DTD_STREQ
ID DTD_STREQ Reviewed; 147 AA.
AC Q54088;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 85.
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};
OS Streptococcus dysgalactiae subsp. equisimilis (Streptococcus equisimilis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=119602;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION TO 48.
RC STRAIN=H46A;
RX PubMed=8232196; DOI=10.1007/bf00280210;
RA Mechold U., Steiner K., Vettermann S., Malke H.;
RT "Genetic organization of the streptokinase region of the Streptococcus
RT equisimilis H46A chromosome.";
RL Mol. Gen. Genet. 241:129-140(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-147.
RC STRAIN=H46A;
RX PubMed=2989113; DOI=10.1016/0378-1119(85)90145-3;
RA Malke H., Roe B.A., Ferretti J.J.;
RT "Nucleotide sequence of the streptokinase gene from Streptococcus
RT equisimilis H46A.";
RL Gene 34:357-362(1985).
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}.
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DR EMBL; X72832; CAA51352.1; -; Genomic_DNA.
DR PIR; S39974; S39974.
DR RefSeq; WP_065354984.1; NZ_UHFO01000001.1.
DR AlphaFoldDB; Q54088; -.
DR SMR; Q54088; -.
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; -; 1.
DR HAMAP; MF_00518; Deacylase_Dtd; 1.
DR InterPro; IPR003732; Daa-tRNA_deacyls_DTD.
DR InterPro; IPR023509; DTD-like_sf.
DR PANTHER; PTHR10472; PTHR10472; 1.
DR Pfam; PF02580; Tyr_Deacylase; 1.
DR SUPFAM; SSF69500; SSF69500; 1.
DR TIGRFAMs; TIGR00256; TIGR00256; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; RNA-binding; tRNA-binding.
FT CHAIN 1..147
FT /note="D-aminoacyl-tRNA deacylase"
FT /id="PRO_0000164598"
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"
SQ SEQUENCE 147 AA; 15907 MW; 19B35E14755967AF CRC64;
MKLVLQRVKE ASVSIDGKIA GAINQGLLLL VGVGPDDAAE DLAYAVRKIV NMRIFSDADG
KMNQSIQDIK GSILSVSQFT LYADTKKGNR PAFTGAAKPD MASQFYDRFN EQLADFVPVE
RGVFGADMQV SLINDGPVTI ILDTKCH
