(data stored in ACNUC1104 zone)

SWISSPROT: D3UYJ9_XENBS

ID   D3UYJ9_XENBS            Unreviewed;       145 AA.
AC   D3UYJ9;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 58.
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:CBJ79377.1};
GN   OrderedLocusNames=XBJ1_0226 {ECO:0000313|EMBL:CBJ79377.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79377.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|Proteomes:UP000002045};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ79377.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79377.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
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}.
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DR   EMBL; FN667741; CBJ79377.1; -; Genomic_DNA.
DR   RefSeq; WP_012986840.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0226; -.
DR   EnsemblBacteria; CBJ79377; CBJ79377; XBJ1_0226.
DR   GeneID; 8829849; -.
DR   KEGG; xbo:XBJ1_0226; -.
DR   PATRIC; fig|406818.4.peg.206; -.
DR   eggNOG; ENOG4108YYA; Bacteria.
DR   eggNOG; COG1490; LUCA.
DR   HOGENOM; HOG000113982; -.
DR   KO; K07560; -.
DR   OMA; MDVSLTN; -.
DR   BioCyc; XBOV406818:XBJ1_RS00980-MONOMER; -.
DR   Proteomes; UP000002045; 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; D3UYJ9.
DR   SWISS-2DPAGE; D3UYJ9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
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, ECO:0000313|EMBL:CBJ79377.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045};
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       137    138       Gly-cisPro motif, important for rejection
FT                                of L-amino acids. {ECO:0000256|HAMAP-
FT                                Rule:MF_00518}.
SQ   SEQUENCE   145 AA;  16133 MW;  7C374ECC8DC37638 CRC64;
     MIALIQRVTQ AKVVVEDETI GEIEQGLLVL LGVEKEDNQQ KAQRLCEKVM GYRVFSDEQG
     KMNLNVQQAN GSLLVVSQFT LAADTQKGLR PSFSGGAEPQ KADEFYRYFV EQCRVTGVKT
     ETGQFAADMK VSLINDGPVT FWLQV
//

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