GLUQ_ECOLI
ID GLUQ_ECOLI Reviewed; 308 AA.
AC P27305; P75662;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 6.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Glutamyl-Q tRNA(Asp) synthetase;
DE Short=Glu-Q-RSs;
DE EC=6.1.1.-;
GN Name=gluQ; Synonyms=yadB; OrderedLocusNames=b0144, JW5892;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8202364; DOI=10.1093/nar/22.9.1637;
RA Fujita N., Mori H., Yura T., Ishihama A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-
RT 4.1 min (110,917-193,643 bp) region.";
RL Nucleic Acids Res. 22:1637-1639(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP 251-308.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 46-245.
RC STRAIN=K12;
RA Masters M.;
RL Submitted (MAR-1992) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
RX PubMed=2180916; DOI=10.1128/jb.172.4.2055-2064.1990;
RA Kang P.J., Craig E.A.;
RT "Identification and characterization of a new Escherichia coli gene that is
RT a dosage-dependent suppressor of a dnaK deletion mutation.";
RL J. Bacteriol. 172:2055-2064(1990).
RN [6]
RP FUNCTION.
RX PubMed=15150343; DOI=10.1093/nar/gkh608;
RA Blaise M., Becker H.D., Keith G., Cambillau C., Lapointe J., Giege R.,
RA Kern D.;
RT "A minimalist glutamyl-tRNA synthetase dedicated to aminoacylation of the
RT tRNAAsp QUC anticodon.";
RL Nucleic Acids Res. 32:2768-2775(2004).
RN [7]
RP FUNCTION.
RX PubMed=15096594; DOI=10.1073/pnas.0401634101;
RA Dubois D.Y., Blaise M., Becker H.D., Campanacci V., Keith G., Giege R.,
RA Cambillau C., Lapointe J., Kern D.;
RT "An aminoacyl-tRNA synthetase-like protein encoded by the Escherichia coli
RT yadB gene glutamylates specifically tRNAAsp.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7530-7535(2004).
RN [8]
RP FUNCTION.
RX PubMed=15096612; DOI=10.1073/pnas.0401982101;
RA Salazar J.C., Ambrogelly A., Crain P.F., McCloskey J.A., Soell D.;
RT "A truncated aminoacyl-tRNA synthetase modifies RNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7536-7541(2004).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 10-308, AND ZINC-BINDING SITE.
RX PubMed=15003446; DOI=10.1016/j.jmb.2004.01.027;
RA Campanacci V., Dubois D.Y., Becker H.D., Kern D., Spinelli S., Valencia C.,
RA Pagot F., Salomoni A., Grisel S., Vincentelli R., Bignon C., Lapointe J.,
RA Giege R., Cambillau C.;
RT "The Escherichia coli YadB gene product reveals a novel aminoacyl-tRNA
RT synthetase like activity.";
RL J. Mol. Biol. 337:273-283(2004).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 10-308 IN COMPLEX WITH GLUTAMATE
RP AND ZINC IONS.
RX PubMed=18602926; DOI=10.1016/j.jmb.2008.06.053;
RA Blaise M., Olieric V., Sauter C., Lorber B., Roy B., Karmakar S.,
RA Banerjee R., Becker H.D., Kern D.;
RT "Crystal structure of glutamyl-queuosine tRNAAsp synthetase complexed with
RT L-glutamate: structural elements mediating tRNA-independent activation of
RT glutamate and glutamylation of tRNAAsp anticodon.";
RL J. Mol. Biol. 381:1224-1237(2008).
CC -!- FUNCTION: Catalyzes the tRNA-independent activation of glutamate in
CC presence of ATP and the subsequent transfer of glutamate onto
CC tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2-
CC cyclopenten-1-yl) moiety of the queuosine in position 34 of the
CC tRNA(Asp), the wobble position of the QUC anticodon. Does not transfer
CC glutamate to either tRNA(Glu) or tRNA(Gln). The incapacity of the
CC glutamylated tRNA(Asp) to bind elongation factor Tu suggests that it is
CC not involved in ribosomal protein biosynthesis.
CC {ECO:0000269|PubMed:15096594, ECO:0000269|PubMed:15096612,
CC ECO:0000269|PubMed:15150343}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 zinc ion per subunit.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.15 uM for tRNA(Asp);
CC KM=3000 uM for glutamate;
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC GluQ subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA23686.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U00096; AAC73255.3; -; Genomic_DNA.
DR EMBL; AP009048; BAB96721.2; -; Genomic_DNA.
DR EMBL; X64595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M34945; AAA23686.1; ALT_SEQ; Genomic_DNA.
