ID   Q5WBE6_SHOC1            Unreviewed;       471 AA.
AC   Q5WBE6;
DT   23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   SubName: Full=D-hydantoinase {ECO:0000313|EMBL:BAD66314.1};
DE            EC=3.5.2.2 {ECO:0000313|EMBL:BAD66314.1};
GN   OrderedLocusNames=ABC3783 {ECO:0000313|EMBL:BAD66314.1};
OS   Shouchella clausii (strain KSM-K16) (Alkalihalobacillus clausii).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Shouchella.
OX   NCBI_TaxID=66692 {ECO:0000313|EMBL:BAD66314.1, ECO:0000313|Proteomes:UP000001168};
RN   [1] {ECO:0000313|EMBL:BAD66314.1, ECO:0000313|Proteomes:UP000001168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16 {ECO:0000313|EMBL:BAD66314.1,
RC   ECO:0000313|Proteomes:UP000001168};
RA   Hakamada Y., Kobayashi T., Hitomi J., Kawai S., Ito S.;
RT   "Molecular cloning and nucleotide sequence of the gene for an alkaline
RT   protease from the alkalophilic Bacillus sp. KSM-K16.";
RL   J. Ferment. Bioeng. 78:105-108(1994).
RN   [2] {ECO:0000313|EMBL:BAD66314.1, ECO:0000313|Proteomes:UP000001168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16 {ECO:0000313|EMBL:BAD66314.1,
RC   ECO:0000313|Proteomes:UP000001168};
RX   PubMed=7632397; DOI=10.1007/s002530050437;
RA   Kobayashi T., Hakamada Y., Adachi S., Hitomi J., Yoshimatsu T., Koike K.,
RA   Kawai S., Ito S.;
RT   "Purification and properties of an alkaline protease from alkalophilic
RT   Bacillus sp. KSM-K16.";
RL   Appl. Microbiol. Biotechnol. 43:473-481(1995).
RN   [3] {ECO:0000313|EMBL:BAD66314.1, ECO:0000313|Proteomes:UP000001168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16 {ECO:0000313|EMBL:BAD66314.1,
RC   ECO:0000313|Proteomes:UP000001168};
RX   PubMed=9278275; DOI=10.1093/protein/10.6.627;
RA   Shirai T., Suzuki A., Yamane T., Ashida T., Kobayashi T., Ito S.;
RT   "High-resolution crystal structure of M-protease: phylogeny aided analysis
RT   of the high-alkaline adaptation mechanism.";
RL   Protein Eng. 10:627-634(1997).
RN   [4] {ECO:0000313|Proteomes:UP000001168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16 {ECO:0000313|Proteomes:UP000001168};
RA   Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA   Kawai S., Ito S., Horikoshi K.;
RT   "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT   K16.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:BAD66314.1, ECO:0000313|Proteomes:UP000001168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16 {ECO:0000313|EMBL:BAD66314.1,
RC   ECO:0000313|Proteomes:UP000001168};
RX   PubMed=17429572; DOI=10.1007/s00792-007-0074-1;
RA   Kageyama Y., Takaki Y., Shimamura S., Nishi S., Nogi Y., Uchimura K.,
RA   Kobayashi T., Hitomi J., Ozaki K., Kawai S., Ito S., Horikoshi K.;
RT   "Intragenomic diversity of the V1 regions of 16S rRNA genes in high-
RT   alkaline protease-producing Bacillus clausii spp.";
RL   Extremophiles 11:597-603(2007).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- PTM: Carbamylation allows a single lysine to coordinate two divalent
CC       metal cations. {ECO:0000256|PIRSR:PIRSR611778-50}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Hydantoinase/dihydropyrimidinase family.
CC       {ECO:0000256|ARBA:ARBA00008829}.
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DR   EMBL; AP006627; BAD66314.1; -; Genomic_DNA.
DR   RefSeq; WP_011248617.1; NC_006582.1.
DR   AlphaFoldDB; Q5WBE6; -.
DR   STRING; 66692.ABC3783; -.
DR   KEGG; bcl:ABC3783; -.
DR   eggNOG; COG0044; Bacteria.
DR   HOGENOM; CLU_015572_2_0_9; -.
DR   OrthoDB; 9765462at2; -.
DR   Proteomes; UP000001168; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004157; F:dihydropyrimidinase activity; IEA:UniProtKB-EC.
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   InterPro; IPR006680; Amidohydro-rel.
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; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:BAD66314.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001168}.
FT   DOMAIN          50..437
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   MOD_RES         151
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611778-50"
SQ   SEQUENCE   471 AA;  51287 MW;  3994872272C3241F CRC64;
     MKRLIQNGTI VTASDTYKAD LLIEGETIAQ IGQQLAVQGV DEIIDASGCF VFPGGIDPHT
     HLDMPFGGTV TKDDFETGTI AAAYGGTTTI IDFCLTEKEK PLHTAIEAWH KKAAGKAAID
     YGFHLMIGEI NEAVLNELPA IVSTEGISSF KVFMAYKHVF QADDATLFET LTKAKELGAL
     VMVHAENGDV IDYLTKQALK EGKTAPIYHA LTRPVEAEGE ATGRACQLAS LAQSQLYVVH
     VTCQEAVQQI AEARKQGADI WGETCPQYLV LDESMLRKPG FEGAKYVWSP PLREKQHQDA
     LWKALKTGAL QTIGSDQCSF DFAGQKDLGI NDFTKIPNGG PIIEDRFSLL YSEGVAKGRI
     GLNEFVDLVS TRAAKLFGLY PKKGCIAVGA DADIVLFDPQ AERVLSARTH HLAVDYSAFE
     GMRVKGTPRT VLSRGKVIVR DQTYVGTPGE GAFLKRARYG ELWTNDLVGQ R
//