ID SYQ_BORBR Reviewed; 587 AA. AC Q7WGA6; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 27-MAR-2024, entry version 117. 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}; OrderedLocusNames=BB4013; OS Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) OS (Alcaligenes bronchisepticus). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=257310; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-588 / NCTC 13252 / RB50; RX PubMed=12910271; DOI=10.1038/ng1227; RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I., RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., RA Barrell B.G., Maskell D.J.; RT "Comparative analysis of the genome sequences of Bordetella pertussis, RT Bordetella parapertussis and Bordetella bronchiseptica."; RL Nat. Genet. 35:32-40(2003). 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; BX640449; CAE34376.1; -; Genomic_DNA. DR RefSeq; WP_010927011.1; NC_002927.3. DR AlphaFoldDB; Q7WGA6; -. DR SMR; Q7WGA6; -. DR KEGG; bbr:BB4013; -. DR eggNOG; COG0008; Bacteria. DR HOGENOM; CLU_001882_2_3_4; -. DR Proteomes; UP000001027; Chromosome. 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 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; 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..587 FT /note="Glutamine--tRNA ligase" FT /id="PRO_1000095479" FT MOTIF 58..68 FT /note="'HIGH' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT MOTIF 301..305 FT /note="'KMSKS' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 59..61 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 65..71 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 91 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 240 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 259 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 294..295 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" SQ SEQUENCE 587 AA; 66607 MW; 12A2583015C422BD CRC64; MTHAPTPPAA SNFLRPIIED DLQANRFQGK LWAGKPGPAA LQAQGQPDPA RIRTRFPPEP NGYLHIGHAK SICVNFGLAR DYGGVCHLRF DDTNPEKEEQ EYVDAIIEAV HWLGFDWQAD GNDNLYFASD YFEFMYEFAE ALVQAGHAYV DEQSAEEIRA SRGTLTEPGT DSPWRDRPAD ESLLRLREMR DGKHPDGSLV LRARIDMASP NINLRDPVMY RVRHATHHRT GNAWCIYPMY SWAHPVEDAL EGITHSICTL EFEDQRPFYD WILARLAELG KLARPLPHQY EFARLNLTYV VTSKRKLLQL VREGYVDGWD DPRMPTLFGL RRRGYTPSSI RLFCDRTAVS KSDSRIDYSL LEQAVRDDLD PVAPRSVAVL DPLKLVITNY PEGRSETCSA PRNPHDPQAG VREFPFTREL WIEQDDFREE PPKKYFRLFP GNTVRLKYGY VVRCTGFTKD QSGKVVEVQA EYLPDTKSGT PGADSVKVKG NITWVSAAHA VPAQVHLYDR LFADAHPDGG DKDFLACLNP HSKQTVQAWL EPGIEAVPGA TWQFERLGYF TVDSKDSRPE APVLNRIVTL RDSWQAA //