(data stored in SCRATCH3701 zone)

SWISSPROT: GLUQ_ECOBW

ID   GLUQ_ECOBW              Reviewed;         308 AA.
AC   C4ZRN7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 2.
DT   11-DEC-2019, entry version 57.
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}; OrderedLocusNames=BWG_0137;
OS   Escherichia coli (strain K12 / MC4100 / BW2952).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=595496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MC4100 / BW2952;
RX   PubMed=19376874; DOI=10.1128/jb.00118-09;
RA   Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R.,
RA   Wang L.;
RT   "Genomic sequencing reveals regulatory mutations and recombinational events
RT   in the widely used MC4100 lineage of Escherichia coli K-12.";
RL   J. Bacteriol. 191:4025-4029(2009).
CC   -!- FUNCTION: Catalyzes the tRNA-independent activation of glutamate in
CC       presence of ATP and the subsequent transfer of glutamate onto a
CC       tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2-
CC       cyclopenten-1-yl) moiety of the queuosine in the wobble position of the
CC       QUC anticodon. {ECO:0000255|HAMAP-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-Rule:MF_01428};
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       GluQ subfamily. {ECO:0000255|HAMAP-Rule:MF_01428}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACR63341.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; CP001396; ACR63341.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000937424.1; NC_012759.1.
DR   SMR; C4ZRN7; -.
DR   EnsemblBacteria; ACR63341; ACR63341; BWG_0137.
DR   KEGG; ebw:BWG_0137; -.
DR   HOGENOM; HOG000252723; -.
DR   KO; K01894; -.
DR   OMA; WLLRMED; -.
DR   BioCyc; ECOL595496:BWG_RS00730-MONOMER; -.
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; C4ZRN7.
DR   SWISS-2DPAGE; C4ZRN7.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Metal-binding;
KW   Nucleotide-binding; Zinc.
FT   CHAIN           1..308
FT                   /note="Glutamyl-Q tRNA(Asp) synthetase"
FT                   /id="PRO_1000215270"
FT   REGION          19..23
FT                   /note="Glutamate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   MOTIF           22..32
FT                   /note="'HIGH' region"
FT   MOTIF           238..242
FT                   /note="'KMSKS' region"
FT   METAL           111
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   METAL           113
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   METAL           125
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   METAL           129
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   BINDING         55
FT                   /note="Glutamate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   BINDING         182
FT                   /note="Glutamate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   BINDING         200
FT                   /note="Glutamate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   BINDING         241
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
SQ   SEQUENCE   308 AA;  34868 MW;  69BA4A164AB4363C CRC64;
     MLPPYFLFKE MTDTQYIGRF APSPSGELHF GSLIAALGSY LQARARQGRW LVRIEDIDPP
     REVPGAAETI LRQLEHYGLH WDGDVLWQSQ RHDAYREALA WLHEQGLSYY CTCTRARIQS
     IGGIYDGHCR VLHHGPDNAA VRIRQQHPVT QFTDQLRGII HADEKLARED FIIHRRDGLF
     AYNLAVVVDD HFQGVTEIVR GADLIEPTVR QISLYQLFGW KVPDYIHLPL ALNPQGAKLS
     KQNHAPALPK GDPRPVLIAA LQFLGQQAEA HWQDFSVEQI LQSAVKNWRL TAVPESAIVN
     STFSNASC
//

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