PROSITE documentation PDOC00685
Orn/DAP/Arg decarboxylases family 2 signatures


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 (ODC). ODC catalyzes the transformation of ornithine into putrescine.
  • Prokaryotic diaminopimelic acid decarboxylase (EC (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 (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 [4], 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 [5].

These enzymes are collectively known as group IV decarboxylases [3].

Last update:

April 2006 / Pattern revised.


Technical section

PROSITE methods (with tools and information) covered by this documentation:

ODR_DC_2_1, PS00878; Orn/DAP/Arg decarboxylases family 2 pyridoxal-P attachment site  (PATTERN)

ODR_DC_2_2, PS00879; Orn/DAP/Arg decarboxylases family 2 signature 2  (PATTERN)


1AuthorsBairoch A.
SourceUnpublished observations (1993).

2AuthorsMartin C. Cami B. Yeh P. Stragier P. Parsot C. Patte J.-C.
SourceMol. Biol. Evol. 5:549-559(1988).

3AuthorsSandmeier E. Hale T.I. Christen P.
TitleMultiple evolutionary origin of pyridoxal-5'-phosphate-dependent amino acid decarboxylases.
SourceEur. J. Biochem. 221:997-1002(1994).
PubMed ID8181483

4AuthorsPoulin R. Lu L. Ackermann B. Bey P. Pegg A.E.
TitleMechanism of the irreversible inactivation of mouse ornithine decarboxylase by alpha-difluoromethylornithine. Characterization of sequences at the inhibitor and coenzyme binding sites.
SourceJ. Biol. Chem. 267:150-158(1992).
PubMed ID1730582

5AuthorsMoore R.C. Boyle S.M.
TitleNucleotide sequence and analysis of the speA gene encoding biosynthetic arginine decarboxylase in Escherichia coli.
SourceJ. Bacteriol. 172:4631-4640(1990).
PubMed ID2198270

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