ID   A0A1I5X9S0_9RHOB        Unreviewed;       486 AA.
AC   A0A1I5X9S0;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Dihydropyrimidinase {ECO:0000313|EMBL:SFQ28729.1};
GN   ORFNames=SAMN05421853_103247 {ECO:0000313|EMBL:SFQ28729.1};
OS   Roseivivax halotolerans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseivivax.
OX   NCBI_TaxID=93684 {ECO:0000313|EMBL:SFQ28729.1, ECO:0000313|Proteomes:UP000243106};
RN   [1] {ECO:0000313|Proteomes:UP000243106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10271 {ECO:0000313|Proteomes:UP000243106};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FOXV01000003; SFQ28729.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5X9S0; -.
DR   STRING; 93684.SAMN05421853_103247; -.
DR   Proteomes; UP000243106; Unassembled WGS sequence.
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   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; 2.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000243106}.
FT   DOMAIN          47..433
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   MOD_RES         147
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611778-50"
SQ   SEQUENCE   486 AA;  53496 MW;  026BEB9FF29129C5 CRC64;
     MTKVIKNGTI VTADRTWKAD ILIEGETIKQ IGEDLKGDEY IDAEGAYVIP GGIDPHTHLE
     MPFMGTTAAE TFETGTWAAA CGGTTMLVDF CLPGADGSIK NAINEWHRKS APQICSDIGY
     HMAVTGWNET IFDEMKDAVD MGVNSFKHFM AYKGALMIED DEMFASFKRC KELGALPMVH
     AENGDLVADM QQQMLEQGIT GPEGHAYSRP PEFEGEAANR AITIADAAGV PLYIVHVSCE
     QAHEAIRRAR QKGMRVYGEP LAQFLTLDES EYFNKDWDHA ARRVMSPPFR NKEHQDSLWA
     GLQAGSLQVV ATDHAAFSTE QKRMGVGDFT KIPNGSNGLE ERLGVLWTEG VETGRLTMNE
     FVAVTSSNVA KILNIYPKKG AIVEGADADI VVWDPSITKT ISASNHHSIL DYNVFEGFEV
     KAQPRYTISR GEVIWAWGQN SQPQPGRGRF VPRPAFPSAH TALSKWKALT APKQIHRDPM
     NIPAGI
//