ID SYQ_XANOR Reviewed; 579 AA. AC Q5GWF4; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 27-MAR-2024, entry version 108. 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=XOO3713; OS Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=291331; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KACC10331 / KXO85; RX PubMed=15673718; DOI=10.1093/nar/gki206; RA Lee B.-M., Park Y.-J., Park D.-S., Kang H.-W., Kim J.-G., Song E.-S., RA Park I.-C., Yoon U.-H., Hahn J.-H., Koo B.-S., Lee G.-B., Kim H., RA Park H.-S., Yoon K.-O., Kim J.-H., Jung C.-H., Koh N.-H., Seo J.-S., RA Go S.-J.; RT "The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the RT bacterial blight pathogen of rice."; RL Nucleic Acids Res. 33:577-586(2005). 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; AE013598; AAW76967.1; -; Genomic_DNA. DR AlphaFoldDB; Q5GWF4; -. DR SMR; Q5GWF4; -. DR STRING; 291331.XOO3713; -. DR KEGG; xoo:XOO3713; -. DR HOGENOM; CLU_001882_2_3_6; -. DR Proteomes; UP000006735; 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; 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; Reference proteome. FT CHAIN 1..579 FT /note="Glutamine--tRNA ligase" FT /id="PRO_0000242882" FT MOTIF 41..51 FT /note="'HIGH' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT MOTIF 292..296 FT /note="'KMSKS' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 42..44 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 48..54 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 74 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 218 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 237 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 285..286 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" FT BINDING 293..295 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00126" SQ SEQUENCE 579 AA; 65668 MW; F01C8EEEB9994A80 CRC64; MSETLATDAT TPAEKKDFIR QIVREDLASG KHTVIRTRFP PEPNGYLHIG HAKAICLDFG LAAEFGGLCN LRLDDTNPAK EDPEFAAAIQ DDVRWLGYDW AQLRHASDYF EVYYLAAQKL IRDGHAFVCD LSAEQVRQYR GTLTEPGRHS PFRERSVEEN LDLFQRMRAG EFPDGARTLR AKIDMASGNI NLRDPALYRI KHVEHQNTGN AWPIYPMYDF AHSLGDAVEG ITHSLCTLEF EDHRPLYDWC VDKVDLVGHP ELLQPLLDKG LPREAAKPRQ IEFSRLNINY TVMSKRKLTA LVEEQLVDGW DDPRMYTLQG LRRRGYTPAA MRLFVERVGI SKQNSLIDFS VLEGCLREDL DAAAARRMAV IDPLKLVLTN LPEGHTETLQ FSNHPKDESF GTREVPFARV LWIEREDFAE VPPKGWKRLV PGGEIRLRGA GIARVDEVIK NADGDIVALR GWLDPESRPG MEGANRKVKG TIHWVSAAHA VEAEIRLYDR LFSVEKPDDE SEGKTYRDYL NPESKRNVRG YVEPSAALAA PEQAFQFERT GYFVADSRDH SASTPVFNRS VTLRDAWAK //