ID DTD_HAEIN Reviewed; 144 AA. AC P44814; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAR-2024, entry version 142. 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=D-tyrosyl-tRNA(Tyr) deacylase {ECO:0000303|PubMed:12571243}; DE AltName: Full=Gly-tRNA(Ala) deacylase {ECO:0000255|HAMAP-Rule:MF_00518}; GN Name=dtd {ECO:0000255|HAMAP-Rule:MF_00518}; OrderedLocusNames=HI_0670; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F., RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS), AND SUBUNIT. RX PubMed=12571243; DOI=10.1074/jbc.m213150200; RA Lim K., Tempczyk A., Bonander N., Toedt J., Howard A., Eisenstein E., RA Herzberg O.; RT "A catalytic mechanism for D-Tyr-tRNATyr deacylase based on the crystal RT structure of Hemophilus influenzae HI0670."; RL J. Biol. Chem. 278:13496-13502(2003). 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 ECO:0000269|PubMed:12571243}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00518, CC ECO:0000305}. 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, ECO:0000305}. CC -!- CAUTION: Initially the conserved reside Thr-80 was thought to be a CC nucleophile (PubMed:12571243); mutagenesis in E.coli and P.falciparum CC indicates it is not. {ECO:0000305|PubMed:12571243}. 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; L42023; AAC22330.1; -; Genomic_DNA. DR PIR; E64156; E64156. DR RefSeq; NP_438830.1; NC_000907.1. DR PDB; 1J7G; X-ray; 1.64 A; A=1-144. DR PDBsum; 1J7G; -. DR AlphaFoldDB; P44814; -. DR SMR; P44814; -. DR STRING; 71421.HI_0670; -. DR EnsemblBacteria; AAC22330; AAC22330; HI_0670. DR KEGG; hin:HI_0670; -. DR PATRIC; fig|71421.8.peg.700; -. DR eggNOG; COG1490; Bacteria. DR HOGENOM; CLU_076901_1_1_6; -. DR OrthoDB; 9801395at2; -. DR PhylomeDB; P44814; -. DR BioCyc; HINF71421:G1GJ1-705-MONOMER; -. DR BRENDA; 3.1.1.96; 2529. DR EvolutionaryTrace; P44814; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0051500; F:D-tyrosyl-tRNA(Tyr) deacylase activity; IBA:GO_Central. 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 GO; GO:0006399; P:tRNA metabolic process; IBA:GO_Central. 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 NCBIfam; TIGR00256; D-aminoacyl-tRNA deacylase; 1. 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. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Hydrolase; Reference proteome; RNA-binding; KW tRNA-binding. FT CHAIN 1..144 FT /note="D-aminoacyl-tRNA deacylase" FT /id="PRO_0000164546" FT MOTIF 136..137 FT /note="Gly-cisPro motif, important for rejection of L-amino FT acids" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00518" FT STRAND 2..15 FT /evidence="ECO:0007829|PDB:1J7G" FT STRAND 18..32 FT /evidence="ECO:0007829|PDB:1J7G" FT HELIX 39..51 FT /evidence="ECO:0007829|PDB:1J7G" FT STRAND 62..64 FT /evidence="ECO:0007829|PDB:1J7G" FT TURN 66..70 FT /evidence="ECO:0007829|PDB:1J7G" FT STRAND 72..77 FT /evidence="ECO:0007829|PDB:1J7G" FT HELIX 79..82 FT /evidence="ECO:0007829|PDB:1J7G" FT HELIX 99..114 FT /evidence="ECO:0007829|PDB:1J7G" FT STRAND 119..121 FT /evidence="ECO:0007829|PDB:1J7G" FT STRAND 129..143 FT /evidence="ECO:0007829|PDB:1J7G" SQ SEQUENCE 144 AA; 15862 MW; D8F84702EF5A3CBB CRC64; MIALIQRVSQ AKVDVKGETI GKIGKGLLVL LGVEKEDNRE KADKLAEKVL NYRIFSDEND KMNLNVQQAQ GELLIVSQFT LAADTQKGLR PSFSKGASPA LANELYEYFI QKCAEKLPVS TGQFAADMQV SLTNDGPVTF WLNV //