GLUQ_SALTY
ID GLUQ_SALTY Reviewed; 298 AA.
AC Q8ZRQ7;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 113.
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=STM0185;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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=AAL19149.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE006468; AAL19149.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_459190.3; NC_003197.2.
DR AlphaFoldDB; Q8ZRQ7; -.
DR SMR; Q8ZRQ7; -.
DR STRING; 99287.STM0185; -.
DR PaxDb; Q8ZRQ7; -.
DR EnsemblBacteria; AAL19149; AAL19149; STM0185.
DR GeneID; 1251703; -.
DR KEGG; stm:STM0185; -.
DR PATRIC; fig|99287.12.peg.195; -.
DR HOGENOM; CLU_015768_0_1_6; -.
DR OMA; WLLRMED; -.
DR PhylomeDB; Q8ZRQ7; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004818; F:glutamate-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IBA:GO_Central.
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..298
FT /note="Glutamyl-Q tRNA(Asp) synthetase"
FT /id="PRO_0000208325"
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; 33567 MW; 24A2A70C54F58276 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 LRFAVAHWRL TAVPTSANVN PAFSNASR
