ID A0A7M1P3G2_HAEPA Unreviewed; 144 AA. AC A0A7M1P3G2; DT 07-APR-2021, integrated into UniProtKB/TrEMBL. DT 07-APR-2021, sequence version 1. DT 03-MAY-2023, entry version 7. DE RecName: Full=D-aminoacyl-tRNA deacylase {ECO:0000256|HAMAP-Rule:MF_00518}; DE Short=DTD {ECO:0000256|HAMAP-Rule:MF_00518}; DE EC=3.1.1.96 {ECO:0000256|HAMAP-Rule:MF_00518}; DE AltName: Full=Gly-tRNA(Ala) deacylase {ECO:0000256|HAMAP-Rule:MF_00518}; DE EC=3.1.1.- {ECO:0000256|HAMAP-Rule:MF_00518}; GN Name=dtd {ECO:0000256|HAMAP-Rule:MF_00518, GN ECO:0000313|EMBL:QOR19712.1}; GN ORFNames=INP93_02475 {ECO:0000313|EMBL:QOR19712.1}; OS Haemophilus parainfluenzae. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=729 {ECO:0000313|EMBL:QOR19712.1, ECO:0000313|Proteomes:UP000594952}; RN [1] {ECO:0000313|EMBL:QOR19712.1, ECO:0000313|Proteomes:UP000594952} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M1C130_2 {ECO:0000313|EMBL:QOR19712.1, RC ECO:0000313|Proteomes:UP000594952}; RA Watts S.C., Judd L.M., Carzino R., Ranganathan S., Holt K.E.; RT "Genomic diversity and antimicrobial resistance of Haemophilus colonising RT the airways of young children with cystic fibrosis."; RL Submitted (OCT-2020) 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:0000256|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:0000256|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; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00518}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00518}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_00518}. CC -!- SIMILARITY: Belongs to the DTD family. {ECO:0000256|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; CP063121; QOR19712.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7M1P3G2; -. DR Proteomes; UP000594952; 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 {ECO:0000256|HAMAP-Rule:MF_00518}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00518, ECO:0000313|EMBL:QOR19712.1}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00518}; KW tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00518}. FT MOTIF 136..137 FT /note="Gly-cisPro motif, important for rejection of L-amino FT acids" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00518" SQ SEQUENCE 144 AA; 15649 MW; 8D182E32D876C381 CRC64; MIALIQRVTQ AKVEVEGQIV GQIGKGLLVL LGVEKEDDQA KADKLAEKVL NYRIFSDEND KMNLNVQQIG GEVLVVSQFT LAADTQKGLR PSFSKGAAPT LANELYGYFS QKCAEKVTVA NGQFAADMQV SLTNDGPVTF WLNV //