ID W8U5R9_PEPAC Unreviewed; 149 AA.
AC W8U5R9;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=D-aminoacyl-tRNA deacylase {ECO:0000256|HAMAP-Rule:MF_00518};
DE Short=DTD {ECO:0000256|HAMAP-Rule:MF_00518};
DE EC=3.1.1.96 {ECO:0000256|HAMAP-Rule:MF_00518};
DE AltName: Full=Gly-tRNA(Ala) deacylase {ECO:0000256|HAMAP-Rule:MF_00518};
DE EC=3.1.1.- {ECO:0000256|HAMAP-Rule:MF_00518};
GN Name=dtd {ECO:0000256|HAMAP-Rule:MF_00518,
GN ECO:0000313|EMBL:AHM56276.1};
GN ORFNames=EAL2_c09770 {ECO:0000313|EMBL:AHM56276.1};
OS Peptoclostridium acidaminophilum DSM 3953.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Peptoclostridium.
OX NCBI_TaxID=1286171 {ECO:0000313|EMBL:AHM56276.1, ECO:0000313|Proteomes:UP000019591};
RN [1] {ECO:0000313|EMBL:AHM56276.1, ECO:0000313|Proteomes:UP000019591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3953 {ECO:0000313|EMBL:AHM56276.1,
RC ECO:0000313|Proteomes:UP000019591};
RX PubMed=24926057;
RA Poehlein A., Andreesen J.R., Daniel R.;
RT "Complete Genome Sequence of Amino Acid-Utilizing Eubacterium
RT acidaminophilum al-2 (DSM 3953).";
RL Genome Announc. 2:e00573-14(2014).
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:0000256|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:0000256|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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00518};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00518}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_00518}.
CC -!- SIMILARITY: Belongs to the DTD family. {ECO:0000256|ARBA:ARBA00009673,
CC ECO:0000256|HAMAP-Rule:MF_00518}.
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DR EMBL; CP007452; AHM56276.1; -; Genomic_DNA.
DR RefSeq; WP_025435288.1; NZ_CP007452.1.
DR AlphaFoldDB; W8U5R9; -.
DR STRING; 1286171.EAL2_c09770; -.
DR KEGG; eac:EAL2_c09770; -.
DR PATRIC; fig|1286171.3.peg.927; -.
DR eggNOG; COG1490; Bacteria.
DR HOGENOM; CLU_076901_1_0_9; -.
DR OrthoDB; 9801395at2; -.
DR Proteomes; UP000019591; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051499; F:D-aminoacyl-tRNA deacylase activity; IEA:UniProtKB-UniRule.
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 CDD; cd00563; Dtyr_deacylase; 1.
DR Gene3D; 3.50.80.10; D-tyrosyl-tRNA(Tyr) deacylase; 1.
DR HAMAP; MF_00518; Deacylase_Dtd; 1.
DR InterPro; IPR003732; Daa-tRNA_deacyls_DTD.
DR InterPro; IPR023509; DTD-like_sf.
DR NCBIfam; TIGR00256; D-aminoacyl-tRNA deacylase; 1.
DR PANTHER; PTHR10472:SF5; D-AMINOACYL-TRNA DEACYLASE 1; 1.
DR PANTHER; PTHR10472; D-TYROSYL-TRNA TYR DEACYLASE; 1.
DR Pfam; PF02580; Tyr_Deacylase; 1.
DR SUPFAM; SSF69500; DTD-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00518};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00518, ECO:0000313|EMBL:AHM56276.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019591};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00518};
KW tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00518}.
FT MOTIF 137..138
FT /note="Gly-cisPro motif, important for rejection of L-amino
FT acids"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00518"
SQ SEQUENCE 149 AA; 16568 MW; 73AD9E538C26B46B CRC64;
MRAVVQRVTK SSVKVEDEII GSVGKGLMVL LGVTHDDTED DVKYLAEKIS NLRIFEDENE
KMNLSLLDVK GELLAVSQFT LYGDCRKGRR PNFTDAAKPD IANSLYEIFV KELEGMGIHV
ETGSFGAHMM VDILNDGPVT MLLDSKRSF
//
