ID   GLUQ_SALPA              Reviewed;         298 AA.
AC   Q5PD33;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=SPA0191;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV76224.1; -; Genomic_DNA.
DR   RefSeq; WP_001667835.1; NC_006511.1.
DR   AlphaFoldDB; Q5PD33; -.
DR   SMR; Q5PD33; -.
DR   EnsemblBacteria; AAV76224; AAV76224; SPA0191.
DR   KEGG; spt:SPA0191; -.
DR   HOGENOM; CLU_015768_0_1_6; -.
DR   OMA; WLLRMED; -.
DR   Proteomes; UP000008185; 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; Zinc.
FT   CHAIN           1..298
FT                   /note="Glutamyl-Q tRNA(Asp) synthetase"
FT                   /id="PRO_0000208323"
FT   MOTIF           12..22
FT                   /note="'HIGH' region"
FT   MOTIF           228..232
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         101
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   BINDING         103
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   BINDING         115
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   BINDING         119
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   BINDING         172
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   BINDING         190
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT   BINDING         231
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
SQ   SEQUENCE   298 AA;  33597 MW;  D1A2A70C54F59977 CRC64;
     MTDSHYIGRF APSPSGELHF GSLIAALGSY LQARAQRGIW RVRIEDIDPP REVPGAAATI
     LRQLEHYGLH WDGEVLWQSQ RHEAYREALA WLHEQGLSYY CTCPRSRIQR LGGIYDGHCR
     TLCHGPENAA VRIKQQHPVM HFHDALRGDI QADPQLASED FIIHRRDGLF AYNLAVVVDD
     HFQGVTEIVR GADLIEPTVR QLSLYKQFGW RAPGYVHLPL ALNEQGAKLS KQNHAPALAT
     GDPRPVLVQA LRFLGQRDVV AWQEMSVEEL LRFAVTHWRL TAVPTSANVN PAFSNASR