DTD_BEUC1
ID DTD_BEUC1 Reviewed; 141 AA.
AC C5C226;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 67.
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=Bcav_3409;
OS Beutenbergia cavernae (strain ATCC BAA-8 / DSM 12333 / NBRC 16432).
OC Bacteria; Actinobacteria; Micrococcales; Beutenbergiaceae; Beutenbergia.
OX NCBI_TaxID=471853;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-8 / DSM 12333 / NBRC 16432;
RX PubMed=21304633; DOI=10.4056/sigs.1162;
RA Land M., Pukall R., Abt B., Goker M., Rohde M., Glavina Del Rio T.,
RA Tice H., Copeland A., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D.,
RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Hauser L., Chang Y.J., Jefferies C.C.,
RA Saunders E., Brettin T., Detter J.C., Han C., Chain P., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Lapidus A.;
RT "Complete genome sequence of Beutenbergia cavernae type strain (HKI
RT 0122).";
RL Stand. Genomic Sci. 1:21-28(2009).
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; CP001618; ACQ81651.1; -; Genomic_DNA.
DR RefSeq; WP_015883888.1; NC_012669.1.
DR AlphaFoldDB; C5C226; -.
DR SMR; C5C226; -.
DR STRING; 471853.Bcav_3409; -.
DR EnsemblBacteria; ACQ81651; ACQ81651; Bcav_3409.
DR KEGG; bcv:Bcav_3409; -.
DR eggNOG; COG1490; Bacteria.
DR HOGENOM; CLU_076901_1_2_11; -.
DR OMA; GVFQAHM; -.
DR OrthoDB; 1862614at2; -.
DR Proteomes; UP000007962; 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 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..141
FT /note="D-aminoacyl-tRNA deacylase"
FT /id="PRO_1000211720"
FT MOTIF 133..134
FT /note="Gly-cisPro motif, important for rejection of L-amino
FT acids"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00518"
SQ SEQUENCE 141 AA; 14757 MW; 4B90CA2A0D949112 CRC64;
MRVVLQRVSR ARVLVDGQVV GEVSGEGLVA FVGVTPGDGA GEVALLARKI AELRVLRDER
SVLDAGAGVL VVSQFTLYAD TRKGRRPTWS AAAPRPVAEP VVDALVEALR ERGVVVATGV
FGADMAVELT NDGPVTILLE A
