ID   DTDA_METB6              Reviewed;         436 AA.
AC   A7IAL9;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   25-MAY-2022, entry version 69.
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=Mboo_2266;
OS   Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanoregulaceae; Methanoregula.
OX   NCBI_TaxID=456442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21154 / JCM 14090 / 6A8;
RX   PubMed=25998264; DOI=10.1099/mic.0.000117;
RA   Braeuer S., Cadillo-Quiroz H., Kyrpides N., Woyke T., Goodwin L.,
RA   Detter C., Podell S., Yavitt J.B., Zinder S.H.;
RT   "Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic
RT   peatland environments.";
RL   Microbiology 161:1572-1581(2015).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABS56780.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000780; ABS56780.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_048068472.1; NC_009712.1.
DR   AlphaFoldDB; A7IAL9; -.
DR   SMR; A7IAL9; -.
DR   STRING; 456442.Mboo_2266; -.
DR   EnsemblBacteria; ABS56780; ABS56780; Mboo_2266.
DR   GeneID; 5411083; -.
DR   KEGG; mbn:Mboo_2266; -.
DR   eggNOG; arCOG00501; Archaea.
DR   eggNOG; arCOG01616; Archaea.
DR   HOGENOM; CLU_610619_0_0_2; -.
DR   OrthoDB; 25601at2157; -.
DR   Proteomes; UP000002408; 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..436
FT                   /note="D-aminoacyl-tRNA deacylase"
FT                   /id="PRO_0000345221"
SQ   SEQUENCE   436 AA;  46842 MW;  6156D8789DACA773 CRC64;
     MKVALIHSRD DVAGCTIRRH IEQCLDDAHG SANGRTYEFV EVGGRLINAE GVDATLDVNL
     VIFLSRHSSV NPVPVLTVHA TGNFGAAELG GSPRTLAPAA PAMMQATLRA LARYCPEGYR
     VSYEVTHHGP TGLSHPSFFV EIGSTEKEWV DPVAGRAVAE AVLGADPAGA VPLIGIGGTH
     YAPRETAIAL SSRGAFGHIA SSRLQVALLD RELVQAMVVQ SRAVAAYIDR KAVLPGDVSR
     ISAILDELGI PRLSETEITS LGHLAWEAYR EVRALAATVG PQTRCFIHAL EGTGPLVLVS
     LDPVLLSEAK RCDESALVQR FGPLPVAHLA TEDNVLLPQF VAFERNSSKI INDLNTLCVK
     IIRNRESTAT ENDYLVIRKV RFDPQKAREL GVPAGPAYRQ LAAGQAVEYD GQIITPDRVS
     VATETRIHIP GLENYS