ID   DTD_HERAR               Reviewed;         149 AA.
AC   A4G1U1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=D-aminoacyl-tRNA deacylase {ECO:0000255|HAMAP-Rule:MF_00518};
DE            Short=DTD {ECO:0000255|HAMAP-Rule:MF_00518};
DE            EC=3.1.1.96 {ECO:0000255|HAMAP-Rule:MF_00518};
DE   AltName: Full=Gly-tRNA(Ala) deacylase {ECO:0000255|HAMAP-Rule:MF_00518};
GN   Name=dtd {ECO:0000255|HAMAP-Rule:MF_00518}; OrderedLocusNames=HEAR0249;
OS   Herminiimonas arsenicoxydans.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herminiimonas.
OX   NCBI_TaxID=204773;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ULPAs1;
RX   PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA   Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA   Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA   Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E.,
RA   Lieutaud A., Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P.,
RA   Perdrial N., Schoepp B., Siguier P., Simeonova D.D., Rouy Z., Segurens B.,
RA   Turlin E., Vallenet D., van Dorsselaer A., Weiss S., Weissenbach J.,
RA   Lett M.-C., Danchin A., Bertin P.N.;
RT   "A tale of two oxidation states: bacterial colonization of arsenic-rich
RT   environments.";
RL   PLoS Genet. 3:518-530(2007).
CC   -!- FUNCTION: An aminoacyl-tRNA editing enzyme that deacylates mischarged
CC       D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala),
CC       protecting cells against glycine mischarging by AlaRS. Acts via tRNA-
CC       based rather than protein-based catalysis; rejects L-amino acids rather
CC       than detecting D-amino acids in the active site. By recycling D-
CC       aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme
CC       counteracts the toxicity associated with the formation of D-aminoacyl-
CC       tRNA entities in vivo and helps enforce protein L-homochirality.
CC       {ECO:0000255|HAMAP-Rule:MF_00518}.
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_00518};
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_00518};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00518}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00518}.
CC   -!- DOMAIN: A Gly-cisPro motif from one monomer fits into the active site
CC       of the other monomer to allow specific chiral rejection of L-amino
CC       acids. {ECO:0000255|HAMAP-Rule:MF_00518}.
CC   -!- SIMILARITY: Belongs to the DTD family. {ECO:0000255|HAMAP-
CC       Rule:MF_00518}.
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DR   EMBL; CU207211; CAL60478.1; -; Genomic_DNA.
DR   RefSeq; WP_011869824.1; NC_009138.1.
DR   AlphaFoldDB; A4G1U1; -.
DR   SMR; A4G1U1; -.
DR   STRING; 204773.HEAR0249; -.
DR   EnsemblBacteria; CAL60478; CAL60478; HEAR0249.
DR   KEGG; har:HEAR0249; -.
DR   eggNOG; COG1490; Bacteria.
DR   HOGENOM; CLU_076901_1_1_4; -.
DR   OMA; GVFQAHM; -.
DR   OrthoDB; 1862614at2; -.
DR   Proteomes; UP000006697; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051499; F:D-aminoacyl-tRNA deacylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0106026; F:Gly-tRNA(Ala) hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043908; F:Ser(Gly)-tRNA(Ala) hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019478; P:D-amino acid catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00563; Dtyr_deacylase; 1.
DR   Gene3D; 3.50.80.10; -; 1.
DR   HAMAP; MF_00518; Deacylase_Dtd; 1.
DR   InterPro; IPR003732; Daa-tRNA_deacyls_DTD.
DR   InterPro; IPR023509; DTD-like_sf.
DR   PANTHER; PTHR10472; PTHR10472; 1.
DR   Pfam; PF02580; Tyr_Deacylase; 1.
DR   SUPFAM; SSF69500; SSF69500; 1.
DR   TIGRFAMs; TIGR00256; TIGR00256; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Reference proteome; RNA-binding; tRNA-binding.
FT   CHAIN           1..149
FT                   /note="D-aminoacyl-tRNA deacylase"
FT                   /id="PRO_1000050839"
FT   MOTIF           137..138
FT                   /note="Gly-cisPro motif, important for rejection of L-amino
FT                   acids"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00518"
SQ   SEQUENCE   149 AA;  15708 MW;  F2A4057FD5F79E09 CRC64;
     MIALLQRVTR ASVVVNDVTI GAIGAGLMVL LCAERGDTPK EADALLGKLL AYRVFADDAG
     KMNRSVTDVA GGVLLVPQFT LAADTCSGTR PSFTPAAAPE LARSLFDYFV AQAVQRHVQV
     ATGEFGADMQ VSLTNDGPVT FWLQVKPAI