ID SYQ_PSEAE Reviewed; 556 AA. AC Q9I2U8; DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 132. 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=PA1794; OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=208964; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / RC 1C / PRS 101 / PAO1; RX PubMed=10984043; DOI=10.1038/35023079; RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic RT pathogen."; RL Nature 406:959-964(2000). 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; AE004091; AAG05183.1; -; Genomic_DNA. DR PIR; F83421; F83421. DR RefSeq; NP_250485.1; NC_002516.2. DR RefSeq; WP_003113586.1; NZ_QZGE01000003.1. DR PDB; 5BNZ; X-ray; 1.90 A; A/B=1-556. DR PDBsum; 5BNZ; -. DR AlphaFoldDB; Q9I2U8; -. DR SMR; Q9I2U8; -. DR STRING; 208964.PA1794; -. DR PaxDb; 208964-PA1794; -. DR GeneID; 878828; -. DR KEGG; pae:PA1794; -. DR PATRIC; fig|208964.12.peg.1861; -. DR PseudoCAP; PA1794; -. DR HOGENOM; CLU_001882_2_3_6; -. DR InParanoid; Q9I2U8; -. DR OrthoDB; 9801560at2; -. DR PhylomeDB; Q9I2U8; -. DR BioCyc; PAER208964:G1FZ6-1826-MONOMER; -. DR Proteomes; UP000002438; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004819; F:glutamine-tRNA ligase activity; IBA:GO_Central. DR GO; GO:0006425; P:glutaminyl-tRNA aminoacylation; IBA:GO_Central. 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 1: Evidence at protein level; KW 3D-structure; 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_0000195843" 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" FT HELIX 12..22 FT /evidence="ECO:0007829|PDB:5BNZ" FT STRAND 30..33 FT /evidence="ECO:0007829|PDB:5BNZ" FT STRAND 37..39 FT /evidence="ECO:0007829|PDB:5BNZ" FT HELIX 43..58 FT /evidence="ECO:0007829|PDB:5BNZ" FT STRAND 62..67 FT /evidence="ECO:0007829|PDB:5BNZ" FT HELIX 76..89 FT /evidence="ECO:0007829|PDB:5BNZ" FT STRAND 95..97 FT /evidence="ECO:0007829|PDB:5BNZ" FT HELIX 101..104 FT /evidence="ECO:0007829|PDB:5BNZ" FT HELIX 105..117 FT /evidence="ECO:0007829|PDB:5BNZ" FT STRAND 121..124 FT /evidence="ECO:0007829|PDB:5BNZ" FT HELIX 128..135 FT /evidence="ECO:0007829|PDB:5BNZ" FT STRAND 138..140 FT /evidence="ECO:0007829|PDB:5BNZ" FT TURN 146..149 FT /evidence="ECO:0007829|PDB:5BNZ" FT HELIX 152..163 FT /evidence="ECO:0007829|PDB:5BNZ" FT STRAND 173..176 FT /evidence="ECO:0007829|PDB:5BNZ" FT HELIX 185..187 FT /evidence="ECO:0007829|PDB:5BNZ" FT STRAND 191..195 FT /evidence="ECO:0007829|PDB:5BNZ" FT TURN 201..203 FT /evidence="ECO:0007829|PDB:5BNZ" FT STRAND 208..211 FT /evidence="ECO:0007829|PDB:5BNZ" FT HELIX 213..224 FT /evidence="ECO:0007829|PDB:5BNZ" FT STRAND 227..232 FT /evidence="ECO:0007829|PDB:5BNZ" FT HELIX 233..238 FT /evidence="ECO:0007829|PDB:5BNZ" FT HELIX 239..248 FT /evidence="ECO:0007829|PDB:5BNZ" FT STRAND 256..260 FT /evidence="ECO:0007829|PDB:5BNZ" FT HELIX 272..280 FT /evidence="ECO:0007829|PDB:5BNZ" FT STRAND 283..286 FT /evidence="ECO:0007829|PDB:5BNZ" FT STRAND 292..294 FT /evidence="ECO:0007829|PDB:5BNZ" FT HELIX 295..301 FT /evidence="ECO:0007829|PDB:5BNZ" FT HELIX 305..315 FT /evidence="ECO:0007829|PDB:5BNZ" FT HELIX 327..340 FT /evidence="ECO:0007829|PDB:5BNZ" FT STRAND 346..355 FT /evidence="ECO:0007829|PDB:5BNZ" FT STRAND 363..370 FT /evidence="ECO:0007829|PDB:5BNZ" FT STRAND 372..374 FT /evidence="ECO:0007829|PDB:5BNZ" FT STRAND 378..390 FT /evidence="ECO:0007829|PDB:5BNZ" FT HELIX 391..393 FT /evidence="ECO:0007829|PDB:5BNZ" FT STRAND 410..413 FT /evidence="ECO:0007829|PDB:5BNZ" FT STRAND 418..426 FT /evidence="ECO:0007829|PDB:5BNZ" FT STRAND 432..440 FT /evidence="ECO:0007829|PDB:5BNZ" FT STRAND 460..462 FT /evidence="ECO:0007829|PDB:5BNZ" FT STRAND 466..473 FT /evidence="ECO:0007829|PDB:5BNZ" FT STRAND 476..481 FT /evidence="ECO:0007829|PDB:5BNZ" FT HELIX 491..494 FT /evidence="ECO:0007829|PDB:5BNZ" FT STRAND 499..508 FT /evidence="ECO:0007829|PDB:5BNZ" FT HELIX 510..514 FT /evidence="ECO:0007829|PDB:5BNZ" FT STRAND 520..523 FT /evidence="ECO:0007829|PDB:5BNZ" FT TURN 524..526 FT /evidence="ECO:0007829|PDB:5BNZ" FT STRAND 527..531 FT /evidence="ECO:0007829|PDB:5BNZ" FT TURN 533..535 FT /evidence="ECO:0007829|PDB:5BNZ" FT STRAND 543..547 FT /evidence="ECO:0007829|PDB:5BNZ" SQ SEQUENCE 556 AA; 62913 MW; EE75B1BB2C0A77F1 CRC64; MSKPETTAAP NFLRQIVQAD LDAGKHAKIV TRFPPEPNGY LHIGHAKSIC LNFGLAQEFA GDCHLRFDDT NPAKEDQEYI DAIEADIKWL GFQWSGEVCY ASNYFDQLHA WAVELIKAGK AFVCDLGPEE MREYRGTLTE PGRNSPYRDR SVEENLDLFA RMKAGEFPDG ARSLRAKIDM GSPNMNLRDP ILYRIRHAHH HQTGDKWCIY PSYDFTHGQS DAIEGITHSI CTLEFEDHRP LYEWFLANLP VPAQPRQYEF SRLNLNYTVT SKRKLKQLVD EGHVSGWDDP RMSTLSGYRR RGYTPESIRN FCEMIGVNRA SGVVDIGMLE FSIRDHLDAT APRAMCVLKP LKVVITNYPE GQVENLELPR HPKEDMGVRV LPFGRELFID AGDFEEVPPA GYKRLIPGGE VRLRGSYVIR ADEAIKDADG NIVELRCSYD PDTLGKNPEG RKVKGVIHWV PAEGSVECEV RLYDRLFRSA NPEKAEEGGS FLDNINADSL QVLAGCRAEP SLGQANPEDR FQFEREGYFV ADLKDSRPGK PVFNRTVTLR DSWGQG //