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Database: UniProt
Entry: A0A3B7PS36_9GAMM
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ID   A0A3B7PS36_9GAMM        Unreviewed;       146 AA.
AC   A0A3B7PS36;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
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   ORFNames=BEN74_11240 {ECO:0000313|EMBL:AYA03346.1};
OS   Acinetobacter sp. WCHAc010034.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1879049 {ECO:0000313|EMBL:AYA03346.1, ECO:0000313|Proteomes:UP000264687};
RN   [1] {ECO:0000313|EMBL:AYA03346.1, ECO:0000313|Proteomes:UP000264687}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WCHAc010034 {ECO:0000313|EMBL:AYA03346.1,
RC   ECO:0000313|Proteomes:UP000264687};
RA   Hu Y., Long H., Feng Y., Zong Z.;
RT   "The complete genome of Acinetobacter sp. strain WCHAc010034.";
RL   Submitted (SEP-2018) 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|ARBA:ARBA00009673,
CC       ECO:0000256|HAMAP-Rule:MF_00518}.
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DR   EMBL; CP032279; AYA03346.1; -; Genomic_DNA.
DR   RefSeq; WP_068913433.1; NZ_CP032279.1.
DR   AlphaFoldDB; A0A3B7PS36; -.
DR   STRING; 1879049.GCA_001696615_03499; -.
DR   OrthoDB; 9801395at2; -.
DR   Proteomes; UP000264687; 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   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   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00518};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00518, ECO:0000313|EMBL:AYA03346.1};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00518};
KW   tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00518}.
FT   MOTIF           137..138
FT                   /note="Gly-cisPro motif, important for rejection of L-amino
FT                   acids"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00518"
SQ   SEQUENCE   146 AA;  16033 MW;  D023553C748C2EE3 CRC64;
     MRALLQRVLE AKVVVDGETA GEIGHGVLVF LGLGKQDTLE KGQKLIDKIL KYRFFDDEQG
     KMGWNLAQAN GGLLLVSQFT LMAQTRKGLR PDFGPAMPPA EAQALYLQLA DYAKSQFPNV
     QTGIFAADMK VHLVNDGPVT FNLEVE
//
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