SYW_VIBCH
ID SYW_VIBCH Reviewed; 338 AA.
AC Q9KNV7;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 109.
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=VC_2623;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(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 -!- SEQUENCE CAUTION:
CC Sequence=AAF95764.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE003852; AAF95764.1; ALT_INIT; Genomic_DNA.
DR PIR; E82052; E82052.
DR RefSeq; NP_232251.2; NC_002505.1.
DR RefSeq; WP_000042615.1; NZ_LT906614.1.
DR PDB; 3SZ3; X-ray; 1.50 A; A=1-338.
DR PDBsum; 3SZ3; -.
DR AlphaFoldDB; Q9KNV7; -.
DR SMR; Q9KNV7; -.
DR STRING; 243277.VC_2623; -.
DR DNASU; 2615640; -.
DR EnsemblBacteria; AAF95764; AAF95764; VC_2623.
DR GeneID; 57741224; -.
DR KEGG; vch:VC_2623; -.
DR PATRIC; fig|243277.26.peg.2501; -.
DR eggNOG; COG0180; Bacteria.
DR HOGENOM; CLU_029244_1_1_6; -.
DR OMA; GWGQFKP; -.
DR EvolutionaryTrace; Q9KNV7; -.
DR Proteomes; UP000000584; Chromosome 1.
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; 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.
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..338
FT /note="Tryptophan--tRNA ligase"
FT /id="PRO_0000136705"
FT MOTIF 12..20
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT MOTIF 198..202
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 189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT BINDING 198..202
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:3SZ3"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:3SZ3"
FT HELIX 18..23
FT /evidence="ECO:0007829|PDB:3SZ3"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:3SZ3"
FT HELIX 28..34
FT /evidence="ECO:0007829|PDB:3SZ3"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:3SZ3"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:3SZ3"
FT HELIX 53..69
FT /evidence="ECO:0007829|PDB:3SZ3"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:3SZ3"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:3SZ3"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:3SZ3"
FT HELIX 87..96
FT /evidence="ECO:0007829|PDB:3SZ3"
FT HELIX 101..105
FT /evidence="ECO:0007829|PDB:3SZ3"
FT HELIX 108..117
FT /evidence="ECO:0007829|PDB:3SZ3"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:3SZ3"
FT HELIX 123..137
FT /evidence="ECO:0007829|PDB:3SZ3"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:3SZ3"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:3SZ3"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:3SZ3"
FT HELIX 151..168
FT /evidence="ECO:0007829|PDB:3SZ3"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:3SZ3"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:3SZ3"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:3SZ3"
FT HELIX 216..224
FT /evidence="ECO:0007829|PDB:3SZ3"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:3SZ3"
FT HELIX 244..257
FT /evidence="ECO:0007829|PDB:3SZ3"
FT HELIX 261..267
FT /evidence="ECO:0007829|PDB:3SZ3"
FT TURN 268..270
FT /evidence="ECO:0007829|PDB:3SZ3"
FT HELIX 275..300
FT /evidence="ECO:0007829|PDB:3SZ3"
FT HELIX 303..332
FT /evidence="ECO:0007829|PDB:3SZ3"
SQ SEQUENCE 338 AA; 37433 MW; E455592CF469A9A0 CRC64;
MSKPIVLSGV QPSGELSIGN YLGALRQWQQ MQDDYDCQYC VVDLHAITVR QDPQALHEAT
LDALAICLAV GVDPKKSTLF VQSHVPEHAQ LGWVLNCYTQ MGELSRMTQF KDKSARYAND
VNAGLFGYPV LMAADILLYG AHQVPVGSDQ KQHLELARDI ATRFNNIYSP EQPIFTIPEP
YIPTVNARVM SLQDATKKMS KSDDNRKNVI TLLEDPKSII KKINKAQTDA ETPPRIAYDV
ENKAGIANLM GLYSAATGKT FAEIEAQYAG VEMYGPFKKD VGEAVVAMLE PVQAEYQRIR
NDREYLNSVM RDGAEKASAK ALQTLKKVYA AVGFVARP
