DTDA_THEAC
ID DTDA_THEAC Reviewed; 256 AA.
AC Q9HM47;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 95.
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=Ta0022;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
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; AL445063; CAC11171.1; -; Genomic_DNA.
DR RefSeq; WP_010900450.1; NC_002578.1.
DR AlphaFoldDB; Q9HM47; -.
DR SMR; Q9HM47; -.
DR STRING; 273075.Ta0022; -.
DR EnsemblBacteria; CAC11171; CAC11171; CAC11171.
DR GeneID; 1455691; -.
DR KEGG; tac:Ta0022; -.
DR eggNOG; arCOG01616; Archaea.
DR HOGENOM; CLU_056464_1_0_2; -.
DR OMA; CYEATHH; -.
DR OrthoDB; 84039at2157; -.
DR Proteomes; UP000001024; 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.
DR PIRSF; PIRSF016210; UCP016210; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..256
FT /note="D-aminoacyl-tRNA deacylase"
FT /id="PRO_0000158976"
SQ SEQUENCE 256 AA; 28719 MW; E919C73FEA1D66FD CRC64;
MHLIVASRSD PASVRMLDYL TEKYTFSEKG GVLNHGDFDL VIIEDRHIFH DMSLSGKYDY
LVVLSRHSSA ADVKSLTAHP TGNFGPSADL GGKPRTINIS CPRVMSGTLR RMMESYSGSR
FEVTFEATHH GPIFDIPNYY VEIGTTENEW NDPEALSTTV DSVMNPDVRD YDAFVGVGGG
HYAPKIKEYF RENSVNIGHI ISKHDHDALE PWEIDMAVKR TPGCKGFIMD RKGTRGNVRE
MVKKYADENS LELITI
