{PDOC00585}
{PS00703; OKR_DC_1}
{BEGIN}
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* Orn/Lys/Arg decarboxylases family 1 pyridoxal-phosphate attachment site *
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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 4.1.1.17) (ODC). ODC catalyzes the
   transformation of ornithine into putrescine.
 - Prokaryotic  lysine  decarboxylase  (EC 4.1.1.18) (LDC).  LDC catalyzes the
   transformation of lysine into cadaverine.
 - Escherichia coli biodegradative arginine decarboxylase (EC 4.1.1.19) (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].

-Consensus pattern: [STAV]-x-S-x-H-K-x(2)-[GSTAN](2)-x-[STA]-Q-[STA](2)
                    [K is the pyridoxal-P attachment site]
-Sequences known to belong to this class detected by the pattern: ALL,  except
 for yaaO.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: November 1997 / Text revised.

[ 1] Bairoch A.
     Unpublished observations (1993).
[ 2] Sandmeier E., Hale T.I., Christen P.
     Eur. J. Biochem. 221:997-1002(1994).
[ 3] Meng S.-Y., Bennett G.N.
     "Nucleotide sequence of the Escherichia coli cad operon: a system for
     neutralization of low extracellular pH."
     J. Bacteriol. 174:2659-2669(1992).
     PubMed=1556085
[ 4] Stim K.P., Bennett G.N.
     "Nucleotide sequence of the adi gene, which encodes the biodegradative
     acid-induced arginine decarboxylase of Escherichia coli."
     J. Bacteriol. 175:1221-1234(1993).
     PubMed=8383109
{END}