(data stored in ACNUC7421 zone)

SWISSPROT: GLUQ_ECO57

ID   GLUQ_ECO57              Reviewed;         308 AA.
AC   Q8X909; Q7AHN1;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 3.
DT   08-MAY-2019, entry version 105.
DE   RecName: Full=Glutamyl-Q tRNA(Asp) synthetase {ECO:0000255|HAMAP-Rule:MF_01428};
DE            Short=Glu-Q-RSs {ECO:0000255|HAMAP-Rule:MF_01428};
DE            EC=6.1.1.- {ECO:0000255|HAMAP-Rule:MF_01428};
GN   Name=gluQ {ECO:0000255|HAMAP-Rule:MF_01428};
GN   OrderedLocusNames=Z0155, ECs0148;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Catalyzes the tRNA-independent activation of glutamate
CC       in presence of ATP and the subsequent transfer of glutamate onto a
CC       tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-
CC       dihydroxy-2-cyclopenten-1-yl) moiety of the queuosine in the
CC       wobble position of the QUC anticodon. {ECO:0000255|HAMAP-
CC       Rule:MF_01428}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01428};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01428};
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. GluQ subfamily. {ECO:0000255|HAMAP-Rule:MF_01428}.
DR   EMBL; AE005174; AAG54448.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33571.1; -; Genomic_DNA.
DR   PIR; D85498; D85498.
DR   PIR; D90647; D90647.
DR   RefSeq; NP_308175.3; NC_002695.1.
DR   RefSeq; WP_000937419.1; NZ_SDVX01000001.1.
DR   SMR; Q8X909; -.
DR   STRING; 155864.EDL933_0148; -.
DR   EnsemblBacteria; AAG54448; AAG54448; Z0155.
DR   EnsemblBacteria; BAB33571; BAB33571; BAB33571.
DR   GeneID; 913766; -.
DR   KEGG; ece:Z0155; -.
DR   KEGG; ecs:ECs0148; -.
DR   PATRIC; fig|386585.9.peg.247; -.
DR   eggNOG; ENOG4106F3G; Bacteria.
DR   eggNOG; COG0008; LUCA.
DR   HOGENOM; HOG000252723; -.
DR   KO; K01894; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0043039; P:tRNA aminoacylation; IEA:InterPro.
DR   GO; GO:0006400; P:tRNA modification; IEA:InterPro.
DR   Gene3D; 3.40.50.620; -; 2.
DR   HAMAP; MF_01428; Glu_Q_tRNA_synth; 1.
DR   InterPro; IPR022380; Glu-Q_TRNA(Asp)_Synthase.
DR   InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR   InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   TIGRFAMs; TIGR03838; queuosine_YadB; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q8X909.
DR   SWISS-2DPAGE; Q8X909.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase;
KW   Metal-binding; Nucleotide-binding; Reference proteome; Zinc.
FT   CHAIN         1    308       Glutamyl-Q tRNA(Asp) synthetase.
FT                                /FTId=PRO_0000208301.
FT   REGION       19     23       Glutamate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01428}.
FT   MOTIF        22     32       "HIGH" region.
FT   MOTIF       238    242       "KMSKS" region.
FT   METAL       111    111       Zinc. {ECO:0000255|HAMAP-Rule:MF_01428}.
FT   METAL       113    113       Zinc. {ECO:0000255|HAMAP-Rule:MF_01428}.
FT   METAL       125    125       Zinc. {ECO:0000255|HAMAP-Rule:MF_01428}.
FT   METAL       129    129       Zinc. {ECO:0000255|HAMAP-Rule:MF_01428}.
FT   BINDING      55     55       Glutamate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01428}.
FT   BINDING     182    182       Glutamate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01428}.
FT   BINDING     200    200       Glutamate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01428}.
FT   BINDING     241    241       ATP. {ECO:0000255|HAMAP-Rule:MF_01428}.
SQ   SEQUENCE   308 AA;  34885 MW;  EC1623668D42345C CRC64;
     MLPPYFLFKE MTDTQYIGRF APSPSGELHF GSLIAALGSY LQARARHGRW LVRIEDIDPP
     REVPGAAETI LRQLEHYGLH WDGDVLWQSQ RHHAYREALA WLHEQGLSYY CTCTRARIQS
     IGGIYDGHCR VLHHGPDNAA VRIRQQHPVT QFTDQLRGII HADEKLARED FIIHRRDGLF
     AYNLAVVVDD HFQGVSEIVR GADLIEPTVR QISLYQLFGW KVPDYIHLPL ALNPQGAKLS
     KQNHAPALPK GDPRPVLIAA LQFLGQQAEA HWQDFSVEQI LQSAVKNWRL TAVPESAIVN
     STFSNASC
//

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