ID   A0A2S4YRG0_9ACTN        Unreviewed;       537 AA.
AC   A0A2S4YRG0;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=N-acyl-D-amino-acid deacylase {ECO:0000313|EMBL:POX51516.1};
GN   ORFNames=C3489_20000 {ECO:0000313|EMBL:POX51516.1};
OS   Streptomyces sp. Ru71.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2080746 {ECO:0000313|EMBL:POX51516.1, ECO:0000313|Proteomes:UP000237414};
RN   [1] {ECO:0000313|EMBL:POX51516.1, ECO:0000313|Proteomes:UP000237414}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ru71 {ECO:0000313|EMBL:POX51516.1,
RC   ECO:0000313|Proteomes:UP000237414};
RA   Suneja G., Sharma R.;
RT   "Genome sequencing of cellulose degrading bacteria.";
RL   Submitted (FEB-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:POX51516.1}.
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DR   EMBL; PQSS01000032; POX51516.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S4YRG0; -.
DR   OrthoDB; 9766983at2; -.
DR   Proteomes; UP000237414; Unassembled WGS sequence.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   CDD; cd01297; D-aminoacylase; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR013108; Amidohydro_3.
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; 1.
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:UP000237414}.
FT   DOMAIN          54..517
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   537 AA;  58012 MW;  3B00E1B90FD666C7 CRC64;
     MEDLVIRDAD VVDGSGAGSY RADVVIDDGR IVSIVKEAAA AGCQRPSAMR ELGAEGLVLA
     PGFIDMHAHS DLQLLRDPDH SAKAAQGVTL EVLGQDGLSY APVDDRTLEE VRRAIAGWNG
     YGDDIDFDWR SVGEYLDRLD RGIAVNAAYL IPQGTVRALA VGWEDRPATP QELDRMRQLV
     AEGMEQGAVG LSSGLTYTPG MYAEDAELTE LCRVVARYGG YYCPHHRSYG AGALQAYAEM
     VELTRQAGCA LHLAHATMNF GVNKGRAPEL LALLDDALAS GADITLDTYP YTPGCTTLVA
     LLPSWASEGG PEAVLKRLAD DDTAERIRRH LEVEGSDGCH GVPVEWETIE ISGVGDPSLA
     EYVGHTVRAA AGRRGEEPWT VARRLLSADR LGTTILQHVG HEENVRAIMR HRAHTGGSDG
     ILRGSKPHPR AYGTFPHYLG HYVRELGVLS LEECVAHLTG RPAARLRLPD RGLVREGHRA
     DLVLFDPATV AAGSTYAEPR RLPTGIPYVL VDGRFVIEDG RRTDVLAGRA VRRPPAP
//