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Three different enzymes - all pyridoxal-dependent decarboxylases - seem to share regions of sequence similarity [1,2,3,4], especially in the vicinity of the lysine residue which serves as the attachment site for the pyridoxal-phosphate (PLP) group. These enzymes are:

• Glutamate decarboxylase (EC 4.1.1.15) (GAD). Catalyzes the decarboxylation of glutamate into the neurotransmitter GABA (4-aminobutanoate).
• Histidine decarboxylase (EC 4.1.1.22) (HDC). Catalyzes the decarboxylation of histidine to histamine. There are two completely unrelated types of HDC: those that use PLP as a cofactor (found in Gram-negative bacteria and mammals), and those that contain a covalently bound pyruvoyl residue (found in Gram-positive bacteria).
• Aromatic-L-amino-acid decarboxylase (EC 4.1.1.28) (DDC), also known as L-dopa decarboxylase or tryptophan decarboxylase. DDC catalyzes the decarboxylation of tryptophan to tryptamine. It also acts on 5-hydroxy- tryptophan and dihydroxyphenylalanine (L-dopa).
• Tyrosine decarboxylase (EC 4.1.1.25) (TyrDC) which converts tyrosine into tyramine, a precursor of isoquinoline alkaloids and various amides.
• Cysteine sulfinic acid decarboxylase (EC 4.1.1.29).
• L-2,4-diaminobutyrate decarboxylase (EC 4.1.1.-) (DABA decarboxylase).

These enzymes are collectively known as group II decarboxylases [3,4].

April 2006 / Pattern revised.

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

DDC_GAD_HDC_YDC, PS00392; DDC / GAD / HDC / TyrDC pyridoxal-phosphate attachment site  (PATTERN)

Consensus pattern: S-[LIVMFYW]-x-{KG}-x(3)-K-[LIVMFYWGH]-[LIVMFYWG]-x-{R}-x-[LIVMFYW]-{V}-[CA]-x(2)-[LIVMFYWQ]-{K}-x-[RK] K is the pyridoxal-P attachment site Sequences known to belong to this class detected by the pattern: ALL, except for a probable Caenorhabditis elegans DDC and for Petunia GAD Other sequence(s) detected in Swiss-Prot: 5

• Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00392 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00392 • Scan Swiss-Prot/TrEMBL entries against PS00392 • view ligand binding statistics

Matching PDB structures: 1JS3 1JS6 1PMM 1PMO ... [ALL]

1	Authors	Jackson F.R.
	Title	Prokaryotic and eukaryotic pyridoxal-dependent decarboxylases are homologous.
	Source	J. Mol. Evol. 31:325-329(1990).
	PubMed ID	2124279

2	Authors	Joseph D.R., Sullivan P.M., Wang Y.-M., Kozak C., Fenstermacher D.A., Behrendsen M.E., Zahnow C.A.
	Title	Characterization and expression of the complementary DNA encoding rat histidine decarboxylase.
	Source	Proc. Natl. Acad. Sci. U.S.A. 87:733-737(1990).
	PubMed ID	2300558

3	Authors	Sandmeier E., Hale T.I., Christen P.
	Title	Multiple evolutionary origin of pyridoxal-5'-phosphate-dependent amino acid decarboxylases.
	Source	Eur. J. Biochem. 221:997-1002(1994).
	PubMed ID	8181483

4	Authors	Ishii S., Mizuguchi H., Nishino J., Hayashi H., Kagamiyama H.
	Title	Functionally important residues of aromatic L-amino acid decarboxylase probed by sequence alignment and site-directed mutagenesis.
	Source	J. Biochem. 120:369-376(1996).
	PubMed ID	8889823

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