ID   DTDA_METLZ              Reviewed;         443 AA.
AC   A2STU3;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 71.
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=Mlab_1586;
OS   Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanocorpusculaceae; Methanocorpusculum.
OX   NCBI_TaxID=410358;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43576 / DSM 4855 / Z;
RX   PubMed=21304657; DOI=10.4056/sigs.35575;
RA   Anderson I.J., Sieprawska-Lupa M., Goltsman E., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Tice H., Dalin E., Barry K., Pitluck S., Hauser L.,
RA   Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT   "Complete genome sequence of Methanocorpusculum labreanum type strain Z.";
RL   Stand. Genomic Sci. 1:197-203(2009).
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; CP000559; ABN07749.1; -; Genomic_DNA.
DR   RefSeq; WP_011833952.1; NC_008942.1.
DR   AlphaFoldDB; A2STU3; -.
DR   SMR; A2STU3; -.
DR   STRING; 410358.Mlab_1586; -.
DR   EnsemblBacteria; ABN07749; ABN07749; Mlab_1586.
DR   GeneID; 4794667; -.
DR   KEGG; mla:Mlab_1586; -.
DR   eggNOG; arCOG01616; Archaea.
DR   HOGENOM; CLU_610619_0_0_2; -.
DR   OMA; MECTHHG; -.
DR   OrthoDB; 25601at2157; -.
DR   Proteomes; UP000000365; 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   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   PANTHER; PTHR34667; PTHR34667; 1.
DR   Pfam; PF04414; tRNA_deacylase; 1.
DR   SUPFAM; SSF56281; SSF56281; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..443
FT                   /note="D-aminoacyl-tRNA deacylase"
FT                   /id="PRO_0000345219"
SQ   SEQUENCE   443 AA;  47911 MW;  DA091FCE6C697994 CRC64;
     MIIDILNSDS DPAGRNIRAA IDELLKNPPE GGFPLFDGNE VTFHTVSGRI IHAEKSAVNP
     DADLIIVVSR HSSVNPVPVL TVHPAGNFGI AGLGGNDREL GLTSPAWMKS ILQNHAEFVP
     EGYRVSYEIT HHGPTDFPVP FFFVEVGSTE KEWNDPAACI AAAKSVLYAR PSPEIVPLIG
     FGGTHYAVRQ TAIGLETKGA FGHMMHTRDV GSVSKEMVSQ MIAKSCGVFA AHIDRKALSK
     QEISHIEGIL AEVGLEEITE GDLRKMNAMS FSTWVAYRDL AALQAPGLKI FPHGRIFDGD
     PAVVELPSDL FSAAFLGYEE IFLAELDKMG NIFHTTGKGG RLMPTLLTSA KNRQKVSGDL
     IVLSVQQITR TQDSLVEGDQ ITIARRQFDP VLARTLGVPS GPLYGQLVAG KPVTLPDGRM
     ITPDMVTKVV RTSIKIPGLE NYS