ID   A0A0G1Q615_9BACT        Unreviewed;       526 AA.
AC   A0A0G1Q615;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=N-acyl-D-amino-acid deacylase {ECO:0000313|EMBL:KKU40282.1};
GN   ORFNames=UX55_C0010G0004 {ECO:0000313|EMBL:KKU40282.1};
OS   Candidatus Azambacteria bacterium GW2011_GWE2_46_45.
OC   Bacteria; Candidatus Azambacteria.
OX   NCBI_TaxID=1618625 {ECO:0000313|EMBL:KKU40282.1, ECO:0000313|Proteomes:UP000034202};
RN   [1] {ECO:0000313|EMBL:KKU40282.1, ECO:0000313|Proteomes:UP000034202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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:KKU40282.1}.
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DR   EMBL; LCMQ01000010; KKU40282.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1Q615; -.
DR   PATRIC; fig|1618625.3.peg.164; -.
DR   Proteomes; UP000034202; 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          45..207
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
FT   DOMAIN          421..507
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   526 AA;  58116 MW;  BBC04883F9E093EC CRC64;
     MAFDILIKNG TLIDGTGRER YPADVGINKN AIAEIGDLKN QKAEKVIDAA NLHVVPGFID
     VLNHSDTYWT MFPMPSMESL LRQGITTIIG GNCGASLAPL VEGNVIAAIQ KWADMSEVSI
     NWLRMSEFLE QLERMKFGVN FGTLVGHGTL RRGLIKDEVR NLTGDEMAKI KFMLEEALES
     GAFGLSTGLA FSHAKTTPVE EIIELAKLVE KYDGVYASHL RDEAGRLDDS VTETIRVAME
     SQAKIQISHF KAMGQSGWPN FAANLERLEQ AHDGGLNVNF DVFPYTVTGS VLYTLLPDWA
     AEGGKKKLLS RLRDPHERRK IIHELKKNPL AEYDKIIVAI SPADKTFIGK SLKEIAQNQG
     VEPEEALLNM ILVAEDQLIA FIHSLSEENV AAGIASKISM VSSDGSGYNL GYARKGILVH
     PRSFGAFPRL LGKYVREEKK LSWEEAVRKI SSLPAEKYGL KKRGLITESN FADLTIYNPE
     TVSDLATFKN PYLYPRGVEY VIVNGKTAIE KGVYNGELAG RVLRKS
//