ID   L2EMG9_9BURK            Unreviewed;       486 AA.
AC   L2EMG9;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=N-acyl-D-amino-acid deacylase {ECO:0000313|EMBL:ELA00566.1};
GN   ORFNames=D769_04714 {ECO:0000313|EMBL:ELA00566.1};
OS   Cupriavidus sp. HMR-1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=1249621 {ECO:0000313|EMBL:ELA00566.1, ECO:0000313|Proteomes:UP000010442};
RN   [1] {ECO:0000313|EMBL:ELA00566.1, ECO:0000313|Proteomes:UP000010442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMR-1 {ECO:0000313|EMBL:ELA00566.1,
RC   ECO:0000313|Proteomes:UP000010442};
RX   PubMed=23409271;
RA   Li L.G., Cai L., Zhang T.;
RT   "Genome of Cupriavidus sp. HMR-1, a Heavy Metal-Resistant Bacterium.";
RL   Genome Announc. 1:E00202-E00212(2013).
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:ELA00566.1}.
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DR   EMBL; ANKP01000033; ELA00566.1; -; Genomic_DNA.
DR   RefSeq; WP_008642547.1; NZ_ANKP01000033.1.
DR   AlphaFoldDB; L2EMG9; -.
DR   PATRIC; fig|1249621.3.peg.933; -.
DR   Proteomes; UP000010442; Unassembled WGS sequence.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR   CDD; cd01297; D-aminoacylase; 1.
DR   Gene3D; 3.30.1490.130; D-aminoacylase. Domain 3; 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; IPR013108; Amidohydro_3.
DR   InterPro; IPR023100; D-aminoacylase_insert_dom_sf.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR11647:SF99; D-PHENYLHYDANTOINASE-RELATED; 1.
DR   PANTHER; PTHR11647; HYDRANTOINASE/DIHYDROPYRIMIDINASE FAMILY MEMBER; 1.
DR   Pfam; PF07969; Amidohydro_3; 2.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   4: Predicted;
FT   DOMAIN          52..243
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
FT   DOMAIN          353..465
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   486 AA;  52330 MW;  F00DB2CE75CB4AE5 CRC64;
     MAEQASNHHD LLIRGGTVID GSKAPRFTAD IAVRDGRIAA VGDLAGHTAE HTLDATGRIV
     APGFIDSHTH DDQAVLSQAA MPFKISQGVT TVVAGNCGIS AAPLRADMDL PMPLGLIDAP
     PEGRFTTFAA YLDALRATPS SVNVAAMVGH STLRAVTMSA LDRPANDDEI AAMQALVEEA
     MQAGAIGMST GTFYPPAIKA TTEEIIEVCR PLSARKALYV THMRNESDQV MEALEETFQI
     GRALDVPVVV SHHKVQNTPN FGRSRVTLPF IQETMQHQCV SLDCYPYTAG STMIRTEPAM
     LEGRVRIASS VPHPECTGRD LDDIAREWGV AKQEAARRLQ PGTAIYFLMD EADVQRILAF
     DETMIGSDGI PVGENPHPRL WGTFPRVLGH YCREVGLFPL ETAVWKMTGL TARNFGLHGR
     GTLAVGNHAD IVVFDAGTIR DAADYDTPTR PAEGIDTVIV NGAITWHGGQ HTGARNGQVI
     RRRHAA
//