(data stored in ACNUC7421 zone)

SWISSPROT: DTD_AERHH

ID   DTD_AERHH               Reviewed;         145 AA.
AC   A0KEZ2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 81.
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=AHA_0281;
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240;
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
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; CP000462; ABK39550.1; -; Genomic_DNA.
DR   RefSeq; WP_011704287.1; NC_008570.1.
DR   RefSeq; YP_854808.1; NC_008570.1.
DR   SMR; A0KEZ2; -.
DR   STRING; 380703.AHA_0281; -.
DR   EnsemblBacteria; ABK39550; ABK39550; AHA_0281.
DR   GeneID; 4490438; -.
DR   KEGG; aha:AHA_0281; -.
DR   PATRIC; fig|380703.7.peg.268; -.
DR   eggNOG; ENOG4108YYA; Bacteria.
DR   eggNOG; COG1490; LUCA.
DR   HOGENOM; HOG000113982; -.
DR   KO; K07560; -.
DR   OMA; MDVSLTN; -.
DR   BioCyc; AHYD380703:G1G7B-281-MONOMER; -.
DR   Proteomes; UP000000756; 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; A0KEZ2.
DR   SWISS-2DPAGE; A0KEZ2.
KW   Complete proteome; Cytoplasm; Hydrolase; Reference proteome;
KW   RNA-binding; tRNA-binding.
FT   CHAIN         1    145       D-aminoacyl-tRNA deacylase.
FT                                /FTId=PRO_1000050808.
FT   MOTIF       137    138       Gly-cisPro motif, important for rejection
FT                                of L-amino acids. {ECO:0000255|HAMAP-
FT                                Rule:MF_00518}.
SQ   SEQUENCE   145 AA;  15244 MW;  F446CA1FDA311BE8 CRC64;
     MIALIQRVSE ASVTVEGEMT GAIGQGLLVL LGVEQGDDEA KADKLLHKVS GYRIFSDENG
     KMNLNVSQAG GGLLVVSQFT LAADTNKGMR PSFSGGAHPV EAERLYDYFV AQAAASGIPT
     ATGRFAADMK VALVNDGPVT FWLQV
//

If you have problems or comments...

PBIL Back to PBIL home page