ID DTD_THENN Reviewed; 149 AA. AC B9KAP7; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 24-MAR-2009, sequence version 1. DT 28-JUN-2023, entry version 71. 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=CTN_1854; OS Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E). OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae; OC Thermotoga. OX NCBI_TaxID=309803; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E; RA Lim S.K., Kim J.S., Cha S.H., Park B.C., Lee D.S., Tae H.S., Kim S.-J., RA Kim J.J., Park K.J., Lee S.Y.; RT "The genome sequence of the hyperthermophilic bacterium Thermotoga RT neapolitana."; RL Submitted (NOV-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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000916; ACM24030.1; -; Genomic_DNA. DR RefSeq; WP_015920266.1; NC_011978.1. DR AlphaFoldDB; B9KAP7; -. DR SMR; B9KAP7; -. DR STRING; 309803.CTN_1854; -. DR EnsemblBacteria; ACM24030; ACM24030; CTN_1854. DR KEGG; tna:CTN_1854; -. DR eggNOG; COG1490; Bacteria. DR HOGENOM; CLU_076901_1_0_0; -. DR OMA; VFGADMK; -. DR Proteomes; UP000000445; 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; D-tyrosyl-tRNA(Tyr) deacylase; 1. DR HAMAP; MF_00518; Deacylase_Dtd; 1. DR InterPro; IPR003732; Daa-tRNA_deacyls_DTD. DR InterPro; IPR023509; DTD-like_sf. DR PANTHER; PTHR10472:SF5; D-AMINOACYL-TRNA DEACYLASE 1; 1. DR PANTHER; PTHR10472; D-TYROSYL-TRNA TYR DEACYLASE; 1. DR Pfam; PF02580; Tyr_Deacylase; 1. DR SUPFAM; SSF69500; DTD-like; 1. DR TIGRFAMs; TIGR00256; D-tyrosyl-tRNA(Tyr) deacylase; 1. PE 3: Inferred from homology; KW Cytoplasm; Hydrolase; RNA-binding; tRNA-binding. FT CHAIN 1..149 FT /note="D-aminoacyl-tRNA deacylase" FT /id="PRO_1000146219" 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; 16589 MW; ED6505109AC134B7 CRC64; MRAVVQRVNE AKVIVDEKVV GAIGKGLLVF VGVGKDDTEK DCEWLAEKVS GLRIFEDEEG KMNLSIMDVG GEVLVVSQFT LYGDCRRGKR PSFTEAAPPE KGKELYEKFV DLLEKKGLKV EKGIFRAHMH VHLVNDGPVT LLLDSSRLF //