DTD_PETMO
ID DTD_PETMO Reviewed; 150 AA.
AC A9BIE9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 25-MAY-2022, entry version 82.
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=Pmob_1934;
OS Petrotoga mobilis (strain DSM 10674 / SJ95).
OC Bacteria; Thermotogae; Petrotogales; Petrotogaceae; Petrotoga.
OX NCBI_TaxID=403833;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10674 / SJ95;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Noll K., Richardson P.;
RT "Complete sequence of Petroga mobilis SJ95.";
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}.
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DR EMBL; CP000879; ABX32621.1; -; Genomic_DNA.
DR RefSeq; WP_012209718.1; NC_010003.1.
DR AlphaFoldDB; A9BIE9; -.
DR SMR; A9BIE9; -.
DR STRING; 403833.Pmob_1934; -.
DR EnsemblBacteria; ABX32621; ABX32621; Pmob_1934.
DR KEGG; pmo:Pmob_1934; -.
DR eggNOG; COG1490; Bacteria.
DR HOGENOM; CLU_076901_1_0_0; -.
DR OMA; GVFQAHM; -.
DR OrthoDB; 1862614at2; -.
DR Proteomes; UP000000789; 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; -; 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..150
FT /note="D-aminoacyl-tRNA deacylase"
FT /id="PRO_1000081660"
FT MOTIF 138..139
FT /note="Gly-cisPro motif, important for rejection of L-amino
FT acids"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00518"
SQ SEQUENCE 150 AA; 17019 MW; 3237B320E21AB2BD CRC64;
MRAVVQRVSQ ASVTISDNIV AQIEKGLLVF LGISKIDQVS DISWMADKIV NLRIFEDDQN
KMNRSLLDIM GDMIVVSQFT LYGDCRKGRR PSFTDSATPE KAKVLYDNFL SYLKEKYPIN
VQQGEFQAHM KVNIVNDGPV TLLLDSQKLF
