The domain within your query sequence starts at position 70 and ends at position 493; the E-value for the GDC-P domain shown below is 1.1e-202.

RRHIGPGDKDRREMLQALGLASIDELIEKTVPASIRLKRPLKMEDPICENEILETLHAIA
SKNQIWRSYIGMGYYNCSVPQTILRNLLENSGWVTQYTPYQPEVSQGRLESLLNYQTMVS
DITGLDMANASLLDEATAAAEAMQLCHRHNKRKKFFVDPRCHPQTIAVVQTRAKYRGVLV
ELKLPHEMDFSGKDVCGVLFQYPDTEGKVEDFTELVDRAHQTGSLTCCATDLLALCILRP
PGEFGVDIALGNSQRFGVPLGYGGPHAAFFAVKENLVRMMPGRMVGVTRDATGKEVYRLA
LQTREQHIRRDKATSNICTAQALLANMAAMFAIYHGSQGLKHIAKRVHNATLILSEGLKR
AGHQLQHDLFFDTLKVQCGCSVKEVLGRAAQRQINFRLFDDGTLGISLDETVTEKDLDDL
LWIF

GDC-P

GDC-P
PFAM accession number:PF02347
Interpro abstract (IPR020581):

The P protein is part of the glycine decarboxylase multienzyme complex (GDC), also annotated as glycine cleavage system or glycine synthase. GDC consists of four proteins P, H, L and T [(PUBMED:8181752)]. The P protein (EC 1.4.4.2) binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor, carbon dioxide is released and the remaining methylamin moiety is then transferred to the lipoamide cofactor of the H protein. The reaction catalysed by this protein is:

Glycine + lipoylprotein = S-aminomethyldihydrolipoylprotein + CO2

The subunit composition of glycine cleavage system P proteins have been classified into two types. Those from eukaryotes and some of the P proteins from prokaryotes (e.g. Escherichia coli) are in the homodimeric form. The rest of those from prokaryotes are heterotetrameric, with two different subunits which, based on sequence similarities, correspond respectively to the N and C-terminal halves of the eukaryotic subunit [(PUBMED:15791207)].

GO process:oxidation-reduction process (GO:0055114), glycine catabolic process (GO:0006546)
GO function:glycine dehydrogenase (decarboxylating) activity (GO:0004375)

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