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Database: UniProt
Entry: A0A1H1T6A5_9ACTN
LinkDB: A0A1H1T6A5_9ACTN
Original site: A0A1H1T6A5_9ACTN 
ID   A0A1H1T6A5_9ACTN        Unreviewed;       517 AA.
AC   A0A1H1T6A5;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=N-acyl-D-amino-acid deacylase {ECO:0000313|EMBL:SDS55663.1};
GN   ORFNames=SAMN04489812_2270 {ECO:0000313|EMBL:SDS55663.1};
OS   Microlunatus soli.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Microlunatus.
OX   NCBI_TaxID=630515 {ECO:0000313|EMBL:SDS55663.1, ECO:0000313|Proteomes:UP000199103};
RN   [1] {ECO:0000313|EMBL:SDS55663.1, ECO:0000313|Proteomes:UP000199103}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21800 {ECO:0000313|EMBL:SDS55663.1,
RC   ECO:0000313|Proteomes:UP000199103};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; LT629772; SDS55663.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1T6A5; -.
DR   STRING; 630515.SAMN04489812_2270; -.
DR   OrthoDB; 9766983at2; -.
DR   Proteomes; UP000199103; Chromosome i.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
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; 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:UP000199103}.
FT   DOMAIN          41..205
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
FT   DOMAIN          296..499
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   517 AA;  54567 MW;  022891D0656B9580 CRC64;
     MTVKITGGTV VDPYDGSYPA ELMLDGDRIA AIGTDLPAAD QTIDATGRMI MPGAIDAHSH
     ADARVFDDDV QLGLLRSGVT SVIAGQDGIS FAPGDGRYAT DYFGALNGRH PSYRGGGVGA
     LLDGWDGRTR LNVGYLVPAG TVRYEVLGRE ARRPTPFELE AMVGMVADGM AAGALGLSTG
     LDYVPGVFAD AAELAALCGP VAAASGIYVS HIRGYEENAG VGVDELIEIC RRSGVRGHAS
     HFHARPELIG ELIERARRAG VDFSWDAYPY FRGFTLLSMV LLPSELIMLG NAEAAHRLQD
     EAVRSELAAG FAARVEEHEN LGIGWEHRIR IASAGTGSDR DLEGLTLAEA GTRRGLDPLQ
     VGYRLLAGSG LTTTTVMEIP QPRTDDHLAR QFTLSGACSG SDGIFFGGAP HPRGFGCVAR
     MYGRFGRERG DFDWPQLTRI TSGTAAEAFG LSGRGRVVAG AVADLVLLDP TTVADRADYA
     NPRELSVGID QVLVRGRLVL DGGELTADLA GGSVRRG
//
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