The domain within your query sequence starts at position 166 and ends at position 310; the E-value for the Pyridoxal_deC domain shown below is 2.6e-12.

FNVLYNKKPVIYLSAAARPGLGQYLCNQLGLPFPCLCRVPCNTMFGSQHQMDVAFLEKLI
KDDVERGRLPLLLVANAGTAAVGHTDKIGRLKELCEQYGIWLHVEGVNLATLALGYVSSS
VLAATKCDSMTLTPGLWLGLPAVPA

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)]; and L-aspartate decarboxylase, which converts aspartate to beta-alanine [(PUBMED:24415726)]. These enzymes belong to the group II decarboxylases [(PUBMED:8181483), (PUBMED:8889823)].
GO process:carboxylic acid metabolic process (GO:0019752)
GO function:carboxy-lyase activity (GO:0016831), pyridoxal phosphate binding (GO:0030170)

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