ID   A0A1G7CA23_9ACTN        Unreviewed;       581 AA.
AC   A0A1G7CA23;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=N-acyl-D-amino-acid deacylase {ECO:0000313|EMBL:SDE36167.1};
GN   ORFNames=SAMN05216270_11946 {ECO:0000313|EMBL:SDE36167.1};
OS   Glycomyces harbinensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Glycomycetales; Glycomycetaceae;
OC   Glycomyces.
OX   NCBI_TaxID=58114 {ECO:0000313|EMBL:SDE36167.1, ECO:0000313|Proteomes:UP000198949};
RN   [1] {ECO:0000313|EMBL:SDE36167.1, ECO:0000313|Proteomes:UP000198949}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.3516 {ECO:0000313|EMBL:SDE36167.1,
RC   ECO:0000313|Proteomes:UP000198949};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FNAD01000019; SDE36167.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G7CA23; -.
DR   STRING; 58114.SAMN05216270_11946; -.
DR   Proteomes; UP000198949; 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; 2.
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          45..506
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
FT   REGION          512..581
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        512..533
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        564..581
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   581 AA;  62136 MW;  766FB2A6C2C809DD CRC64;
     MAAMDFVIRG AEIADGTGAP RFAAEVGVKD GRVAAIGGRL EGAAVIDAGG LVLAPGFIDM
     HAHSELAILD DHDHLAKLGQ GCTLEVLGQD GLSYAPVDES TAPQMWEAIA AWNGRPDVDY
     DWRTVGEYLD RLDRGVPVNA AYLVPHGTVR MAAMGWEDRA PTGDELAAMK ALVAQGMEEG
     AFGLSAGLSY TPGMYADTAE LVELCGVVAR YGGYFGPHQR SYGAGAMEGY AEMIQIAAES
     GCALHLAHAT LNYRVNEGRA AELLKLVDEG LDSGLAISLD TYPYLPGMTM LAALLPSWSL
     AGGYAALRER LNDPEARARI VHELDVTGTD GANGVPADWS RYEIASVTKP ELRGFVGRPV
     AEAAGARRPA EFYLDLLVRD DFGTGCLMHV GNEENVRAIM RHGVHTGSSD GVLAGDKIHP
     RAWGSFARYL GHYTRELGLL SVEECVAHLS GRPAAVLGLK DRGLVKEGFA ADLVLFDPEA
     VDARATFDEP RQQAAGVPYV FVNGRTAIEE GRRTDALAGR SVRRREGASS AGRKRGKRLS
     WPMVDPPPIP VGTGPTDAPE ACRGCEDPSP RRRSDKRMRF F
//