PROSITE documentation PDOC00585
Orn/Lys/Arg decarboxylases family 1 pyridoxal-phosphate attachment site


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]. The first family consists of:

  • Prokaryotic ornithine decarboxylase (EC (ODC). ODC catalyzes the transformation of ornithine into putrescine.
  • Prokaryotic lysine decarboxylase (EC (LDC). LDC catalyzes the transformation of lysine into cadaverine.
  • Escherichia coli biodegradative arginine decarboxylase (EC (ADC). ADC catalyzes the transformation of arginine into agmatine.
  • Bacillus subtilis hypothetical protein yaaO.

One of the regions of sequence similarity contains a conserved lysine residue which is known, in Escherichia coli LDC [3] and in ADC [4], to be the site of attachment of the pyridoxal-phosphate group. We have used this region as a signature pattern.

These enzymes are collectively known as group III decarboxylases [2].

Last update:

November 1997 / Text revised.


Technical section

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

OKR_DC_1, PS00703; Orn/Lys/Arg decarboxylases family 1 pyridoxal-P attachment site  (PATTERN)


1AuthorsBairoch A.
SourceUnpublished observations (1993).

2AuthorsSandmeier E. Hale T.I. Christen P.
SourceEur. J. Biochem. 221:997-1002(1994).

3AuthorsMeng S.-Y. Bennett G.N.
TitleNucleotide sequence of the Escherichia coli cad operon: a system for neutralization of low extracellular pH.
SourceJ. Bacteriol. 174:2659-2669(1992).
PubMed ID1556085

4AuthorsStim K.P. Bennett G.N.
TitleNucleotide sequence of the adi gene, which encodes the biodegradative acid-induced arginine decarboxylase of Escherichia coli.
SourceJ. Bacteriol. 175:1221-1234(1993).
PubMed ID8383109

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