PROSITE documentation PDOC00585

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

Description:

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].

Last update:

November 1997 / Text revised.

Technical section:

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

OKR_DC_1, PS00703Orn/Lys/Arg decarboxylases family 1 pyridoxal-P attachment site  (PATTERN)
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
• Retrieve an alignment of Swiss-Prot true positive hits:
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Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00703
Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00703
Scan Swiss-Prot/TrEMBL entries against PS00703
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Matching PDB structures: 1C4K 1ORD [ALL]

References:

1 AuthorsBairoch A.
SourceUnpublished observations (1993).
2 AuthorsSandmeier E., Hale T.I., Christen P.
SourceEur. J. Biochem. 221:997-1002(1994).
3 AuthorsMeng 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
4 AuthorsStim 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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