GLUQ_KLEP3
ID GLUQ_KLEP3 Reviewed; 293 AA.
AC B5Y1P2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=KPK_4592;
OS Klebsiella pneumoniae (strain 342).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=507522;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=342;
RX PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA Methe B.A.;
RT "Complete genome sequence of the N2-fixing broad host range endophyte
RT Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL PLoS Genet. 4:E1000141-E1000141(2008).
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; CP000964; ACI08023.1; -; Genomic_DNA.
DR AlphaFoldDB; B5Y1P2; -.
DR SMR; B5Y1P2; -.
DR EnsemblBacteria; ACI08023; ACI08023; KPK_4592.
DR KEGG; kpe:KPK_4592; -.
DR HOGENOM; CLU_015768_0_1_6; -.
DR OMA; WLLRMED; -.
DR OrthoDB; 1409413at2; -.
DR Proteomes; UP000001734; 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..293
FT /note="Glutamyl-Q tRNA(Asp) synthetase"
FT /id="PRO_1000145741"
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 293 AA; 32976 MW; 69B569C95873D847 CRC64;
MTDSRYIGRF APSPSGELHF GSLIAALGSY LQARANQGIW RVRIEDIDPP REVPGAADTI
LRQLDHYGLH WDGDVLWQSQ RHEAYREALA WLGEQGLSYY CTCTRARIHA VGGIYDGHCR
DLGLGAENAA LRLRQTRPVL QFTDRLHGTL IANEPLARED FIIHRRDGLF AYNLAVVVDD
HFQGITEIVR GADLIEPTVR QISLYQHFGW QAPDYLHLPL ALNADGNKLS KQNHAPALPE
GDPRPEIVRA LRFLNQDIAQ DWQALSMDDL LSQAVANWQP AKIEHSQMAP AEL
