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Database: UniProt
Entry: A0A1F4K281_9BURK
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ID   A0A1F4K281_9BURK        Unreviewed;       156 AA.
AC   A0A1F4K281;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   08-MAY-2019, entry version 15.
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   ORFNames=A3F78_17745 {ECO:0000313|EMBL:OGB28751.1};
OS   Burkholderiales bacterium RIFCSPLOWO2_12_FULL_61_40.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales.
OX   NCBI_TaxID=1797566 {ECO:0000313|EMBL:OGB28751.1, ECO:0000313|Proteomes:UP000178940};
RN   [1] {ECO:0000313|EMBL:OGB28751.1, ECO:0000313|Proteomes:UP000178940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U.,
RA   Brodie E.L., Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected
RT   biogeochemical processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
CC   -!- FUNCTION: An aminoacyl-tRNA editing enzyme that deacylates
CC       mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-
CC       tRNA(Ala), protecting cells against glycine mischarging by AlaRS.
CC       Acts via tRNA-based rather than protein-based catalysis; rejects
CC       L-amino acids rather than detecting D-amino acids in the active
CC       site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA
CC       molecules, this enzyme counteracts the toxicity associated with
CC       the formation of D-aminoacyl-tRNA entities in vivo and helps
CC       enforce protein L-homochirality. {ECO:0000256|HAMAP-Rule:MF_00518,
CC       ECO:0000256|SAAS:SAAS01081655}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + H(+) +
CC         tRNA; Xref=Rhea:RHEA:13953, Rhea:RHEA-COMP:10123, Rhea:RHEA-
CC         COMP:10124, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:59871, ChEBI:CHEBI:78442, ChEBI:CHEBI:79333;
CC         EC=3.1.1.96; Evidence={ECO:0000256|HAMAP-Rule:MF_00518,
CC         ECO:0000256|SAAS:SAAS01118112};
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;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00518};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00518,
CC       ECO:0000256|SAAS:SAAS01081681}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00518,
CC       ECO:0000256|SAAS:SAAS00388074}.
CC   -!- DOMAIN: A Gly-cisPro motif from one monomer fits into the active
CC       site of the other monomer to allow specific chiral rejection of L-
CC       amino acids. {ECO:0000256|HAMAP-Rule:MF_00518}.
CC   -!- SIMILARITY: Belongs to the DTD family. {ECO:0000256|HAMAP-
CC       Rule:MF_00518, ECO:0000256|SAAS:SAAS00573604}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OGB28751.1}.
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DR   EMBL; MESI01000122; OGB28751.1; -; Genomic_DNA.
DR   Proteomes; UP000178940; 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   Gene3D; 3.50.80.10; -; 1.
DR   HAMAP; MF_00518; Deacylase_Dtd; 1.
DR   InterPro; IPR003732; Daa-tRNA_deacyls_DTD.
DR   InterPro; IPR023509; DTD-like_sf.
DR   PANTHER; PTHR10472; PTHR10472; 1.
DR   Pfam; PF02580; Tyr_Deacylase; 1.
DR   SUPFAM; SSF69500; SSF69500; 1.
DR   TIGRFAMs; TIGR00256; TIGR00256; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000178940};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00518,
KW   ECO:0000256|SAAS:SAAS00094371};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00518,
KW   ECO:0000256|SAAS:SAAS00464654};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00518,
KW   ECO:0000256|SAAS:SAAS01081646};
KW   tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00518,
KW   ECO:0000256|SAAS:SAAS01081683}.
FT   MOTIF       142    143       Gly-cisPro motif, important for rejection
FT                                of L-amino acids. {ECO:0000256|HAMAP-
FT                                Rule:MF_00518}.
SQ   SEQUENCE   156 AA;  16527 MW;  4A0AFBA1900B4DB9 CRC64;
     MQALLQRVRH ARVVVEGHTV GEIGAGLLVL LCAEQGDTEF QADKLLAKLL KLRIFSDAQG
     KMNLSVQDLD GAGTPGGLLV VSQFTLAADT SGGNRPSFKG AAVPEEGRRL YDYFVAQARQ
     FHAEVQTGVF AADMQVELVN DGPVTVPLRV APVAAG
//
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