The domain within your query sequence starts at position 231 and ends at position 531; the E-value for the Hydantoinase_A domain shown below is 6.6e-102.

RGHTACADAYLTPTIQRYVQGFRRGFQGQLKNVQVLFMRSDGGLAPMDAFSGSRAVLSGP
AGGVVGYSTTTYQLEGGQPVIGFDMGGTSTDVSRYAGEFEHVFEASTAGVTLQAPQLDIN
TVAAGGGSRLFFRSGLFVVGPESAGAHPGPACYRKGGPVTVTDANLVLGRLLPASFPCIF
GPGEDQPLSPEASRKALEAVAMEVNSFLASGPCPASQLSLEEVAMGFVRVANEAMCRPIR
ALTQARGHDPSAHVLACFGGAGGQHACAIARALGMDTVHIHRHSGLLSALGLALADVVHE
A

Hydantoinase_A

 Hydantoinase_A
PFAM accession number:PF01968
Interpro abstract (IPR002821):

This domain is found in the enzymes hydantoinase A (HyuA) and oxoprolinase ( EC 3.5.2.9 ). Both enzymes catalyse reactions involving the hydrolysis of 5-membered rings via hydrolysis of their internal imide bonds [ (PUBMED:8943290) ]. This domain is also found in (4-{4-[2-(gamma-L-glutamylamino)ethyl]phenoxymethyl}furan-2-yl)methanamine synthase from Methanocaldococcus jannaschii which is involved in methanofuran biosynthesis, catalyzing the condensation between 5-(aminomethyl)-3-furanmethanol diphosphate and gamma-glutamyltyramine to produce 4-[N-(gamma-L-glutamyl)-p-(beta-aminoethyl)phenoxymethyl]-(aminomethyl)furan (APMF-Glu) [ (PUBMED:26100040) ]. D-5-(2-methylthioethyl)hydantoin amidohydrolase (HyuA) from Pseudomonas is a component of the hydantoinase process, an enzymatic cascade converting D-5-(2-methylthioethyl)hydantoin to N-carbamoyl-D-methionine [ (PUBMED:1732229) ].

GO function:hydrolase activity (GO:0016787)

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