{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P0A6M4","secondaryAccessions":["P32147","Q2M8I4"],"uniProtkbId":"DTD_ECOLI","entryAudit":{"firstPublicDate":"2005-05-10","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2005-05-10","entryVersion":153,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Escherichia coli (strain K12)","taxonId":83333,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00518"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10918062"}],"value":"D-aminoacyl-tRNA deacylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00518"}],"value":"DTD"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00518"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10383414"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10918062"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"4292198"}],"value":"3.1.1.96"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"4292198"}],"value":"D-tyrosyl RNA deacylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10383414"}],"value":"D-tyrosyl-tRNA(Tyr) deacylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00518"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"28362257"}],"value":"Gly-tRNA(Ala) deacylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"27224426"}],"value":"Gly-tRNA(Gly) deacylase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00518"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10918062"}],"value":"dtd"},"synonyms":[{"value":"yihZ"}],"orderedLocusNames":[{"value":"b3887"},{"value":"JW3858"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10383414"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10918062"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15292242"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16902403"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24302572"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25441601"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27224426"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28362257"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"4292198"}],"value":"An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs, has no observable editing activity on tRNAs charged with cognate L-amino acid (PubMed:10383414, PubMed:10918062, PubMed:24302572, PubMed:27224426, PubMed:4292198). Edits mischarged glycyl-tRNA(Ala) more efficiently than AlaRS (PubMed:28362257). Acts via tRNA-based rather than protein-based catalysis (PubMed:24302572, PubMed:27224426, PubMed:28362257). Rejects correctly charged L-amino acid-tRNAs from its binding site rather than specifically recognizing incorrectly charged D-amino acid-tRNAs (PubMed:27224426). Hydrolyzes correctly charged, achiral, glycyl-tRNA(Gly); GTP-bound EF-Tu (tested with T.thermophilus EF-Tu AC Q5SHN6) protects charged glycyl-tRNA(Gly) from hydrolysis, while increasing Dtd levels or inactivating EF-Tu decreases protection (PubMed:27224426). Hydrolyzes mischarged glycyl-tRNA(Ala) (but not seryl-tRNA(Ala)) even in the presence of EF-Tu, edits about 4-fold better than the editing domain of AlaRS (PubMed:28362257). Has greater activity on glycyl-tRNA(Ala) than glycyl-tRNA(Gly) due in part to its recognition of the conserved tRNA(Ala) G3.U70 wobble base pair (PubMed:28362257). Binds D-amino acids but not L-amino acids (PubMed:16902403). Overexpression of E.coli or P.falciparum Dtd is toxic in E.coli, toxicity can be rescued by supplementation with Gly (PubMed:27224426). By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality (PubMed:15292242). Hydrolyzes D-tyrosyl-tRNA(Tyr) (PubMed:10383414, PubMed:24302572, PubMed:27224426, PubMed:4292198). Hydrolyzes D-phenylalanyl-tRNA(Phe) (PubMed:24302572, PubMed:4292198). Hydrolyzes D-aspartyl-tRNA(Asp) (PubMed:10918062). Hydrolyzes D-tryptophanyl-tRNA(Trp) (PubMed:10918062). Hydrolyzes glycyl-tRNA(Gly) (PubMed:27224426). Hydrolyzes glycyl-tRNA(Ala) (PubMed:28362257)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"glycyl-tRNA(Ala) + H2O = tRNA(Ala) + glycine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:53744"},{"database":"Rhea","id":"RHEA-COMP:9657"},{"database":"Rhea","id":"RHEA-COMP:13640"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57305"},{"database":"ChEBI","id":"CHEBI:78442"},{"database":"ChEBI","id":"CHEBI:78522"}],"ecNumber":"3.1.1.96","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00518"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28362257"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a D-aminoacyl-tRNA + H2O = a tRNA + a D-alpha-amino acid + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13953"},{"database":"Rhea","id":"RHEA-COMP:10123"},{"database":"Rhea","id":"RHEA-COMP:10124"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:59871"},{"database":"ChEBI","id":"CHEBI:78442"},{"database":"ChEBI","id":"CHEBI:79333"}],"ecNumber":"3.1.1.96","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00518"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10383414"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10918062"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"4292198"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-tyrosyl-tRNA(Tyr) + H2O = D-tyrosine + tRNA(Tyr)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:25347"},{"database":"Rhea","id":"RHEA-COMP:9707"},{"database":"Rhea","id":"RHEA-COMP:9872"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:58570"},{"database":"ChEBI","id":"CHEBI:78442"},{"database":"ChEBI","id":"CHEBI:78723"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10383414"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24302572"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27224426"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"4292198"}]}},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":1.0,"unit":"uM","substrate":"D-tyrosyl-tRNA(Tyr)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10383414"}]},{"constant":1.0,"unit":"uM","substrate":"glycyl-tRNA(Gly)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27224426"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10383414"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10918062"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27224426"}],"value":"kcat/KM is 6 uM(-1)sec(-1) for D-tyrosyl-tRNA(Tyr) (PubMed:10383414). kcat/KM is 2.8 uM(-1)sec(-1) for D-tryptophanyl-tRNA(Trp) (PubMed:10918062). kcat/KM is 12 uM(-1)sec(-1) for D-aspartyl-tRNA(Asp) (PubMed:10918062). kcat/KM is 10 uM (-1)sec(-1) for glycyl-tRNA(Gly) (PubMed:27224426)."}]}}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00518"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10383414"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11568181"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P0A6M4","intActId":"EBI-562575"},"interactantTwo":{"uniProtKBAccession":"P06961","geneName":"cca","intActId":"EBI-545256"},"numberOfExperiments":2,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00518"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"4292198"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00518"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24302572"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27224426"}],"value":"A Gly-cisPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of L-amino acids (PubMed:24302572, PubMed:27224426)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10383414"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10918062"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15292242"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25441601"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28362257"}],"value":"No phenotype in rich or minimal medium, decreased growth rate in the presence of excess D-tyrosine (PubMed:10383414). A double dtd-dadA deletion mutant has a more pronounced growth defect in the presence of D-Tyr (in strain K12 / EC989) (PubMed:10383414). In a dtd deletion mutant about 40% of tRNA(Tyr) is D-tyrosyl-tRNA(Tyr); overexpressing the gene for tRNA(Tyr) suppresses the toxicity of D-Tyr by increasing the levels of L-tyrosyl-tRNA(Tyr) available for translation (PubMed:15292242). Decreased growth in the presence of D-Asp, D-Ser, D-Gln and D-Trp (PubMed:10918062). Poor growth on 20 mg/ml D-Tyr, no growth on 500 mg/ml D-Tyr or 20 mg/ml D-Trp (PubMed:25441601). Overexpression of genes for tRNA(Asp) or tRNA(Trp) suppresses the toxicity of their respective D-amino acids (PubMed:15292242). No effect seen when grown in 3 or 10 mM Gly; in a mutant that no longer edits mischarged glycyl-tRNA(Ala) or seryl-tRNA(Ala) (triple mutation in alaS) Gly becomes toxic, but excess Ala restores growth (PubMed:28362257)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00518"}],"value":"Belongs to the DTD family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24302572"}],"value":"Initially the conserved reside Thr-80 was thought to be a nucleophile; mutagenesis in this organism and P.falciparum indicates it is not"}],"commentType":"CAUTION"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":145,"modifier":"EXACT"}},"description":"D-aminoacyl-tRNA 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