GLUQ_YERPE
ID GLUQ_YERPE Reviewed; 321 AA.
AC Q8ZBL1; Q0WBP8; Q74XU5; Q8D1A9;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
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};
GN OrderedLocusNames=YPO3398, y0789, YP_0287;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM84376.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAS60562.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL590842; CAL21987.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM84376.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE017042; AAS60562.1; ALT_INIT; Genomic_DNA.
DR PIR; AH0412; AH0412.
DR RefSeq; WP_002228220.1; NZ_WHLN01000005.1.
DR RefSeq; YP_002348290.1; NC_003143.1.
DR AlphaFoldDB; Q8ZBL1; -.
DR SMR; Q8ZBL1; -.
DR STRING; 214092.YPO3398; -.
DR PaxDb; Q8ZBL1; -.
DR EnsemblBacteria; AAM84376; AAM84376; y0789.
DR EnsemblBacteria; AAS60562; AAS60562; YP_0287.
DR GeneID; 57975311; -.
DR KEGG; ype:YPO3398; -.
DR KEGG; ypk:y0789; -.
DR KEGG; ypm:YP_0287; -.
DR PATRIC; fig|1028802.3.peg.1608; -.
DR eggNOG; COG0008; Bacteria.
DR HOGENOM; CLU_015768_0_1_6; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; 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..321
FT /note="Glutamyl-Q tRNA(Asp) synthetase"
FT /id="PRO_0000208339"
FT MOTIF 28..38
FT /note="'HIGH' region"
FT MOTIF 244..248
FT /note="'KMSKS' region"
FT BINDING 25..29
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT BINDING 61
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
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 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT BINDING 188
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT BINDING 206
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT BINDING 247
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
SQ SEQUENCE 321 AA; 36310 MW; B31685CC82FF74F9 CRC64;
MVQQAVIQRS ANQRATNQPT EYIGRFAPSP SGDLHFGSLI AALGSYLQAR AQGGKWLVRI
EDIDPPREVP GAASRILAAL EHYGLHWDGP VIYQSQRHEA YRATLNWLEQ QGLSYYCTCT
RSRIHQLGGF YDGYCRDRHL PASGAAIRLR QTQPVYAFYD KLLGELHAHP ALAQEDFIIR
RRDGLFAYNL AVVVDDAFQG VTEIVRGADL IEPTVRQIAL YQQLQHPVPG YIHLPLALNN
QGNKLSKQNH APPLPNGDPR PILIDALKFL RQPLPEYWQD LDLYLLLRYA VKHWTLVSIP
LQGAITPQKT QRHSQSKYGE L
