ID   A4EGA4_9RHOB            Unreviewed;       484 AA.
AC   A4EGA4;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Dihydropyrimidinase {ECO:0000313|EMBL:EBA13926.1};
GN   ORFNames=RCCS2_08554 {ECO:0000313|EMBL:EBA13926.1};
OS   Roseobacter sp. CCS2.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseobacter.
OX   NCBI_TaxID=391593 {ECO:0000313|EMBL:EBA13926.1, ECO:0000313|Proteomes:UP000003535};
RN   [1] {ECO:0000313|EMBL:EBA13926.1, ECO:0000313|Proteomes:UP000003535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCS2 {ECO:0000313|EMBL:EBA13926.1,
RC   ECO:0000313|Proteomes:UP000003535};
RA   Mary Ann M.A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (MAR-2007) 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}.
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:EBA13926.1}.
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DR   EMBL; AAYB01000001; EBA13926.1; -; Genomic_DNA.
DR   RefSeq; WP_008231976.1; NZ_AAYB01000001.1.
DR   AlphaFoldDB; A4EGA4; -.
DR   eggNOG; COG0044; Bacteria.
DR   OrthoDB; 9775759at2; -.
DR   Proteomes; UP000003535; 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;
FT   DOMAIN          47..420
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   484 AA;  53071 MW;  E7D56323FF059AF4 CRC64;
     MTKVIKNGTI VTHDLTYNAD VLIDGGKIIE IGQNLSGDEQ LDATDCYVMP GGIDPHVHLE
     MPFMGTYSSD DFESGTRAGL AGGTTMVVDF CLPNQGESLL DAIKRWDNKS TRANCDYSFH
     MAVTWWGEQV FNDMETVVND RGINTFKHFL AYKGALMVND DELFSSFNRL SELGAIAMVH
     AENGDVVAEM TAKLLAEGNT GPEAHAYSRP SQVEGEATNR AIMIADMAGV PLYVVHTSCE
     ESHEAIRRAR QQGKRVWGEP LIQHLTLDES EYFNKDWDHA ARRVMSPPFR NKQHQDSLWA
     GLQSGSLSVV ATDHCAFTTE QKRTGVGDFS KIPNGTGGLE DRMPMLWTHG VETGRLTPNE
     FVAVTSTNIA KILNCYPNKG AVMVGADADL VVWDPAKTKT ITAGSQQSAI DYNVFEGKEV
     KGLPRFTLTR GHVAIHDGDV RTQEGHGKFV KREANTPVNK ALSSWKELTA PQPVQRTGIP
     ATGV
//