InterPro domain: IPR022644

These enzymes are collectively known as group IV decarboxylases [ 1 ].Pyridoxal-dependent decarboxylases acting on ornithine, lysine, arginine andrelated substrates can be classified into two different families on the basisof sequence similarities [ 2 , 3 ].Members of this family while most probably evolutionary related, do not shareextensive regions of sequence similarities. The proteins contain a conserved lysineresidue which is known, in mouse ODC [ 3 ], to be the site of attachment of thepyridoxal-phosphate group. The proteins also contain a stretch of threeconsecutive glycine residues and has been proposed to be part of a substrate-binding region [ 4 ].

1. Multiple evolutionary origin of pyridoxal-5'-phosphate-dependent amino acid decarboxylases. Eur. J. Biochem. 221, 997-1002
2. Pseudomonas aeruginosa diaminopimelate decarboxylase: evolutionary relationship with other amino acid decarboxylases. Mol. Biol. Evol. 5, 549-59
3. 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, 150-8
4. Nucleotide sequence and analysis of the speA gene encoding biosynthetic arginine decarboxylase in Escherichia coli. J. Bacteriol. 172, 4631-40