DTDA_METBU
ID DTDA_METBU Reviewed; 479 AA.
AC Q12UQ4;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 25-MAY-2022, entry version 76.
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=Mbur_1941;
OS Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS ACE-M).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX NCBI_TaxID=259564;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA Cavicchioli R.;
RT "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT burtonii: the role of genome evolution in cold adaptation.";
RL ISME J. 3:1012-1035(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; CP000300; ABE52822.1; -; Genomic_DNA.
DR RefSeq; WP_011499964.1; NC_007955.1.
DR AlphaFoldDB; Q12UQ4; -.
DR SMR; Q12UQ4; -.
DR STRING; 259564.Mbur_1941; -.
DR EnsemblBacteria; ABE52822; ABE52822; Mbur_1941.
DR GeneID; 25393183; -.
DR KEGG; mbu:Mbur_1941; -.
DR HOGENOM; CLU_610619_0_0_2; -.
DR OMA; MECTHHG; -.
DR OrthoDB; 25601at2157; -.
DR Proteomes; UP000001979; 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..479
FT /note="D-aminoacyl-tRNA deacylase"
FT /id="PRO_0000345215"
SQ SEQUENCE 479 AA; 53540 MW; B7CE5DAD399E7BD1 CRC64;
MTEDNEVQIA GMSIVIVCSV VDPASQNIKE HLLKLRDWVE MSVPGGIFDD LSAVYQSGNF
YIIEVTEHHI YQDGIDRKIE EAGLDCDLLI FASKHKSADG RRLLTAHFTG NPGSADFGGY
PGELSMAAPF ALRCLLRNMA ELSESIGFDV SMESTHHGPS DLDVPSVYAE IGSSEVEWVD
QDAGDIVARS ILSVRSGFCP VGIGFGGGHY AARQSELVLG SDISFGHNFP NYQLQFVDVD
MFRKAVERSG ADLVYCDRKA MSSDEKKRIN ELADEFGLDV LRESDIKGME GVCWDIFRIF
WHKVRDEGLS GRVKVPVGLK DKLSENVCDI FDFDVSNVVT VVIDNELLKL VRSVDAGGVK
RLLDMSNVVY SERDDATISN HFYTFWNRDA EDFLTFIVDE CIKILKGRYD TEYVFEENVL
YISDERFSPE LARKWGVPSG PMFGELAKGQ SVMIEGNTVL PEMVHERTQK SLVLRNVIF
