GLUQ_NEIMF
ID GLUQ_NEIMF Reviewed; 295 AA.
AC A1KVT5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=NMC1820;
OS Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM
OS 15464 / FAM18).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=272831;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700532 / DSM 15464 / FAM18;
RX PubMed=17305430; DOI=10.1371/journal.pgen.0030023;
RA Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C.,
RA Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K.,
RA Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S.,
RA Quail M.A., Achtman M., Barrell B.G., Saunders N.J., Parkhill J.;
RT "Meningococcal genetic variation mechanisms viewed through comparative
RT analysis of serogroup C strain FAM18.";
RL PLoS Genet. 3:230-240(2007).
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; AM421808; CAM10990.1; -; Genomic_DNA.
DR RefSeq; WP_002220294.1; NC_008767.1.
DR AlphaFoldDB; A1KVT5; -.
DR SMR; A1KVT5; -.
DR EnsemblBacteria; CAM10990; CAM10990; NMC1820.
DR KEGG; nmc:NMC1820; -.
DR HOGENOM; CLU_015768_0_1_4; -.
DR OMA; WLLRMED; -.
DR OrthoDB; 1409413at2; -.
DR Proteomes; UP000002286; 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..295
FT /note="Glutamyl-Q tRNA(Asp) synthetase"
FT /id="PRO_1000024358"
FT MOTIF 8..18
FT /note="'HIGH' region"
FT MOTIF 234..238
FT /note="'KMSKS' region"
FT BINDING 5..9
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT BINDING 41
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
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 117
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 178
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT BINDING 196
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT BINDING 237
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
SQ SEQUENCE 295 AA; 32987 MW; 94FE20EC7DADB334 CRC64;
MYTGRFAPSP TGLLHIGSLL TAAASYADAR SNGGKWLVRM EDLDPPREMP GAASHILHTL
EAFGFEWDGE VAYQSRRYAL YEETLCRLQT AGLVYPCHCS RKDWQAAAVH GADGFVYNGR
CRNPQQRPAL QGKQPAWRIR VPDRDIGFSD GIVGGYAQNL ARDIGDFVLL RADGYWAYQL
AVVADDAEQG VTHIVRGQDL LVSTPRQIYL QQCLGVPTPQ YAHLPLLTNA QGQKWSKQTL
APALDLNRRE QLLRQVFRYL KLPEAPETDR PAELLDWAVA HWDMGKVPKH AITTP
