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DTDA_PYRAE
ID   DTDA_PYRAE              Reviewed;         251 AA.
AC   Q8ZVE0;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 90.
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=PAE2331;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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; AE009441; AAL64116.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ZVE0; -.
DR   SMR; Q8ZVE0; -.
DR   STRING; 178306.PAE2331; -.
DR   EnsemblBacteria; AAL64116; AAL64116; PAE2331.
DR   KEGG; pai:PAE2331; -.
DR   PATRIC; fig|178306.9.peg.1737; -.
DR   eggNOG; arCOG01616; Archaea.
DR   HOGENOM; CLU_056464_1_0_2; -.
DR   InParanoid; Q8ZVE0; -.
DR   OMA; CYEATHH; -.
DR   Proteomes; UP000002439; Chromosome.
DR   GO; GO:0051499; F:D-aminoacyl-tRNA deacylase activity; IBA:GO_Central.
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.
DR   PIRSF; PIRSF016210; UCP016210; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..251
FT                   /note="D-aminoacyl-tRNA deacylase"
FT                   /id="PRO_0000158970"
SQ   SEQUENCE   251 AA;  28126 MW;  5F186BB0B70DCB4C CRC64;
     MYVLVLSLGD PVSRTFLELH PMPLVETRGD IEVRKYGEIP AVVYKGEPTE FYREDILASL
     GKYAIFISRH EMSNPRPLFT VHTPGSWPDV SVANPRLASA LFRALCKHAY EPFECAFEAT
     HHAPNTSLVS ATFIEVGSTE AEWRDKRAVG VLAQALEEAL TKEFEGPTPT MAIGDLHYVT
     ISDSVLRGEF DLGHVVPKYI NITTNIVENI LKKHTISIKK TIIFRKNIKN PIRTEIIELL
     RAKGIEVTLK G
 
 
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