ID   DTD_CHLTE               Reviewed;         150 AA.
AC   Q8KBF6;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=CT1831;
OS   Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS   (Chlorobium tepidum).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX   NCBI_TaxID=194439;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX   PubMed=12093901; DOI=10.1073/pnas.132181499;
RA   Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA   DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA   Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.,
RA   Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V.,
RA   Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M.,
RA   White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA   Fraser C.M.;
RT   "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT   anaerobic, green-sulfur bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
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; AE006470; AAM73052.1; -; Genomic_DNA.
DR   RefSeq; NP_662710.1; NC_002932.3.
DR   RefSeq; WP_010933491.1; NC_002932.3.
DR   AlphaFoldDB; Q8KBF6; -.
DR   SMR; Q8KBF6; -.
DR   STRING; 194439.CT1831; -.
DR   EnsemblBacteria; AAM73052; AAM73052; CT1831.
DR   KEGG; cte:CT1831; -.
DR   PATRIC; fig|194439.7.peg.1663; -.
DR   eggNOG; COG1490; Bacteria.
DR   HOGENOM; CLU_076901_1_0_10; -.
DR   OMA; GVFQAHM; -.
DR   OrthoDB; 1862614at2; -.
DR   Proteomes; UP000001007; 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..150
FT                   /note="D-aminoacyl-tRNA deacylase"
FT                   /id="PRO_0000164528"
FT   MOTIF           138..139
FT                   /note="Gly-cisPro motif, important for rejection of L-amino
FT                   acids"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00518"
SQ   SEQUENCE   150 AA;  16225 MW;  F8A7F28004F56FBE CRC64;
     MRTVVQQVRE ASVSIGGELH SSIGTGLLVL AGISRDDTAD DLAWMSRKIP NLRIFEDEKG
     KMNRSLKDIG GALLVVSQFT LYADASRGNR PGFSESAPPE LARVLFDRFV ESIRHEAGCP
     VETGVFGADM QVSLVNDGPV TIILESPKKP