DTD_AQUAE
ID DTD_AQUAE Reviewed; 148 AA.
AC O66742;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=D-tyrosyl-tRNA(Tyr) deacylase {ECO:0000305};
DE AltName: Full=Gly-tRNA(Ala) deacylase {ECO:0000255|HAMAP-Rule:MF_00518};
GN Name=dtd {ECO:0000255|HAMAP-Rule:MF_00518}; OrderedLocusNames=aq_428;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.76 ANGSTROMS).
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of D-Tyr-tRNA(tyr) deacylase from Aquifex aeolicus.";
RL Submitted (JUN-2006) to the PDB data bank.
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; AE000657; AAC06704.1; -; Genomic_DNA.
DR PIR; B70339; B70339.
DR RefSeq; NP_213302.1; NC_000918.1.
DR RefSeq; WP_010880240.1; NC_000918.1.
DR PDB; 2DBO; X-ray; 2.76 A; A=1-148.
DR PDBsum; 2DBO; -.
DR AlphaFoldDB; O66742; -.
DR SMR; O66742; -.
DR STRING; 224324.aq_428; -.
DR EnsemblBacteria; AAC06704; AAC06704; aq_428.
DR KEGG; aae:aq_428; -.
DR PATRIC; fig|224324.8.peg.353; -.
DR eggNOG; COG1490; Bacteria.
DR HOGENOM; CLU_076901_1_0_0; -.
DR InParanoid; O66742; -.
DR OMA; GVFQAHM; -.
DR OrthoDB; 1862614at2; -.
DR EvolutionaryTrace; O66742; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0051500; F:D-tyrosyl-tRNA(Tyr) deacylase activity; IBA:GO_Central.
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 GO; GO:0006399; P:tRNA metabolic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Reference proteome; RNA-binding;
KW tRNA-binding.
FT CHAIN 1..148
FT /note="D-aminoacyl-tRNA deacylase"
FT /id="PRO_0000164513"
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"
FT STRAND 2..15
FT /evidence="ECO:0007829|PDB:2DBO"
FT STRAND 18..32
FT /evidence="ECO:0007829|PDB:2DBO"
FT HELIX 39..51
FT /evidence="ECO:0007829|PDB:2DBO"
FT TURN 66..70
FT /evidence="ECO:0007829|PDB:2DBO"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:2DBO"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:2DBO"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:2DBO"
FT HELIX 99..114
FT /evidence="ECO:0007829|PDB:2DBO"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:2DBO"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:2DBO"
FT STRAND 130..144
FT /evidence="ECO:0007829|PDB:2DBO"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:2DBO"
SQ SEQUENCE 148 AA; 16968 MW; 24A3324C96C21234 CRC64;
MRAVIQRVKK SWVEVDGKVV GSINEGLNVF LGVRKGDTEE DIEKLVNKIL NLRIFEDERG
KFQYSVLDIK GEILVVSQFT LYANVKKGRR PSFEEAEEPK RAKELYEKFV DKIKESGLKV
ETGIFGAMMD VFIENWGPVT IIIDSREI
