ID   SYW_AQUAE               Reviewed;         395 AA.
AC   O67115;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 126.
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=aq_992;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
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}.
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DR   EMBL; AE000657; AAC07073.1; -; Genomic_DNA.
DR   PIR; H70385; H70385.
DR   RefSeq; NP_213678.1; NC_000918.1.
DR   RefSeq; WP_010880616.1; NC_000918.1.
DR   AlphaFoldDB; O67115; -.
DR   SMR; O67115; -.
DR   STRING; 224324.aq_992; -.
DR   PRIDE; O67115; -.
DR   EnsemblBacteria; AAC07073; AAC07073; aq_992.
DR   KEGG; aae:aq_992; -.
DR   PATRIC; fig|224324.8.peg.778; -.
DR   eggNOG; COG0180; Bacteria.
DR   HOGENOM; CLU_029244_0_0_0; -.
DR   InParanoid; O67115; -.
DR   OMA; GWGQFKP; -.
DR   OrthoDB; 951354at2; -.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; 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; -; 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   Pfam; PF00579; tRNA-synt_1b; 2.
DR   PRINTS; PR01039; TRNASYNTHTRP.
DR   TIGRFAMs; TIGR00233; trpS; 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..395
FT                   /note="Tryptophan--tRNA ligase"
FT                   /id="PRO_0000136598"
FT   REGION          117..179
FT                   /note="Insert"
FT   MOTIF           9..17
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT   MOTIF           261..265
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT   BINDING         8..10
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT   BINDING         16..17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT   BINDING         204
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT   BINDING         216..218
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT   BINDING         254
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT   BINDING         261..265
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
SQ   SEQUENCE   395 AA;  46709 MW;  72345F53CCEFB8F5 CRC64;
     MRIVSGMRPT GKLHLGHYFG VIRNWVKLQE EHECFFFIAD WHALTTAYKN TKELRQNIRE
     VMIDWLALGL DPQKSVLFIQ SLVKEHAELF LLFGMITPKS WLELNPTYKD LKYNLLRLTD
     LEKEFKEKLK ERISEIVNLI PFNITKEEKF REHLLENLTQ TMIEALFEGE IEPEILKRLN
     VSKRDFYETD TFGFLGYPVL QAADILIYKG EGVPVGEDQL PHIELSREIA RRFNRLYGKI
     FPEPKALLTE TPKIPGTDGR KMSKSYGNAV FFSDEKEEVE KKVMKMFTDP QKIRKNDPGR
     PEICPVFSWH KLFTKDEELV KKIEEDCRAG RLGCVECKRI LLKHLEEFLE PIRERRRELE
     KRINEIEEVF YENSRKAREI AQKTMEEVRK AMNLP