ID SYQ_AZOVD Reviewed; 555 AA. AC C1DHE5; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 26-MAY-2009, sequence version 1. DT 27-MAR-2024, entry version 80. 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=Avin_23520; OS Azotobacter vinelandii (strain DJ / ATCC BAA-1303). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Azotobacter. OX NCBI_TaxID=322710; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DJ / ATCC BAA-1303; RX PubMed=19429624; DOI=10.1128/jb.00504-09; RA Setubal J.C., Dos Santos P., Goldman B.S., Ertesvaag H., Espin G., RA Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L., RA Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A., RA Houmiel K., Imperial J., Kennedy C., Larson T.J., Latreille P., Ligon L.S., RA Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I., RA Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L., RA Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H., RA Dean D.R., Dixon R., Wood D.; RT "Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized RT to support diverse anaerobic metabolic processes."; RL J. Bacteriol. 191:4534-4545(2009). 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; CP001157; ACO78540.1; -; Genomic_DNA. DR RefSeq; WP_012700938.1; NC_012560.1. DR AlphaFoldDB; C1DHE5; -. DR SMR; C1DHE5; -. DR STRING; 322710.Avin_23520; -. DR EnsemblBacteria; ACO78540; ACO78540; Avin_23520. DR KEGG; avn:Avin_23520; -. DR eggNOG; COG0008; Bacteria. DR HOGENOM; CLU_001882_2_3_6; -. DR OrthoDB; 9801560at2; -. DR Proteomes; UP000002424; 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 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; 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..555 FT /note="Glutamine--tRNA ligase" FT /id="PRO_1000203120" FT MOTIF 35..45 FT /note="'HIGH' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT MOTIF 269..273 FT /note="'KMSKS' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 36..38 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 42..48 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 68 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 213 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 232 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 262..263 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" SQ SEQUENCE 555 AA; 62945 MW; 9F927F5515BFDF17 CRC64; MSKPETPAAA NFLRPIVQAD LESGKHAKIV TRFPPEPNGY LHIGHAKSIC LNFGLAQEFG GECNLRFDDT NPAKEDQEYI DAIKSDVRWL GFQWAGEERY ASSYFDQLYD WAIHLIEAGK AYVCDLSPDE AREYRGSLTE PGRNSPYRER SVEENLDLFA RMRAGEFPDG ARALRAKIDM AAPNMNLRDP ILYRIRHAHH HQTGDKWCIY PSYDFTHGQS DAIEGITHSI CTLEFEDHRP LYEWFLDNLP VPCRPRQYEF ARLNLNYTIT SKRKLKQLVD EGHVGGWDDP RMSTLSGYRR RGYTPASIRA FCDMIGVNRA GGVVDIGMLE FAIREDLDAN AARAMCVLKP LKVVITNYPQ GRVESLELPR HPKQDMGVRV LPFSREIYID AGDFEETPPA GYKRLIPGGE VRLRGSYVIR ADEAIKDEAG NIVELRCSYD ENTLGKNPEG RKVKGVIHWV PLEGSIKCEV RLYDRLFKVA NPEKSEEGGS FLDNINSGSL VVLTGCRAEP SLANARPEER FQFEREGYFC ADLKDSRPGA PVFNRTVTLR DSWGQ //