AC   MF_01644;
DC   Protein; auto
TR   HAMAP; MF_01644; -; 1; level=0
XX
Names: D_hydantoinase
XX
ID   PHYDA
DE   RecName: Full=D-phenylhydantoinase;
DE            EC=3.5.2.-;
DE   AltName: Full=Hydantoin-utilizing enzyme HyuA;
GN   Name=hyuA;
XX
CC   -!- FUNCTION: Catalyzes the stereospecific hydrolysis of the cyclic amide
CC       bond of D-hydantoin derivatives with an aromatic side chains at the 5'-
CC       position. Has no activity on dihydropyrimidines. The physiological
CC       function is unknown.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-5-phenylhydantoin + H2O = H(+) + N-carbamoyl-D-
CC         phenylglycine; Xref=Rhea:RHEA:51664, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:140750, ChEBI:CHEBI:140758;
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC       Note=Binds 2 divalent metal cations per subunit.;
CC   -!- SUBUNIT: Homotetramer.
CC   -!- PTM: Carboxylation allows a single lysine to coordinate two divalent
CC       metal cations.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Hydantoinase/dihydropyrimidinase family.
XX
DR   Pfam; PF01979; Amidohydro_1; 1; trigger=no
DR   NCBIfam; TIGR02033; D-hydantoinase; 1; trigger=no
XX
KW   Hydrolase
KW   Metal-binding
XX
GO   GO:0016812; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
XX
FT   From: PHYDA_ECOLI (Q46806)
FT   BINDING         59
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT   Condition: H
FT   BINDING         61
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT   Condition: H
FT   BINDING         151
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /note="via carbamate group"
FT   Condition: K
FT   BINDING         151
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /note="via carbamate group"
FT   Condition: K
FT   BINDING         182
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT   Condition: H
FT   BINDING         239
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT   Condition: H
FT   BINDING         313
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT   Condition: D
FT   BINDING         156
FT                   /ligand="substrate"
FT   Condition: Y
FT   BINDING         286
FT                   /ligand="substrate"
FT   Condition: S
FT   BINDING         335
FT                   /ligand="substrate"
FT   Condition: N
FT   MOD_RES         151
FT                   /note="N6-carboxylysine"
FT   Condition: K
XX
Size: 461-461;
Related: None;
Template: Q46806;
Scope:
 Bacteria; Enterobacteriaceae
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.19 2023/06/01
//