The domain within your query sequence starts at position 58 and ends at position 426; the E-value for the Pyridoxal_deC domain shown below is 2.8e-112.

PEQLRQLLDLEMRDTGESQDKLLKLCQDVIHFSVKTNHPRFFNQLYAGLDYYSLAARIIT
EALNPSIYTYEVSPVFLLVEEAVLKKMIECVGWKEGDGIFNPGGSVSNMCAMNLARYRHC
PDIKEKGLSGLPRLILFTSAECHYSMKKAASFLGIGTQNVYFVETDGRGKMIPEDLEKQI
WQARQEGAVPFLVCATSGTTVLGAFDPLDEIAEVCERHGLWLHVDASWGGSALVSRKHRR
LLHGIHRADSVAWNPHKMLMAGIQCSALLVKDKSDLLKKCYSAKATYLFQQDKFYDVSYD
TGDKSIQCSRRPDAFKFWMTWKALGTSGLEERVNRAFALSRYLVDEIKKREGFKLLMEPE
YTNVCFWYI

Pyridoxal_deC

Pyridoxal_deC
PFAM accession number:PF00282
Interpro abstract (IPR002129):

Pyridoxal phosphate is the active form of vitamin B6 (pyridoxine or pyridoxal). Pyridoxal 5'-phosphate (PLP) is a versatile catalyst, acting as a coenzyme in a multitude of reactions, including decarboxylation, deamination and transamination [ (PUBMED:8690703) (PUBMED:7748903) (PUBMED:15189147) ]. PLP-dependent enzymes are primarily involved in the biosynthesis of amino acids and amino acid-derived metabolites, but they are also found in the biosynthetic pathways of amino sugars and in the synthesis or catabolism of neurotransmitters; pyridoxal phosphate can also inhibit DNA polymerases and several steroid receptors [ (PUBMED:17109392) ]. Inadequate levels of pyridoxal phosphate in the brain can cause neurological dysfunction, particularly epilepsy [ (PUBMED:16763894) ].

PLP enzymes exist in their resting state as a Schiff base, the aldehyde group of PLP forming a linkage with the epsilon-amino group of an active site lysine residue on the enzyme. The alpha-amino group of the substrate displaces the lysine epsilon-amino group, in the process forming a new aldimine with the substrate. This aldimine is the common central intermediate for all PLP-catalysed reactions, enzymatic and non-enzymatic [ (PUBMED:15581583) ].

A number of pyridoxal-dependent decarboxylases share regions of sequence similarity, particularly in the vicinity of a conserved lysine residue, which provides the attachment site for the pyridoxal-phosphate (PLP) group [ (PUBMED:8181483) (PUBMED:2124279) ]. Among these enzymes are aromatic-L-amino-acid decarboxylase (L-dopa decarboxylase or tryptophan decarboxylase), which catalyses the decarboxylation of tryptophan to tryptamine [ (PUBMED:8889823) ]; tyrosine decarboxylase, which converts tyrosine into tyramine; histidine decarboxylase, which catalyses the decarboxylation of histidine to histamine [ (PUBMED:2300558) ]; L-aspartate decarboxylase, which converts aspartate to beta-alanine [ (PUBMED:24415726) ]; and phenylacetaldehyde synthase that catalyses the decarboxylation of L-phenylalanine to 2-phenylethylamine [ (PUBMED:16766535) ]. These enzymes belong to the group II decarboxylases [ (PUBMED:8181483) (PUBMED:8889823) ].

GO process:carboxylic acid metabolic process (GO:0019752)
GO function:pyridoxal phosphate binding (GO:0030170), carboxy-lyase activity (GO:0016831)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Pyridoxal_deC