ID   GLUQ_VEREI              Reviewed;         292 AA.
AC   A1WS08;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=Veis_4720;
OS   Verminephrobacter eiseniae (strain EF01-2).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Verminephrobacter.
OX   NCBI_TaxID=391735;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EF01-2;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT   "Complete sequence of chromosome 1 of Verminephrobacter eiseniae EF01-2.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP000542; ABM60415.1; -; Genomic_DNA.
DR   RefSeq; WP_011812393.1; NC_008786.1.
DR   AlphaFoldDB; A1WS08; -.
DR   SMR; A1WS08; -.
DR   STRING; 391735.Veis_4720; -.
DR   EnsemblBacteria; ABM60415; ABM60415; Veis_4720.
DR   KEGG; vei:Veis_4720; -.
DR   eggNOG; COG0008; Bacteria.
DR   HOGENOM; CLU_015768_0_1_4; -.
DR   OMA; WLLRMED; -.
DR   OrthoDB; 1409413at2; -.
DR   Proteomes; UP000000374; 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:0006424; P:glutamyl-tRNA aminoacylation; IEA:InterPro.
DR   GO; GO:0006400; P:tRNA modification; IEA:InterPro.
DR   Gene3D; 3.40.50.620; -; 1.
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;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Zinc.
FT   CHAIN           1..292
FT                   /note="Glutamyl-Q tRNA(Asp) synthetase"
FT                   /id="PRO_1000024371"
FT   MOTIF           12..22
FT                   /note="'HIGH' region"
FT   MOTIF           240..244
FT                   /note="'KMSKS' region"
FT   BINDING         9..13
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   BINDING         45
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   BINDING         99
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   BINDING         101
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   BINDING         121
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   BINDING         125
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   BINDING         184
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   BINDING         202
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   BINDING         243
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
SQ   SEQUENCE   292 AA;  32088 MW;  C5B0F08AA026F545 CRC64;
     MQSAHYTGRF APSPSGPLHA GSLVAAMASY LDARAHQGRW LLRMEDVDEA RTVQGAAQDI
     AASLSQLGMH WDGPVLVQSR RQQHYQRACA QLGERVYACG CTRKEIADSR LGMAADGAAI
     YPGTCRSGLA AGKRAHALRV RVPEPGQALE QIDFEDRWQG WQRQHLASAV GDFVLRRADG
     FWAYQLAVVV DDAEQGVTHI VRGADLLGST ARQIYLQSLL GYPTPTYLHL PLVTHADGEK
     LSKQNGAQAL NLNRSLTLLH EAARFLGLEV ARVDGVAAFW ELAVLAWRRR YL