DTD_PROMH
ID DTD_PROMH Reviewed; 145 AA.
AC B4EZB4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-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=PMI2874;
OS Proteus mirabilis (strain HI4320).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=529507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI4320;
RX PubMed=18375554; DOI=10.1128/jb.01981-07;
RA Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA Parkhill J., Mobley H.L.T.;
RT "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT both adherence and motility.";
RL J. Bacteriol. 190:4027-4037(2008).
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; AM942759; CAR45661.1; -; Genomic_DNA.
DR RefSeq; WP_004246810.1; NC_010554.1.
DR AlphaFoldDB; B4EZB4; -.
DR SMR; B4EZB4; -.
DR STRING; 529507.PMI2874; -.
DR EnsemblBacteria; CAR45661; CAR45661; PMI2874.
DR GeneID; 6801952; -.
DR KEGG; pmr:PMI2874; -.
DR eggNOG; COG1490; Bacteria.
DR HOGENOM; CLU_076901_1_1_6; -.
DR OMA; GVFQAHM; -.
DR Proteomes; UP000008319; 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; Reference proteome; RNA-binding; tRNA-binding.
FT CHAIN 1..145
FT /note="D-aminoacyl-tRNA deacylase"
FT /id="PRO_1000127559"
FT MOTIF 137..138
FT /note="Gly-cisPro motif, important for rejection of L-amino
FT acids"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00518"
SQ SEQUENCE 145 AA; 15919 MW; 4F214462746D7A20 CRC64;
MIALIQRVTQ AKVDIAGVTV GAINHGLLVL LGVEKDDNQQ KAKRLCEKVC GYRIFSDEND
KMNLNVQQAG GSLLVVSQFT LAAETQKGMR PGFSNGAPPE MAENLYHYFV EQCKQQGLET
QTGQFAADMQ VTLTNDGPVT FWLQV
