SYW_HAEIN
ID SYW_HAEIN Reviewed; 334 AA.
AC P43835;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 132.
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=HI_0637;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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; L42023; AAC22296.1; -; Genomic_DNA.
DR PIR; C64083; C64083.
DR RefSeq; NP_438797.1; NC_000907.1.
DR RefSeq; WP_005694505.1; NC_000907.1.
DR PDB; 6DFU; X-ray; 2.05 A; A/B=1-334.
DR PDBsum; 6DFU; -.
DR AlphaFoldDB; P43835; -.
DR SMR; P43835; -.
DR STRING; 71421.HI_0637; -.
DR EnsemblBacteria; AAC22296; AAC22296; HI_0637.
DR KEGG; hin:HI_0637; -.
DR PATRIC; fig|71421.8.peg.665; -.
DR eggNOG; COG0180; Bacteria.
DR HOGENOM; CLU_029244_1_1_6; -.
DR OMA; GWGQFKP; -.
DR PhylomeDB; P43835; -.
DR BioCyc; HINF71421:G1GJ1-668-MON; -.
DR Proteomes; UP000000579; 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; -; 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; 1.
DR PRINTS; PR01039; TRNASYNTHTRP.
DR TIGRFAMs; TIGR00233; trpS; 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..334
FT /note="Tryptophan--tRNA ligase"
FT /id="PRO_0000136635"
FT MOTIF 12..20
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT MOTIF 195..199
FT /note="'KMSKS' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT BINDING 11..13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT BINDING 19..20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT BINDING 135
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT BINDING 147..149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT BINDING 186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT BINDING 195..199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:6DFU"
FT HELIX 18..22
FT /evidence="ECO:0007829|PDB:6DFU"
FT HELIX 24..31
FT /evidence="ECO:0007829|PDB:6DFU"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:6DFU"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:6DFU"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:6DFU"
FT HELIX 53..69
FT /evidence="ECO:0007829|PDB:6DFU"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:6DFU"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:6DFU"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:6DFU"
FT HELIX 87..97
FT /evidence="ECO:0007829|PDB:6DFU"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:6DFU"
FT HELIX 101..105
FT /evidence="ECO:0007829|PDB:6DFU"
FT HELIX 108..116
FT /evidence="ECO:0007829|PDB:6DFU"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:6DFU"
FT HELIX 123..137
FT /evidence="ECO:0007829|PDB:6DFU"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:6DFU"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:6DFU"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:6DFU"
FT HELIX 151..168
FT /evidence="ECO:0007829|PDB:6DFU"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:6DFU"
FT HELIX 213..221
FT /evidence="ECO:0007829|PDB:6DFU"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:6DFU"
FT HELIX 241..254
FT /evidence="ECO:0007829|PDB:6DFU"
FT HELIX 258..264
FT /evidence="ECO:0007829|PDB:6DFU"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:6DFU"
FT HELIX 270..297
FT /evidence="ECO:0007829|PDB:6DFU"
FT HELIX 299..328
FT /evidence="ECO:0007829|PDB:6DFU"
SQ SEQUENCE 334 AA; 37396 MW; 7A581383BFF1F7A1 CRC64;
MAKPIVFSGV QPSGELTIGN YLGALRNWVK MQEDYECIFC VVDLHAITVR QDPVALRKAT
LDVLALYLAC GIDPNKSTIF VQSHVPEHTQ LSWVLNCYTY FGEMSRMTQF KDKSARYAEN
INVGLFDYPV LMAADILLYQ AKSVPVGDDQ KQHLEITRDI ANRFNALYGN IFTIPEIFIG
KAGARIMSLQ DPEKKMSKSD DNRNNVVTLL EDPKSVAKKI KRAVTDSDEP PVVRYDVQNK
AGVSNLLDIL SAVTDKPIAD LEKEFEGKMY GHLKTAVADE VSTLLASLQE RFHQYRNDET
LLDNILRQGA EKARAKAQET LAKVYEAVGF VAAK
