DTDA_PYRAB
ID DTDA_PYRAB Reviewed; 272 AA.
AC Q9V2R8; G8ZFI2;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=D-aminoacyl-tRNA deacylase {ECO:0000255|HAMAP-Rule:MF_00562};
DE EC=3.1.1.96 {ECO:0000255|HAMAP-Rule:MF_00562, ECO:0000269|PubMed:16844682, ECO:0000269|PubMed:17251192};
DE AltName: Full=D-tyrosyl-tRNA(Tyr) deacylase;
GN Name=dtdA {ECO:0000255|HAMAP-Rule:MF_00562}; Synonyms=dtd2;
GN OrderedLocusNames=PYRAB00070; ORFNames=PAB2349;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, MASS SPECTROMETRY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MUTAGENESIS OF SER-78; HIS-80;
RP HIS-92; GLU-137; HIS-140; HIS-141; GLU-154; TRP-162; HIS-197 AND TYR-198.
RX PubMed=16844682; DOI=10.1074/jbc.m605860200;
RA Ferri-Fioni M.-L., Fromant M., Bouin A.-P., Aubard C., Lazennec C.,
RA Plateau P., Blanquet S.;
RT "Identification in archaea of a novel D-Tyr-tRNATyr deacylase.";
RL J. Biol. Chem. 281:27575-27585(2006).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=17251192; DOI=10.1093/nar/gkl1145;
RA Wydau S., Ferri-Fioni M.-L., Blanquet S., Plateau P.;
RT "GEK1, a gene product of Arabidopsis thaliana involved in ethanol
RT tolerance, is a D-aminoacyl-tRNA deacylase.";
RL Nucleic Acids Res. 35:930-938(2007).
CC -!- FUNCTION: D-aminoacyl-tRNA deacylase with broad substrate specificity.
CC By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules,
CC this enzyme counteracts the toxicity associated with the formation of
CC D-aminoacyl-tRNA entities in vivo. Catalyzes the hydrolysis of D-
CC tyrosyl-tRNA(Tyr) and D-aspartyl-tRNA(Asp).
CC {ECO:0000269|PubMed:16844682, ECO:0000269|PubMed:17251192}.
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_00562,
CC ECO:0000269|PubMed:16844682, ECO:0000269|PubMed:17251192};
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_00562};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-tyrosyl-tRNA(Tyr) + H2O = D-tyrosine + tRNA(Tyr);
CC Xref=Rhea:RHEA:25347, Rhea:RHEA-COMP:9707, Rhea:RHEA-COMP:9872,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:58570, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78723; Evidence={ECO:0000269|PubMed:16844682,
CC ECO:0000269|PubMed:17251192};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00562,
CC ECO:0000269|PubMed:16844682};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-Rule:MF_00562,
CC ECO:0000269|PubMed:16844682};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Thermostable. {ECO:0000269|PubMed:16844682};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00562,
CC ECO:0000269|PubMed:16844682}.
CC -!- MASS SPECTROMETRY: Mass=30907; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:16844682};
CC -!- SIMILARITY: Belongs to the DtdA deacylase family. {ECO:0000255|HAMAP-
CC Rule:MF_00562, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCE69373.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ248283; CAB48930.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE69373.1; ALT_INIT; Genomic_DNA.
DR PIR; C75185; C75185.
DR RefSeq; WP_010867130.1; NC_000868.1.
DR AlphaFoldDB; Q9V2R8; -.
DR SMR; Q9V2R8; -.
DR STRING; 272844.PAB2349; -.
DR EnsemblBacteria; CAB48930; CAB48930; PAB2349.
DR GeneID; 1495689; -.
DR KEGG; pab:PAB2349; -.
DR PATRIC; fig|272844.11.peg.7; -.
DR eggNOG; arCOG01616; Archaea.
DR HOGENOM; CLU_056464_1_0_2; -.
DR OMA; CYEATHH; -.
DR OrthoDB; 84039at2157; -.
DR PhylomeDB; Q9V2R8; -.
DR BRENDA; 3.1.1.96; 5242.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; Chromosome.
DR GO; GO:0051499; F:D-aminoacyl-tRNA deacylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019478; P:D-amino acid catabolic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00562; Deacylase_DtdA; 1.
DR InterPro; IPR018033; Deacylase_DtdA_archaea.
DR InterPro; IPR007508; DtdA.
DR PANTHER; PTHR34667; PTHR34667; 1.
DR Pfam; PF04414; tRNA_deacylase; 1.
DR PIRSF; PIRSF016210; UCP016210; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Zinc.
FT CHAIN 1..272
FT /note="D-aminoacyl-tRNA deacylase"
FT /id="PRO_0000158969"
FT MUTAGEN 78
FT /note="S->A: Reduces deacylase activity."
FT /evidence="ECO:0000269|PubMed:16844682"
FT MUTAGEN 80
FT /note="H->A: Reduces deacylase activity."
FT /evidence="ECO:0000269|PubMed:16844682"
FT MUTAGEN 92
FT /note="H->A: Reduces deacylase activity."
FT /evidence="ECO:0000269|PubMed:16844682"
FT MUTAGEN 137
FT /note="E->A: 10-fold decrease of deacylase activity."
FT /evidence="ECO:0000269|PubMed:16844682"
FT MUTAGEN 140
FT /note="H->A: Loss of deacylase activity."
FT /evidence="ECO:0000269|PubMed:16844682"
FT MUTAGEN 141
FT /note="H->A: No effect."
FT /evidence="ECO:0000269|PubMed:16844682"
FT MUTAGEN 154
FT /note="E->A: Reduces deacylase activity."
FT /evidence="ECO:0000269|PubMed:16844682"
FT MUTAGEN 162
FT /note="W->A: Increases deacylase activity."
FT /evidence="ECO:0000269|PubMed:16844682"
FT MUTAGEN 197
FT /note="H->A: Increases deacylase activity."
FT /evidence="ECO:0000269|PubMed:16844682"
FT MUTAGEN 198
FT /note="Y->A: No effect."
FT /evidence="ECO:0000269|PubMed:16844682"
SQ SEQUENCE 272 AA; 30781 MW; 3B75F554B602D3EB CRC64;
MKVIMTTKVD KASMNIMQKL IENFGFKETE LKFDGNPVYK KDDMVILTTN DEMIYYDYLD
REIEKQLSFK PEIIAFASRH SSKQKLPALT THVTGNWGEA MYGGKDESFA IAIPSAMKLA
LLKMNELNDL GWTVCYEATH HGPSELEVPS FFIEIGSSEE EWVNDRAGEI IAETIVYVLD
NYENSKFKVA LGIGGGHYAP KQTKRALNSD LAFGHILPKY AQPVSRDVIL KAINRFHEKV
EAIYVDWKGS KGETRQLAKS LAQELGLEFI KD
