DTD_HAEIN
ID DTD_HAEIN Reviewed; 144 AA.
AC P44814;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 136.
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:0000303|PubMed:12571243};
DE AltName: Full=Gly-tRNA(Ala) deacylase {ECO:0000255|HAMAP-Rule:MF_00518};
GN Name=dtd {ECO:0000255|HAMAP-Rule:MF_00518}; OrderedLocusNames=HI_0670;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS), AND SUBUNIT.
RX PubMed=12571243; DOI=10.1074/jbc.m213150200;
RA Lim K., Tempczyk A., Bonander N., Toedt J., Howard A., Eisenstein E.,
RA Herzberg O.;
RT "A catalytic mechanism for D-Tyr-tRNATyr deacylase based on the crystal
RT structure of Hemophilus influenzae HI0670.";
RL J. Biol. Chem. 278:13496-13502(2003).
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 ECO:0000269|PubMed:12571243}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00518,
CC ECO:0000305}.
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, ECO:0000305}.
CC -!- CAUTION: Initially the conserved reside Thr-80 was thought to be a
CC nucleophile (PubMed:12571243); mutagenesis in E.coli and P.falciparum
CC indicates it is not. {ECO:0000305|PubMed:12571243}.
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DR EMBL; L42023; AAC22330.1; -; Genomic_DNA.
DR PIR; E64156; E64156.
DR RefSeq; NP_438830.1; NC_000907.1.
DR RefSeq; WP_005694618.1; NC_000907.1.
DR PDB; 1J7G; X-ray; 1.64 A; A=1-144.
DR PDBsum; 1J7G; -.
DR AlphaFoldDB; P44814; -.
DR SMR; P44814; -.
DR STRING; 71421.HI_0670; -.
DR EnsemblBacteria; AAC22330; AAC22330; HI_0670.
DR KEGG; hin:HI_0670; -.
DR PATRIC; fig|71421.8.peg.700; -.
DR eggNOG; COG1490; Bacteria.
DR HOGENOM; CLU_076901_1_1_6; -.
DR OMA; GVFQAHM; -.
DR PhylomeDB; P44814; -.
DR BioCyc; HINF71421:G1GJ1-705-MON; -.
DR BRENDA; 3.1.1.96; 2529.
DR EvolutionaryTrace; P44814; -.
DR Proteomes; UP000000579; 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..144
FT /note="D-aminoacyl-tRNA deacylase"
FT /id="PRO_0000164546"
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"
FT STRAND 2..15
FT /evidence="ECO:0007829|PDB:1J7G"
FT STRAND 18..32
FT /evidence="ECO:0007829|PDB:1J7G"
FT HELIX 39..51
FT /evidence="ECO:0007829|PDB:1J7G"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:1J7G"
FT TURN 66..70
FT /evidence="ECO:0007829|PDB:1J7G"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:1J7G"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:1J7G"
FT HELIX 99..114
FT /evidence="ECO:0007829|PDB:1J7G"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:1J7G"
FT STRAND 129..143
FT /evidence="ECO:0007829|PDB:1J7G"
SQ SEQUENCE 144 AA; 15862 MW; D8F84702EF5A3CBB CRC64;
MIALIQRVSQ AKVDVKGETI GKIGKGLLVL LGVEKEDNRE KADKLAEKVL NYRIFSDEND
KMNLNVQQAQ GELLIVSQFT LAADTQKGLR PSFSKGASPA LANELYEYFI QKCAEKLPVS
TGQFAADMQV SLTNDGPVTF WLNV
