ID SYQ_ECO5E Reviewed; 554 AA. AC B5YQM4; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 1. DT 27-MAR-2024, entry version 84. DE RecName: Full=Glutamine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00126}; DE EC=6.1.1.18 {ECO:0000255|HAMAP-Rule:MF_00126}; DE AltName: Full=Glutaminyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00126}; DE Short=GlnRS {ECO:0000255|HAMAP-Rule:MF_00126}; GN Name=glnS {ECO:0000255|HAMAP-Rule:MF_00126}; GN OrderedLocusNames=ECH74115_0773; OS Escherichia coli O157:H7 (strain EC4115 / EHEC). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=444450; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EC4115 / EHEC; RX PubMed=22135463; DOI=10.1073/pnas.1107176108; RA Eppinger M., Mammel M.K., Leclerc J.E., Ravel J., Cebula T.A.; RT "Genomic anatomy of Escherichia coli O157:H7 outbreaks."; RL Proc. Natl. Acad. Sci. U.S.A. 108:20142-20147(2011). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L- CC glutaminyl-tRNA(Gln); Xref=Rhea:RHEA:20121, Rhea:RHEA-COMP:9662, CC Rhea:RHEA-COMP:9681, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:58359, ChEBI:CHEBI:78442, ChEBI:CHEBI:78521, CC ChEBI:CHEBI:456215; EC=6.1.1.18; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00126}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00126}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00126}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC {ECO:0000255|HAMAP-Rule:MF_00126}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001164; ACI37757.1; -; Genomic_DNA. DR RefSeq; WP_001287136.1; NC_011353.1. DR AlphaFoldDB; B5YQM4; -. DR SMR; B5YQM4; -. DR KEGG; ecf:ECH74115_0773; -. DR HOGENOM; CLU_001882_2_3_6; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004819; F:glutamine-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006425; P:glutaminyl-tRNA aminoacylation; IEA:InterPro. DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR CDD; cd00807; GlnRS_core; 1. DR Gene3D; 3.40.50.620; HUPs; 1. DR HAMAP; MF_00126; Gln_tRNA_synth; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR004514; Gln-tRNA-synth. DR InterPro; IPR022861; Gln_tRNA_ligase_bac. DR InterPro; IPR000924; Glu/Gln-tRNA-synth. DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom. DR InterPro; IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd. DR InterPro; IPR020061; Glu_tRNA_lig_a-bdl. DR InterPro; IPR020056; Rbsml_bL25/Gln-tRNA_synth_N. DR InterPro; IPR011035; Ribosomal_bL25/Gln-tRNA_synth. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR049437; tRNA-synt_1c_C2. DR NCBIfam; TIGR00440; glnS; 1. DR PANTHER; PTHR43097:SF4; GLUTAMINE--TRNA LIGASE; 1. DR PANTHER; PTHR43097; GLUTAMINE-TRNA LIGASE; 1. DR Pfam; PF00749; tRNA-synt_1c; 1. DR Pfam; PF03950; tRNA-synt_1c_C; 1. DR Pfam; PF20974; tRNA-synt_1c_C2; 1. DR PRINTS; PR00987; TRNASYNTHGLU. DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1. DR SUPFAM; SSF50715; Ribosomal protein L25-like; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; KW Nucleotide-binding; Protein biosynthesis. FT CHAIN 1..554 FT /note="Glutamine--tRNA ligase" FT /id="PRO_1000095488" FT REGION 317..324 FT /note="Interaction with tRNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT MOTIF 34..44 FT /note="'HIGH' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT MOTIF 268..272 FT /note="'KMSKS' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 35..37 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 41..47 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 67 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 212 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 231 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 261..262 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 269..271 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" SQ SEQUENCE 554 AA; 63510 MW; A484939DB8B4EC67 CRC64; MSEAEARPTN FIRQIIDEDL ASGKHTTVHT RFPPEPNGYL HIGHAKSICL NFGIAQDYKG QCNLRFDDTN PVKEDIEYVD SIKNDVEWLG FHWSGNVRYS SDYFDQLHAY AIELINKGLA YVDELTPEQI REYRGTLTQP GKNSPYRDRS VEENLALFEK MRTGGFEEGK ACLRAKIDMA SPFIVMRDPV LYRIKFAEHH QTGNKWCIYP MYDFTHCISD ALEGITHSLC TLEFQDNRRL YDWVLDNITI PVHPRQYEFS RLNLEYTVMS KRKLNLLVTD KHVEGWDDPR MPTISGLRRR GYTAASIREF CKRIGVTKQD NTIEMASLES CIREDLNENA PRAMAVIDPV KLVIENYQGE GEMVTMPNHP NKPEMGSRQV PFSGEIWIDR SDFREEANKQ YKRLVLGKEV RLRNAYVIKA ERVEKDAEGN ITTIFCTYDA DTLSKDPADG RKVKGVIHWV SAAHALPVEI RLYDRLFSVP NPGAADDFLS VINPESLVIK QGFAEPSLKD AVAGKAFQFE REGYFCLDSR HSTAEKPVFN RTVGLRDTWA KVGE //