ID SYQ_VIBPA Reviewed; 556 AA. AC Q87RG4; DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot. DT 23-MAY-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=VP0832; OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Vibrio. OX NCBI_TaxID=223926; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RIMD 2210633; RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1; RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.; RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism RT distinct from that of V. cholerae."; RL Lancet 361:743-749(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; BA000031; BAC59095.1; -; Genomic_DNA. DR RefSeq; NP_797211.1; NC_004603.1. DR RefSeq; WP_005454579.1; NC_004603.1. DR AlphaFoldDB; Q87RG4; -. DR SMR; Q87RG4; -. DR GeneID; 1188329; -. DR KEGG; vpa:VP0832; -. DR PATRIC; fig|223926.6.peg.788; -. DR eggNOG; COG0008; Bacteria. DR HOGENOM; CLU_001882_2_3_6; -. DR Proteomes; UP000002493; Chromosome 1. 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; Reference proteome. FT CHAIN 1..556 FT /note="Glutamine--tRNA ligase" FT /id="PRO_0000195853" 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 556 AA; 63969 MW; 355B526332146B44 CRC64; MSEADARPSN FIRQIIDKDL ADGKHTSVHT RFPPEPNGYL HIGHAKSICL NFGIAQDYQG QCNLRFDDTN PEKEDIEYVE SIKKDVNWLG FEWDGEVCYS SNYFDKLYEY AIELINKGLA YVDELSPEQI REYRGTLKEP GKPSPYRDRS VEENLALFEK MRAGEFEEGK ACLRAKIDMG SSFMVMRDPV LYRVRFATHH QTGDKWCIYP MYDFTHCISD ALEGITHSIC TLEFMDNRRL YDWVLDNITI DCRPHQYEFS RLNLEYTVMS KRKLNQLVTE KLVNGWDDPR MPTVSGLRRR GFTPASIREF CKRIGVTKQE NMIEFSSLES CIRDDLNENA PRAMAVLDPV KVVIENFEVG AVENLTLANH PNKPEMGERE VPFTREVWIE REDFREEANK KYKRLVLGKE VRLRGAYVIK AERVEKDAEG NITTIYCTYD PETLGKNPAD GRKVKGVIHW VSADKALPAE IRLYDRLFTV PNPAAAEDFA STINTDSLVV INGFVEPSLA SAEAEQGYQF ERMGYFCADS KDSTADNLVF NRTVGLRDTW AKIENQ //