ID   DTDA_NATPD              Reviewed;         441 AA.
AC   Q3ITN8;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=D-aminoacyl-tRNA deacylase {ECO:0000255|HAMAP-Rule:MF_00562};
DE            EC=3.1.1.96 {ECO:0000255|HAMAP-Rule:MF_00562};
DE   AltName: Full=D-tyrosyl-tRNA(Tyr) deacylase;
GN   Name=dtdA {ECO:0000255|HAMAP-Rule:MF_00562}; OrderedLocusNames=NP_0808A;
OS   Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS   8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Natronomonas.
OX   NCBI_TaxID=348780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC   2260 / Gabara;
RX   PubMed=16169924; DOI=10.1101/gr.3952905;
RA   Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA   Oesterhelt D.;
RT   "Living with two extremes: conclusions from the genome sequence of
RT   Natronomonas pharaonis.";
RL   Genome Res. 15:1336-1343(2005).
CC   -!- FUNCTION: D-aminoacyl-tRNA deacylase with broad substrate specificity.
CC       By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules,
CC       this enzyme counteracts the toxicity associated with the formation of
CC       D-aminoacyl-tRNA entities in vivo. {ECO:0000255|HAMAP-Rule:MF_00562}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA +
CC         H(+); Xref=Rhea:RHEA:13953, Rhea:RHEA-COMP:10123, Rhea:RHEA-
CC         COMP:10124, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:59871,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:79333; EC=3.1.1.96;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00562};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala);
CC         Xref=Rhea:RHEA:53744, Rhea:RHEA-COMP:9657, Rhea:RHEA-COMP:13640,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78522; EC=3.1.1.96;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00562};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00562};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00562};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00562}.
CC   -!- SIMILARITY: Belongs to the DtdA deacylase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00562}.
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DR   EMBL; CR936257; CAI48495.1; -; Genomic_DNA.
DR   RefSeq; WP_011322131.1; NC_007426.1.
DR   AlphaFoldDB; Q3ITN8; -.
DR   SMR; Q3ITN8; -.
DR   STRING; 348780.NP_0808A; -.
DR   EnsemblBacteria; CAI48495; CAI48495; NP_0808A.
DR   GeneID; 3700968; -.
DR   KEGG; nph:NP_0808A; -.
DR   eggNOG; arCOG01616; Archaea.
DR   HOGENOM; CLU_610619_0_0_2; -.
DR   OMA; MECTHHG; -.
DR   OrthoDB; 25601at2157; -.
DR   Proteomes; UP000002698; Chromosome.
DR   GO; GO:0051499; F:D-aminoacyl-tRNA deacylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019478; P:D-amino acid catabolic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00562; Deacylase_DtdA; 1.
DR   InterPro; IPR018033; Deacylase_DtdA_archaea.
DR   InterPro; IPR007508; DtdA.
DR   PANTHER; PTHR34667; PTHR34667; 1.
DR   Pfam; PF04414; tRNA_deacylase; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..441
FT                   /note="D-aminoacyl-tRNA deacylase"
FT                   /id="PRO_0000345225"
SQ   SEQUENCE   441 AA;  46763 MW;  9DF179D302829D83 CRC64;
     MLAIVVSRAD EASEHIGRKL RSLADWTEHE DERRADGAGG GTYYRTDRAE LRIFDDLHIH
     LDGAASAFEE PDLLVFASRH SGDTGPLLTA HATGNFGPAE YGGGDGSLAR AAPNALSAVR
     DAFETHAPDD YDVGIECTHH GPSTVGCSSL FVELGSGPDQ WQDSEGAAAV ARSILSLRGV
     EPHTERTVVG FGGGHYAPRF DRVLTDTDWG VGHVAADWSL TELGDPRDSR AVIAKAFQAS
     GTEFALVDGD RPELEAVIED LGFEVLSETF LQETTGVPLS LVGRLEDDCG PIDDGLRLGE
     PATGYDGEFV TEELPDELLD EANGVDRTAV REAADAVALA YGTADGGSLA VGPVALAAAD
     DYRSLVESLA AVLDTKYDSV EIEASTVIAH REAFDPELAR DAGVDEGPAF GKLSSGASVD
     VDGETVTPDD VHRVRERRFE F