ID SYW_PSEAE Reviewed; 448 AA. AC Q9HVX6; DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 115. DE RecName: Full=Tryptophan--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00140}; DE EC=6.1.1.2 {ECO:0000255|HAMAP-Rule:MF_00140}; DE AltName: Full=Tryptophanyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00140}; DE Short=TrpRS {ECO:0000255|HAMAP-Rule:MF_00140}; GN Name=trpS {ECO:0000255|HAMAP-Rule:MF_00140}; OrderedLocusNames=PA4439; 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 -!- FUNCTION: Catalyzes the attachment of tryptophan to tRNA(Trp). CC {ECO:0000255|HAMAP-Rule:MF_00140}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L- CC tryptophanyl-tRNA(Trp); Xref=Rhea:RHEA:24080, Rhea:RHEA-COMP:9671, CC Rhea:RHEA-COMP:9705, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57912, ChEBI:CHEBI:78442, CC ChEBI:CHEBI:78535, ChEBI:CHEBI:456215; EC=6.1.1.2; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00140}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00140}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00140}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC {ECO:0000255|HAMAP-Rule:MF_00140}. 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; AAG07827.1; -; Genomic_DNA. DR PIR; A83091; A83091. DR RefSeq; NP_253129.1; NC_002516.2. DR RefSeq; WP_003112748.1; NZ_QZGE01000004.1. DR AlphaFoldDB; Q9HVX6; -. DR SMR; Q9HVX6; -. DR STRING; 208964.PA4439; -. DR PaxDb; 208964-PA4439; -. DR GeneID; 880958; -. DR KEGG; pae:PA4439; -. DR PATRIC; fig|208964.12.peg.4648; -. DR PseudoCAP; PA4439; -. DR HOGENOM; CLU_029244_5_1_6; -. DR InParanoid; Q9HVX6; -. DR OrthoDB; 9801042at2; -. DR PhylomeDB; Q9HVX6; -. DR BioCyc; PAER208964:G1FZ6-4527-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:0004830; F:tryptophan-tRNA ligase activity; IBA:GO_Central. DR GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IBA:GO_Central. DR CDD; cd00806; TrpRS_core; 1. DR Gene3D; 3.40.50.620; HUPs; 1. DR Gene3D; 1.10.240.10; Tyrosyl-Transfer RNA Synthetase; 1. DR HAMAP; MF_00140_B; Trp_tRNA_synth_B; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR002305; aa-tRNA-synth_Ic. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR002306; Trp-tRNA-ligase. DR InterPro; IPR024109; Trp-tRNA-ligase_bac-type. DR InterPro; IPR036913; YegP-like_sf. DR NCBIfam; TIGR00233; trpS; 1. DR PANTHER; PTHR43766; TRYPTOPHAN--TRNA LIGASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR43766:SF1; TRYPTOPHAN--TRNA LIGASE, MITOCHONDRIAL; 1. DR Pfam; PF00579; tRNA-synt_1b; 1. DR PRINTS; PR01039; TRNASYNTHTRP. DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1. DR SUPFAM; SSF160113; YegP-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..448 FT /note="Tryptophan--tRNA ligase" FT /id="PRO_0000136662" FT MOTIF 11..19 FT /note="'HIGH' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140" FT MOTIF 204..208 FT /note="'KMSKS' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140" FT BINDING 10..12 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140" FT BINDING 18..19 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140" FT BINDING 143 FT /ligand="L-tryptophan" FT /ligand_id="ChEBI:CHEBI:57912" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140" FT BINDING 155..157 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140" FT BINDING 197 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140" FT BINDING 204..208 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140" SQ SEQUENCE 448 AA; 48962 MW; FA82ECA10A049A84 CRC64; MTTRILTGIT PTGTPHLGNY AGAIRPAILA SRRSDVDSFY FLADYHALIK CDDPARIQRS RLEIAATWLA GGLDVERATF YRQSDIPEIP ELTWLLTCVS AKGLLNRAHA YKAAVDRNVE AGEDPDAGVT MGLYSYPVLM AADILMFNAH KIPVGRDQVQ HVEMARDIGQ RFNHLFGNGR EFFVLPEAVI EENVATLPGL DGRKMSKSYD NTIPLFSPSR QLKDAIARIV TDSRAPGEPK DPDSSHLFLL YSAFASAEQV AAFRQELLEG LAWGEAKQRL FQLLDNELGE ARERYQALIA KPDDIEDILL AGAAKARRIA TPFIAELREA VGLRSLREPL KSAESGKKKA AKAARLVSFR DDDGSFRFRL LDAAGEQLLL SRAFADGKAA GAVSKRLLAG ETADLRAEGN AFGLWLDGEA VAQSPAFADA AARDAAIERT REALAPQE //