(data stored in ACNUC7421 zone)

SWISSPROT: DTD_ANADE

ID   DTD_ANADE               Reviewed;         149 AA.
AC   Q2IMC5;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   08-MAY-2019, entry version 76.
DE   RecName: Full=D-aminoacyl-tRNA deacylase {ECO:0000255|HAMAP-Rule:MF_00518};
DE            Short=DTD {ECO:0000255|HAMAP-Rule:MF_00518};
DE            EC=3.1.1.96 {ECO:0000255|HAMAP-Rule:MF_00518};
DE   AltName: Full=Gly-tRNA(Ala) deacylase {ECO:0000255|HAMAP-Rule:MF_00518};
DE            EC=3.1.1.- {ECO:0000255|HAMAP-Rule:MF_00518};
GN   Name=dtd {ECO:0000255|HAMAP-Rule:MF_00518};
GN   OrderedLocusNames=Adeh_0179;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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:0000255|HAMAP-
CC       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; EC=3.1.1.96;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00518};
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:0000255|HAMAP-Rule:MF_00518};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00518}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00518}.
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:0000255|HAMAP-Rule:MF_00518}.
CC   -!- SIMILARITY: Belongs to the DTD family. {ECO:0000255|HAMAP-
CC       Rule:MF_00518}.
DR   EMBL; CP000251; ABC79956.1; -; Genomic_DNA.
DR   SMR; Q2IMC5; -.
DR   STRING; 290397.Adeh_0179; -.
DR   EnsemblBacteria; ABC79956; ABC79956; Adeh_0179.
DR   KEGG; ade:Adeh_0179; -.
DR   eggNOG; ENOG4108YYA; Bacteria.
DR   eggNOG; COG1490; LUCA.
DR   HOGENOM; HOG000113981; -.
DR   KO; K07560; -.
DR   OMA; MDVSLTN; -.
DR   Proteomes; UP000001935; 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; -; 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;
DR   PRODOM; Q2IMC5.
DR   SWISS-2DPAGE; Q2IMC5.
KW   Complete proteome; Cytoplasm; Hydrolase; Reference proteome;
KW   RNA-binding; tRNA-binding.
FT   CHAIN         1    149       D-aminoacyl-tRNA deacylase.
FT                                /FTId=PRO_0000259261.
FT   MOTIF       137    138       Gly-cisPro motif, important for rejection
FT                                of L-amino acids. {ECO:0000255|HAMAP-
FT                                Rule:MF_00518}.
SQ   SEQUENCE   149 AA;  15716 MW;  C7CBC3C1270A1394 CRC64;
     MRAVVQRVSR AEVRVDGAVT GAVGRGLLVL LGVARDDGAQ DARLLADKLA ALRIFEDAAG
     KMNLAVAEVG GAVLVVSQFT LLGDARKGNR PGFSDAAPPE AANALYEAVC GMLREKGLRV
     ETGVFRADMQ VELVNDGPVT ILLDSRRLF
//

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