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Database: UniProt
Entry: A0A0T5ZJR1_9CHLR
LinkDB: A0A0T5ZJR1_9CHLR
Original site: A0A0T5ZJR1_9CHLR 
ID   A0A0T5ZJR1_9CHLR        Unreviewed;       533 AA.
AC   A0A0T5ZJR1;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=N-acyl-D-amino-acid deacylase, N-acyl-D-amino-acid deacylase {ECO:0000313|EMBL:KRT63033.1};
DE            EC=3.5.1.81 {ECO:0000313|EMBL:KRT63033.1};
GN   ORFNames=XU10_C0016G0025 {ECO:0000313|EMBL:KRT63033.1};
OS   Chloroflexi bacterium CSP1-4.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1640513 {ECO:0000313|EMBL:KRT63033.1, ECO:0000313|Proteomes:UP000051896};
RN   [1] {ECO:0000313|EMBL:KRT63033.1, ECO:0000313|Proteomes:UP000051896}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CSP1-4 {ECO:0000313|EMBL:KRT63033.1};
RA   Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA   Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT   "Critical biogeochemical functions in the subsurface are associated with
RT   bacteria from new phyla and little studied lineages.";
RL   Submitted (MAY-2015) 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:KRT63033.1}.
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DR   EMBL; LDXM01000016; KRT63033.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0T5ZJR1; -.
DR   STRING; 1640513.XU10_C0016G0025; -.
DR   PATRIC; fig|1640513.3.peg.1533; -.
DR   Proteomes; UP000051896; Unassembled WGS sequence.
DR   GO; GO:0047420; F:N-acyl-D-amino-acid deacylase activity; IEA:UniProtKB-EC.
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;
KW   Hydrolase {ECO:0000313|EMBL:KRT63033.1}.
FT   DOMAIN          50..513
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   533 AA;  57651 MW;  CC778542D87C1E5C CRC64;
     MTDAFDLLIE GGTVVDGGGG PGFAAAVGVI GDRLRIISGE TAHLRAARRI DATGHVVAPG
     FIDLHSHGGL MMLAEPRHEP KVRQGVTTEV IGVDGNSYAP FLRQQDLDDF LTLNAGLDGR
     PDIACDWGSV AGYLERFDRR VAVNVAYFIG NSALRISACG WDEVPADARA MDRQRGLLRE
     GMEEGAFGLS SGLDYPPGAY ATTEELGALL AEAAKLGGFY HTHVRYTLGD GFLDPFREAI
     EIGRQGDGPV HLTHFYHRAT YPGPPERMLK LVDDARAEGL DVTFDLYPSE WASTRLLIML
     PPWIQAGGVA KTRERLADRA IRARIRDELA ARGRSYAGAA PWADLRLGYF ARPEHARWEG
     RTLAEYMVET GLDPTDAICD LLLAEDLRVN QVTPGPHTAG LAPFFRHPVS MIGSDGVLIG
     AKPAPRTYGS FPRVLGEFVR EQRLTSLEEA VRKMTAAPAA RLGLADRGLL RDGLKADIVV
     FDPAAVRDLA TYEEPRRFPA GIPHVVVNGT LVVDGGEHTG ALPGRALRRS STA
//
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