ID   A0A2W7RIW9_9BACT        Unreviewed;       525 AA.
AC   A0A2W7RIW9;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   SubName: Full=N-acyl-D-amino-acid deacylase {ECO:0000313|EMBL:PZX60808.1};
GN   ORFNames=LX80_02292 {ECO:0000313|EMBL:PZX60808.1};
OS   Hydrotalea sandarakina.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Hydrotalea.
OX   NCBI_TaxID=1004304 {ECO:0000313|EMBL:PZX60808.1, ECO:0000313|Proteomes:UP000249720};
RN   [1] {ECO:0000313|EMBL:PZX60808.1, ECO:0000313|Proteomes:UP000249720}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23241 {ECO:0000313|EMBL:PZX60808.1,
RC   ECO:0000313|Proteomes:UP000249720};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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:PZX60808.1}.
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DR   EMBL; QKZV01000008; PZX60808.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2W7RIW9; -.
DR   OrthoDB; 9775607at2; -.
DR   Proteomes; UP000249720; 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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000249720};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..525
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015997736"
FT   DOMAIN          63..239
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
FT   DOMAIN          427..502
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   525 AA;  57606 MW;  B5BF16A06E86745F CRC64;
     MRTLFCCLYV LFSLTLNAQT ADILIKNGKI MNGTGNNWFY GDVAIANGKI LAVGQLTGWK
     AHQTIDASGL IVSPGFIDVH THIEGDEARN PTADNFIYDG VTTVITGNCG LSKTDMGAYF
     HFLDSVHLST NVASLIGHND IRKAVMGTAR RAPTPQEMQQ MEKIMQKAMQ DGAVGLSTGL
     IYIPGAYANT NEVVALAKIA AAYNGVYATH MRNEGDSVVP AIKEALYIGE TAGLPVEISH
     FKLSGQQNWG RSKETLALIK DARRNGIDVT IDQYPYTASS TNLGTLLPDW VLADGKDSIN
     ARLSNAAIRK QCIDYMLERL HKRKLKHFSY PVVAYYNFDT TLNGKSIEAI NVLKGRKHTA
     KAEAETVLEM MQHGGAAMVF HGMSEGDVQY IMQYPFCMFG CDAGIRVFGE GVPHPRGYGS
     NAKILGKYVR ELHLFSWEEA IRRMTGLPAQ KFHLYNRGLL LPGYAADVVV FNPNTIIDKA
     TYDSPHQYSE GVQYVIVNGA VTLQNGKHTG VRNGVTLKNN TLQNL
//