ID   HYDA_RHIRD              Reviewed;         457 AA.
AC   Q44184;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=D-hydantoinase;
DE            EC=3.5.2.-;
GN   Name=hyuA;
OS   Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium
OS   radiobacter).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=358;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BCRC 13814 / CECT 4067 / NRRL B-11291;
RA   Grifantini R.;
RL   Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the stereospecific hydrolysis of the cyclic amide
CC       bond of D-hydantoin derivatives. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q55DL0};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q55DL0};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- PTM: Carboxylation allows a single lysine to coordinate two zinc ions.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Hydantoinase/dihydropyrimidinase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X91070; CAA62549.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q44184; -.
DR   SMR; Q44184; -.
DR   BRENDA; 3.5.2.2; 200.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd01314; D-HYD; 1.
DR   Gene3D; 2.30.40.10; -; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011778; Hydantoinase/dihydroPyrase.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR011612; Urease_alpha_N_dom.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   Pfam; PF00449; Urease_alpha; 1.
DR   SUPFAM; SSF51338; SSF51338; 2.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR02033; D-hydantoinase; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Phosphoprotein; Zinc.
FT   CHAIN           1..457
FT                   /note="D-hydantoinase"
FT                   /id="PRO_0000165932"
FT   BINDING         57
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P903"
FT   BINDING         59
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P903"
FT   BINDING         148
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P903"
FT   BINDING         148
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P903"
FT   BINDING         153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P903"
FT   BINDING         181
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P903"
FT   BINDING         237
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P903"
FT   BINDING         286
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         313
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P903"
FT   BINDING         335
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P903"
FT   MOD_RES         69
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14117"
FT   MOD_RES         148
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P903"
SQ   SEQUENCE   457 AA;  49940 MW;  9BC8EE0A86914A5B CRC64;
     MDIIIKNGTI VTADGISPAD LGIKDGKIAQ IGGTFGPAGR TIDASGRYVF PGGIDVHTHV
     ETVSFNTQSA DTFATATVAA ACGGTTTIVD FCQQDRGHSL REAVAKWDGM AGGKSAIDYG
     YHIIVLDPTD SVIEELEVLP DLGITSFKVF MAYRGMNMID DVTLLRTLDK AAKTGSLVMV
     HAENGDAADY LRDKFVADGK TAPIYHALSR PPRVEAEATA RALALAEIVN APIYIVHLTC
     EESFDELMRA KARGVHALAE TCTQYLYLTK DDLERPDFEG AKYVFTPPPR TKKDQEILWN
     ALRNGVLETV SSDHCSWLFE GHKDRGRNDF RAIPNGAPGV EERLMMVYQG VNEGRISLTQ
     FVELVATRPA KVFGMFPEKG TVAVGSDADI VLWDPEAEMV IEQSAMHNAM DYSSYEGHKI
     KGVPKTVLLR GKVIVDEGTY VGAPTDGQFR KRRKYKQ