ID   A0A176KXU1_9ACTN        Unreviewed;       576 AA.
AC   A0A176KXU1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Aminoacylase {ECO:0000313|EMBL:OAA96734.1};
GN   ORFNames=A6P39_31645 {ECO:0000313|EMBL:OAA96734.1};
OS   Streptomyces sp. FXJ1.172.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=710705 {ECO:0000313|EMBL:OAA96734.1};
RN   [1] {ECO:0000313|EMBL:OAA96734.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FXJ1.172 {ECO:0000313|EMBL:OAA96734.1};
RA   Liu M., Liu N., Shang F., Huang Y.;
RT   "Activation and identification of NC-1, a novel cryptic cyclodepsipeptide
RT   from red soil-derived Streptomyces sp. FXJ1.172.";
RL   Submitted (APR-2016) 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:OAA96734.1}.
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DR   EMBL; LWRP01000167; OAA96734.1; -; Genomic_DNA.
DR   RefSeq; WP_067053373.1; NZ_CP119133.1.
DR   AlphaFoldDB; A0A176KXU1; -.
DR   STRING; 710705.A6P39_31645; -.
DR   OrthoDB; 9766983at2; -.
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; 2.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 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;
FT   DOMAIN          46..547
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   576 AA;  62012 MW;  E4213A93503D87EC CRC64;
     MLDHLIKGAT VVDGTGAPAF TADVGLRGGR IAAVGEVTEE ARTSEDATGL VLTPGFVDPH
     THYDAQLFWD PYATPSLNHG VTTVAAGNCG FTLAPLNPAR PEDADYTRRM MAKVEGMSLV
     ALEEGAPWSW HSFGEYLDAL DGRTAVNVGF MVGHCALRRH VMGPDAVGGQ PDEEQLARMA
     GLLHEAMDAG AWGLSTTQSS THSDGDGQPV ASRHARPAEL LALSRAVGEH EGTQIEAIVA
     GCLDQFSDDE IDLLVEMSAV AGRPLNWNVL TVDAAVPERV PRQLSASERA RKAGGRVVAL
     TMPILTPMNM SLGTFCALNL IPGWGPVLAL PVPERIARLK DPAVRSELLR RATSKEAGVF
     RRLADFGRYV IGDTYSEANR GLTGRVVRDI AGERGLDPFA CLVEICANDR LRTVLWPMPR
     DNDPASWALR AETWQHEDVL LGGSDAGAHL DRMCGAPYTT RFIGDCLRGR KLVGLEQAVK
     MLTDDPARLF GLRERGQVRE GWHADLVLLD PERIDAGQAR LVHDLPGDSP RLDSRAIGIR
     AVWVNGAEAI RDDAVSGAVP GKVLRSGRDT RTVSTR
//