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Database: UniProt
Entry: E1T8W3_BURSG
LinkDB: E1T8W3_BURSG
Original site: E1T8W3_BURSG 
ID   E1T8W3_BURSG            Unreviewed;       156 AA.
AC   E1T8W3;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 69.
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   OrderedLocusNames=BC1003_2930 {ECO:0000313|EMBL:ADN58883.1};
OS   Burkholderia sp. (strain CCGE1003).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=640512 {ECO:0000313|EMBL:ADN58883.1};
RN   [1] {ECO:0000313|EMBL:ADN58883.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCGE1003 {ECO:0000313|EMBL:ADN58883.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Daligault H., Davenport K., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA   Martinez-Romero E., Rogel M.A., Auchtung J., Tiedje J.M., Woyke T.;
RT   "Complete sequence of chromosome1 of Burkholderia sp. CCGE1003.";
RL   Submitted (SEP-2010) 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}.
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DR   EMBL; CP002217; ADN58883.1; -; Genomic_DNA.
DR   AlphaFoldDB; E1T8W3; -.
DR   STRING; 640512.BC1003_2930; -.
DR   KEGG; bgf:BC1003_2930; -.
DR   eggNOG; COG1490; Bacteria.
DR   HOGENOM; CLU_076901_1_1_4; -.
DR   OMA; VFGADMK; -.
DR   OrthoDB; 9801395at2; -.
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   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};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00518};
KW   tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00518}.
FT   MOTIF           146..147
FT                   /note="Gly-cisPro motif, important for rejection of L-amino
FT                   acids"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00518"
SQ   SEQUENCE   156 AA;  16547 MW;  164D4DA20B209C9E CRC64;
     MIALIQRVRR AEVRVVEGHS ERVAGAIDAG LLALVCAERG DTEAAADRLL AKVLGYRVFS
     DAAGKMNLSV QNVDGAGRAG GLLLVSQFTL AADTNSGLRP SFTPAAPPDE GKRLFDYFVA
     AARARHPIVE TGEFGADMQV SLVNDGPVTF WLQTHA
//
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