DR PIR; H64737; H64737.
DR RefSeq; NP_414686.3; NC_000913.3.
DR RefSeq; WP_000937424.1; NZ_STEB01000010.1.
DR PDB; 1NZJ; X-ray; 1.50 A; A=11-308.
DR PDB; 4A91; X-ray; 1.75 A; A=11-308.
DR PDBsum; 1NZJ; -.
DR PDBsum; 4A91; -.
DR AlphaFoldDB; P27305; -.
DR SMR; P27305; -.
DR BioGRID; 4259736; 6.
DR DIP; DIP-11180N; -.
DR IntAct; P27305; 6.
DR STRING; 511145.b0144; -.
DR jPOST; P27305; -.
DR PaxDb; P27305; -.
DR PRIDE; P27305; -.
DR EnsemblBacteria; AAC73255; AAC73255; b0144.
DR EnsemblBacteria; BAB96721; BAB96721; BAB96721.
DR GeneID; 944846; -.
DR KEGG; ecj:JW5892; -.
DR KEGG; eco:b0144; -.
DR PATRIC; fig|1411691.4.peg.2137; -.
DR EchoBASE; EB1337; -.
DR eggNOG; COG0008; Bacteria.
DR HOGENOM; CLU_015768_0_1_6; -.
DR InParanoid; P27305; -.
DR OMA; WLLRMED; -.
DR PhylomeDB; P27305; -.
DR BioCyc; EcoCyc:EG11362-MON; -.
DR BioCyc; MetaCyc:EG11362-MON; -.
DR BRENDA; 6.1.1.B3; 2026.
DR SABIO-RK; P27305; -.
DR EvolutionaryTrace; P27305; -.
DR PRO; PR:P27305; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IDA:EcoCyc.
DR GO; GO:0004818; F:glutamate-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IBA:GO_Central.
DR GO; GO:0002097; P:tRNA wobble base modification; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Ligase;
KW Metal-binding; Nucleotide-binding; Reference proteome; Zinc.
FT CHAIN 1..308
FT /note="Glutamyl-Q tRNA(Asp) synthetase"
FT /id="PRO_0000208300"
FT MOTIF 22..32
FT /note="'HIGH' region"
FT MOTIF 238..242
FT /note="'KMSKS' region"
FT BINDING 19..23
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT BINDING 55
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:18602926"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 182
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:18602926"
FT BINDING 200
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:18602926"
FT BINDING 241
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:1NZJ"
FT HELIX 30..45
FT /evidence="ECO:0007829|PDB:1NZJ"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:1NZJ"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:1NZJ"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:1NZJ"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:1NZJ"
FT HELIX 92..104
FT /evidence="ECO:0007829|PDB:1NZJ"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:1NZJ"
FT HELIX 115..120
FT /evidence="ECO:0007829|PDB:1NZJ"
FT TURN 128..132
FT /evidence="ECO:0007829|PDB:1NZJ"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:1NZJ"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:1NZJ"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:1NZJ"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:1NZJ"
FT HELIX 164..168
FT /evidence="ECO:0007829|PDB:1NZJ"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:1NZJ"
FT HELIX 182..192
FT /evidence="ECO:0007829|PDB:1NZJ"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:1NZJ"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:1NZJ"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:1NZJ"
FT HELIX 208..218
FT /evidence="ECO:0007829|PDB:1NZJ"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:1NZJ"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:4A91"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:4A91"
FT HELIX 254..263
FT /evidence="ECO:0007829|PDB:1NZJ"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:1NZJ"
FT HELIX 277..286
FT /evidence="ECO:0007829|PDB:1NZJ"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:1NZJ"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:1NZJ"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:4A91"
SQ SEQUENCE 308 AA; 34868 MW; 69BA4A164AB4363C CRC64;
MLPPYFLFKE MTDTQYIGRF APSPSGELHF GSLIAALGSY LQARARQGRW LVRIEDIDPP
REVPGAAETI LRQLEHYGLH WDGDVLWQSQ RHDAYREALA WLHEQGLSYY CTCTRARIQS
IGGIYDGHCR VLHHGPDNAA VRIRQQHPVT QFTDQLRGII HADEKLARED FIIHRRDGLF
AYNLAVVVDD HFQGVTEIVR GADLIEPTVR QISLYQLFGW KVPDYIHLPL ALNPQGAKLS
KQNHAPALPK GDPRPVLIAA LQFLGQQAEA HWQDFSVEQI LQSAVKNWRL TAVPESAIVN
STFSNASC
