DTDA_METPE
ID DTDA_METPE Reviewed; 435 AA.
AC B8GIX8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 63.
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=Mpal_0158;
OS Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanoregulaceae; Methanosphaerula.
OX NCBI_TaxID=521011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1556 / DSM 19958 / E1-9c;
RX PubMed=26543115; DOI=10.1128/genomea.01280-15;
RA Cadillo-Quiroz H., Browne P., Kyrpides N., Woyke T., Goodwin L., Detter C.,
RA Yavitt J.B., Zinder S.H.;
RT "Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a
RT Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.";
RL Genome Announc. 3:0-0(2015).
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}.
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DR EMBL; CP001338; ACL15551.1; -; Genomic_DNA.
DR RefSeq; WP_012616870.1; NC_011832.1.
DR AlphaFoldDB; B8GIX8; -.
DR SMR; B8GIX8; -.
DR STRING; 521011.Mpal_0158; -.
DR EnsemblBacteria; ACL15551; ACL15551; Mpal_0158.
DR GeneID; 7270929; -.
DR KEGG; mpl:Mpal_0158; -.
DR eggNOG; arCOG00501; Archaea.
DR eggNOG; arCOG01616; Archaea.
DR HOGENOM; CLU_610619_0_0_2; -.
DR OMA; MECTHHG; -.
DR OrthoDB; 25601at2157; -.
DR Proteomes; UP000002457; 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.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..435
FT /note="D-aminoacyl-tRNA deacylase"
FT /id="PRO_1000197954"
SQ SEQUENCE 435 AA; 46677 MW; 31A33BC9F0CD1BC9 CRC64;
MKITLVNSRL DPAGVTIREQ IQVLLADPEY QREGIDWEFL EIDGRLIHQE RIDTGLNSDL
LIFLSRHTSR RPVPVLTVHP TGNPGEALLG GEAGSFAPAA PGWMQAVLQN LVRLVPDGYQ
ASYEVTHHGP TTLSTPSFFV EIGSTDHEWS DPVAGAAVAE AVLTAAPVDP ISLIGFGGTH
YAPRETAVAL ETRGAFGHIL HSREIGGLTG SLLAKIATAA EAEAVYIDRK AIDRPALDHL
YALLEETDLP VLGEKELHQI GSLSWQEYRS LRQIAGDAAP GAHLVIGTLP GGGTPVTATV
PADLLAQAIS ADQGRVMTAI GRMPVVGLTG RGGLLLPIII TYERYRSQII HDLITLCVKT
IREEQHAVID GDRLIIKKER FDPGLAASLG VPPGALFGML KGGQAVRVGD QVIKPEMVRS
CTVTAIHLRG LERYT