ID SYW_PSEPK Reviewed; 449 AA. AC Q88NA1; DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 113. 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}; GN OrderedLocusNames=PP_1311; OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 OS / KT2440). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=160488; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440; RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x; RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H., RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M., RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F., RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I., RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A., RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H., RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C., RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.; RT "Complete genome sequence and comparative analysis of the metabolically RT versatile Pseudomonas putida KT2440."; RL Environ. Microbiol. 4:799-808(2002). 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; AE015451; AAN66935.1; -; Genomic_DNA. DR RefSeq; NP_743471.1; NC_002947.4. DR RefSeq; WP_010952434.1; NC_002947.4. DR AlphaFoldDB; Q88NA1; -. DR SMR; Q88NA1; -. DR STRING; 160488.PP_1311; -. DR PaxDb; 160488-PP_1311; -. DR GeneID; 83682255; -. DR KEGG; ppu:PP_1311; -. DR PATRIC; fig|160488.4.peg.1390; -. DR eggNOG; COG0180; Bacteria. DR HOGENOM; CLU_029244_5_1_6; -. DR OrthoDB; 9801042at2; -. DR PhylomeDB; Q88NA1; -. DR BioCyc; PPUT160488:G1G01-1398-MONOMER; -. DR Proteomes; UP000000556; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004830; F:tryptophan-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR CDD; cd00806; TrpRS_core; 1. DR Gene3D; 2.30.29.80; -; 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; 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. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1..449 FT /note="Tryptophan--tRNA ligase" FT /id="PRO_0000136663" 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 449 AA; 49298 MW; 2A1135E6EF4F1E7C CRC64; MTTRILTGIT TTGTPHLGNY AGAIRPAIRA SQQPGVDSFY FLADYHALIK CDDPLRIQRS RLEIAATWLA GGLDPDKVTF YRQSDIPEIP ELTWLLTCVA AKGLLNRAHA YKASVDKNVE NGEDPDAGVT MGLFSYPVLM AADILMFNAN KVPVGRDQIQ HVEMARDIGQ RFNHLFGQGK DFFALPEAVI EESVATLPGL DGRKMSKSYD NTIPLFTSAK DMKDAISRIV TDSRAPGEAK DPDNAHLFTL YQAFSTPEQC AGFREELLQG LGWGDAKQRL FQLLDGQLAE KREYYHQLIA RPADLEDILL AGAAKARKIA TPFLEQLREA VGLRSFRSSV QATAEVKKKA TKSARFVSFR DEDGSFRFRL LAADGEQLLL SRSFADGKSA GAVSKQLQQG GEADVRIEGL SFGLWLNGEQ VADGPQFDNA EARDAAIQSL NEALAPQQD //