ID B1C9I0_9FIRM Unreviewed; 149 AA.
AC B1C9I0;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 72.
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:EDS72551.1};
GN ORFNames=ANASTE_02273 {ECO:0000313|EMBL:EDS72551.1};
OS Anaerofustis stercorihominis DSM 17244.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Anaerofustis.
OX NCBI_TaxID=445971 {ECO:0000313|EMBL:EDS72551.1, ECO:0000313|Proteomes:UP000005178};
RN [1] {ECO:0000313|EMBL:EDS72551.1, ECO:0000313|Proteomes:UP000005178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17244 {ECO:0000313|EMBL:EDS72551.1,
RC ECO:0000313|Proteomes:UP000005178};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Anaerofustis stercorihominis (DSM 17244).";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDS72551.1, ECO:0000313|Proteomes:UP000005178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17244 {ECO:0000313|EMBL:EDS72551.1,
RC ECO:0000313|Proteomes:UP000005178};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDS72551.1}.
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DR EMBL; ABIL02000006; EDS72551.1; -; Genomic_DNA.
DR RefSeq; WP_007051021.1; NZ_DS560019.1.
DR AlphaFoldDB; B1C9I0; -.
DR STRING; 445971.ANASTE_02273; -.
DR eggNOG; COG1490; Bacteria.
DR HOGENOM; CLU_076901_1_0_9; -.
DR OrthoDB; 9801395at2; -.
DR Proteomes; UP000005178; Unassembled WGS sequence.
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:EDS72551.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005178};
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; 16741 MW; 0433DE4D7418FD3A CRC64;
MKAVVQRVKS SKVTINDRVV GNINKGFNVL FGAEEKDTKK DADYLARKIS NLRVFEDENG
KMNLSIKDIG GQMLIISQFT LAADTKKGNR PSFVNAMEPV EANELYEYFM KKIEEEGISV
KRGIFGEDML VDIVNDGPVT ILFDTKTKE
//
