ID GLUQ_ECOLI Reviewed; 298 AA. AC P27305; P75662; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 5. DT 20-JAN-2009, entry version 83. 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; Enterobacteriales; 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 MEDLINE=94261430; 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 RT 2.4-4.1 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 MEDLINE=97426617; 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., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION RP TO 241-298. 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 RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-235. 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 1-35. RX MEDLINE=90202727; PubMed=2180916; RA Kang P.J., Craig E.A.; RT "Identification and characterization of a new Escherichia coli gene RT that is 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 RT the 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., RA Giege R., Cambillau C., Lapointe J., Kern D.; RT "An aminoacyl-tRNA synthetase-like protein encoded by the Escherichia RT coli 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), 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., RA Valencia C., Pagot F., Salomoni A., Grisel S., Vincentelli R., RA Bignon C., Lapointe J., 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) IN COMPLEX WITH GLUTAMATE AND RP 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 RT with L-glutamate: structural elements mediating tRNA-independent RT activation of glutamate and glutamylation of tRNAAsp anticodon."; RL J. Mol. Biol. 381:1224-1237(2008). CC -!- FUNCTION: Catalyzes the tRNA-independent activation of glutamate CC in presence of ATP and the subsequent transfer of glutamate onto CC tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5- CC dihydroxy-2-cyclopenten-1-yl) moiety of the queuosine in position CC 34 of the tRNA(Asp), the wobble position of the QUC anticodon. CC Does not transfer glutamate to either tRNA(Glu) or tRNA(Gln). The CC incapacity of the glutamylated tRNA(Asp) to bind elongation factor CC Tu suggests that it is not involved in ribosomal protein CC biosynthesis. CC -!- COFACTOR: 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 CC family. GluQ subfamily. CC -!- SEQUENCE CAUTION: CC Sequence=AAA23686.1; Type=Frameshift; Positions=Several; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00096; AAC73255.2; -; Genomic_DNA. DR EMBL; AP009048; BAB96721.2; ALT_INIT; 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; AP_000805.1; -. DR RefSeq; NP_414686.2; -. DR PDB; 1NZJ; X-ray; 1.50 A; A=1-298. DR PDB; 2ZLZ; X-ray; 1.75 A; A=1-298. DR PDBsum; 1NZJ; -. DR PDBsum; 2ZLZ; -. DR DIP; DIP:11180N; -. DR GeneID; 944846; -. DR GenomeReviews; AP009048_GR; JW5892. DR GenomeReviews; U00096_GR; b0144. DR KEGG; ecj:JW5892; -. DR KEGG; eco:b0144; -. DR EchoBASE; EB1337; -. DR EcoGene; EG11362; gluQ. DR HOGENOM; P27305; -. DR BioCyc; EcoCyc:EG11362-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:InterPro. DR HAMAP; MF_01428; -; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR000924; Glu/Gln-tRNA-synth_Ic. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1. DR PANTHER; PTHR10119; Glu_tRNA-synt_1c; 1. DR Pfam; PF00749; tRNA-synt_1c; 1. DR PRINTS; PR00987; TRNASYNTHGLU. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; FALSE_NEG. PE 1: Evidence at protein level; KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; KW Complete proteome; Ligase; Metal-binding; Nucleotide-binding; Zinc. FT CHAIN 1 298 Glutamyl-Q tRNA(Asp) synthetase. FT /FTId=PRO_0000208300. FT REGION 9 13 Glutamate binding. FT MOTIF 12 22 "HIGH" region. FT MOTIF 228 232 "KMSKS" region. FT METAL 101 101 Zinc. FT METAL 103 103 Zinc. FT METAL 115 115 Zinc. FT METAL 119 119 Zinc. FT BINDING 45 45 Glutamate. FT BINDING 172 172 Glutamate. FT BINDING 190 190 Glutamate. FT BINDING 231 231 ATP (By similarity). FT CONFLICT 241 298 GDPRPVLIAALQFLGQQAEAHWQDFSVEQILQSAVKNWRLT FT AVPESAIVNSTFSNASC -> AIHARY (in Ref. 1). FT STRAND 7 10 FT HELIX 20 35 FT STRAND 39 44 FT HELIX 49 51 FT HELIX 56 66 FT HELIX 78 80 FT HELIX 82 94 FT STRAND 98 101 FT HELIX 105 110 FT TURN 118 122 FT STRAND 130 133 FT STRAND 141 144 FT TURN 145 147 FT STRAND 148 151 FT HELIX 154 158 FT STRAND 162 164 FT HELIX 172 182 FT STRAND 187 191 FT HELIX 192 194 FT TURN 195 197 FT HELIX 198 208 FT STRAND 214 218 FT HELIX 244 253 FT HELIX 262 264 FT HELIX 267 276 FT HELIX 280 282 FT STRAND 287 289 SQ SEQUENCE 298 AA; 33601 MW; 1FCD56BA7EC94ED1 CRC64; 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 //