
2. SANDMEIER, E., HALE, T.I. AND CHRISTEN, P.
Multiple evolutionary origin of pyridoxal-5'-phosphate-dependent amino acid
EUR.J.BIOCHEMISTRY 221 997-1002 (1994).
3. POULIN, R., LU, L., ACKERMANN, B., BEY, P. AND PEGG, A.E.
Mechanism of the irreversible inactivation of mouse ornithine decarboxylase
by alpha-difluoromethylornithine. Characterization of sequences at the
inhibitor and coenzyme binding sites.
J.BIOL.CHEM. 267 150-158 (1992).
Pyridoxal-dependent decarboxylases that act on ornithine-, lysine-,
arginine- and related substrates can be classified into different families
on the basis of sequence similarity [1,2]. One of these families includes:
eukaryotic ornithine decarboxylase (ODC), which catalyses the transformation
of ornithine into putrescine; prokaryotic diaminopimelic acid decarboxylase
(DAPDC), which catalyses the conversion of diaminopimelic acid into lysine,
the final step of lysine biosynthesis; Pseudomonas syringae pv. tabaci
protein, tabA, which is probably involved in tabtoxin biosynthesis and
is similar to DAPDC; and bacterial and plant biosynthetic arginine
decarboxylase (ADC), which catalyses the transformation of arginine
into agmatine, the first step in putrescine synthesis from arginine.
Although these proteins, which are known collectively as group IV
decarboxylases , probably share a common evolutionary origin, their
levels of sequence similarity are low, being confined to a few short
ODADCRBXLASE is a 5-element fingerprint that provides a signature for
group IV decarboxylases. The fingerprint was derived from an initial
alignment of 15 sequences: the motifs were drawn from short conserved
regions spanning virtually the full alignment length - motif 1 spans the
region encoded by PROSITE pattern ODR_DC_2_1 (PS00878), which includes a
conserved lysine residue that is the pyridoxal-P attachment site in mouse
ODC . Five iterations on SPTR37_10f were required to reach convergence,
at which point a true set comprising 64 sequences was identified. Several
partial matches were also found, all of which are group IV decarboxylases
and homologues that fail to match one or more motifs.