ID   DTD_GEOUR               Reviewed;         155 AA.
AC   A5GC79;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=Gura_0610;
OS   Geotalea uraniireducens (strain Rf4) (Geobacter uraniireducens).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geotalea.
OX   NCBI_TaxID=351605;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1134 / JCM 13001 / Rf4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Shelobolina E., Aklujkar M.,
RA   Lovley D., Richardson P.;
RT   "Complete sequence of Geobacter uraniireducens Rf4.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000698; ABQ24822.1; -; Genomic_DNA.
DR   RefSeq; WP_011937547.1; NC_009483.1.
DR   AlphaFoldDB; A5GC79; -.
DR   SMR; A5GC79; -.
DR   STRING; 351605.Gura_0610; -.
DR   EnsemblBacteria; ABQ24822; ABQ24822; Gura_0610.
DR   KEGG; gur:Gura_0610; -.
DR   HOGENOM; CLU_076901_1_0_7; -.
DR   OMA; GVFQAHM; -.
DR   OrthoDB; 1862614at2; -.
DR   Proteomes; UP000006695; 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..155
FT                   /note="D-aminoacyl-tRNA deacylase"
FT                   /id="PRO_1000081654"
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   155 AA;  16866 MW;  C9A006BF78A10616 CRC64;
     MKAVIQRVSE AGVKVDGRTV GAVERGILVL LGVEKGDSTK EADWLAEKIV NLRIFEDAAG
     KMNLSLLDIK GELLAVSQFT LAGNCSKGRR PSFDTAAPPE EAIQLYEYFV GKTWELGIPV
     QTGIFQADMK VSLVNDGPVT FILETPKNKE RGTRS