DTDA_HALSA
ID DTDA_HALSA Reviewed; 453 AA.
AC Q9HS70;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 25-MAY-2022, entry version 93.
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};
DE AltName: Full=D-tyrosyl-tRNA(Tyr) deacylase;
GN Name=dtdA {ECO:0000255|HAMAP-Rule:MF_00562}; OrderedLocusNames=VNG_0378C;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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. {ECO:0000255|HAMAP-Rule:MF_00562}.
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 -!- 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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00562};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00562};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00562}.
CC -!- SIMILARITY: Belongs to the DtdA deacylase family. {ECO:0000255|HAMAP-
CC Rule:MF_00562}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG18938.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE004437; AAG18938.1; ALT_INIT; Genomic_DNA.
DR PIR; F84196; F84196.
DR RefSeq; WP_049892484.1; NC_002607.1.
DR AlphaFoldDB; Q9HS70; -.
DR SMR; Q9HS70; -.
DR STRING; 64091.VNG_0378C; -.
DR PaxDb; Q9HS70; -.
DR EnsemblBacteria; AAG18938; AAG18938; VNG_0378C.
DR GeneID; 5953762; -.
DR KEGG; hal:VNG_0378C; -.
DR PATRIC; fig|64091.14.peg.281; -.
DR HOGENOM; CLU_610619_0_0_2; -.
DR InParanoid; Q9HS70; -.
DR OrthoDB; 25601at2157; -.
DR Proteomes; UP000000554; Chromosome.
DR GO; GO:0051499; F:D-aminoacyl-tRNA deacylase activity; IBA:GO_Central.
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.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..453
FT /note="D-aminoacyl-tRNA deacylase"
FT /id="PRO_0000158978"
FT REGION 428..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 453 AA; 47568 MW; F240D364F761E53E CRC64;
MIGIVVSRAD GASTHIWAQL REIEDFERIG PDAYRADGIE VRVFEELHTT IDDAADAFEA
AVDMVVVVSR HSGDTGPLLS AHYTGNFGAA EYGGADRSVA PACPNAHHAV VDSLRSYAPP
EYDVAMECTH HGPTSVGAPS MFVELGSSPA EWQDDAGARA VARAVRDLRG VPPHGDRAVV
VFGGGHYTPR ATRILADTDW PVGHVAADWS LTELGRPNAH RGVVDAMFTA SGAAHALVEG
DRPELTETIR DLGYTVVSET WVRETDGVPL SRVAALEESL TTVDDGLRFG EPAATHTGGY
LVVELPDAVL DAAHAVDTAA TVAAGRSHAL AVTTVNAGRR LAGSAAFPDA DAYEAFVDDV
AAVLNAEYAS VSRADGELTA TREVFDPEAA AALGVPEGPA FGRLAGGEAI EHDGRTIAPA
AVTSTETVRA DVALHERPRE RVRRPSDDEG KGN
