ID A0A084ZMS8_9ENTR Unreviewed; 472 AA.
AC A0A084ZMS8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=D-phenylhydantoinase {ECO:0000256|HAMAP-Rule:MF_01644};
DE EC=3.5.2.- {ECO:0000256|HAMAP-Rule:MF_01644};
DE AltName: Full=Hydantoin-utilizing enzyme HyuA {ECO:0000256|HAMAP-Rule:MF_01644};
GN Name=hydA {ECO:0000313|EMBL:KFB98772.1};
GN Synonyms=hyuA {ECO:0000256|HAMAP-Rule:MF_01644};
GN ORFNames=GTGU_04443 {ECO:0000313|EMBL:KFB98772.1};
OS Trabulsiella guamensis ATCC 49490.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Trabulsiella.
OX NCBI_TaxID=1005994 {ECO:0000313|EMBL:KFB98772.1, ECO:0000313|Proteomes:UP000028630};
RN [1] {ECO:0000313|EMBL:KFB98772.1, ECO:0000313|Proteomes:UP000028630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49490 {ECO:0000313|EMBL:KFB98772.1,
RC ECO:0000313|Proteomes:UP000028630};
RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT the evolutionary history of the Enterobacteriaceae.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|HAMAP-Rule:MF_01644}.
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 Evidence={ECO:0000256|HAMAP-Rule:MF_01644};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01644};
CC Note=Binds 2 divalent metal cations per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01644};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01644}.
CC -!- PTM: Carbamylation allows a single lysine to coordinate two divalent
CC metal cations. {ECO:0000256|PIRSR:PIRSR611778-50}.
CC -!- PTM: Carboxylation allows a single lysine to coordinate two divalent
CC metal cations. {ECO:0000256|HAMAP-Rule:MF_01644}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Hydantoinase/dihydropyrimidinase family.
CC {ECO:0000256|ARBA:ARBA00008829, ECO:0000256|HAMAP-Rule:MF_01644}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFB98772.1}.
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DR EMBL; JMTB01000121; KFB98772.1; -; Genomic_DNA.
DR RefSeq; WP_038162644.1; NZ_JMTB01000121.1.
DR AlphaFoldDB; A0A084ZMS8; -.
DR eggNOG; COG0044; Bacteria.
DR OrthoDB; 5687299at2; -.
DR Proteomes; UP000028630; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016812; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006208; P:pyrimidine nucleobase catabolic process; IEA:InterPro.
DR CDD; cd01314; D-HYD; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR HAMAP; MF_01644; D_hydantoinase; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR023766; D_phenylhydantoinase.
DR InterPro; IPR011778; Hydantoinase/dihydroPyrase.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR NCBIfam; TIGR02033; D-hydantoinase; 1.
DR PANTHER; PTHR11647:SF99; D-PHENYLHYDANTOINASE-RELATED; 1.
DR PANTHER; PTHR11647; HYDRANTOINASE/DIHYDROPYRIMIDINASE FAMILY MEMBER; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 2.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01644, ECO:0000313|EMBL:KFB98772.1};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01644}.
FT DOMAIN 50..434
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT BINDING 59
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01644"
FT BINDING 61
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01644"
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 /evidence="ECO:0000256|HAMAP-Rule:MF_01644"
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 /evidence="ECO:0000256|HAMAP-Rule:MF_01644"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01644"
FT BINDING 182
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01644"
FT BINDING 239
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01644"
FT BINDING 286
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01644"
FT BINDING 313
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01644"
FT BINDING 335
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01644"
FT MOD_RES 151
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01644,
FT ECO:0000256|PIRSR:PIRSR611778-50"
SQ SEQUENCE 472 AA; 51719 MW; 1666CA033314793C CRC64;
MRVLIKNGTV VNADGKAKQD LLIESGIIRQ IADHISPELP CEVIDADGCY VMPGGVDVHT
HFNIDTGMAR SCDDFFTGTR AAACGGTTTI IDHMGFGPAG CRLHHQLEVY HGYAAHKAVI
DYSFHGVIQH INHAILDEIP MMVDAGISSF KLYLTYQYKL NDDEVLQALR HLHQAGALTT
VHPENDAVIH RKRLEFLAAG KTAPKYHALS RPEECEAEAI ARMINLAKLS GNAPLYIVHL
SNGLGLDYLR LAQARHQPVW VETCPQYLLL DDRCYEREDA LNYLLSPPLR NARNNDALWC
GISDGAVDVV ATDHCTFSHA QRQQLSGGDF SRCPNGLPGV ENRLLLLFSH GVMSGRISPE
RFVALTSATP AKLFGLWPQK GLLAPGADGD IVIIDPRQRT TIRHAELHDN ADYSPWEGFA
CQGAIRQTLS HGRVIYNDGV FSGVAGQGRF LRRKPFSAPT SPVDGSVSPL GQ
//
