SYL_XYLFT
ID SYL_XYLFT Reviewed; 879 AA.
AC Q87C65;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Leucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00049};
DE EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049};
DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00049};
DE Short=LeuRS {ECO:0000255|HAMAP-Rule:MF_00049};
GN Name=leuS {ECO:0000255|HAMAP-Rule:MF_00049}; OrderedLocusNames=PD_1230;
OS Xylella fastidiosa (strain Temecula1 / ATCC 700964).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=183190;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Temecula1 / ATCC 700964;
RX PubMed=12533478; DOI=10.1128/jb.185.3.1018-1026.2003;
RA Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y.,
RA Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A.,
RA Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S.,
RA Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., Carrer H.,
RA Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L.,
RA Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L.,
RA Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S.,
RA Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F.,
RA Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G.,
RA Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A.,
RA Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L.,
RA Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P.;
RT "Comparative analyses of the complete genome sequences of Pierce's disease
RT and citrus variegated chlorosis strains of Xylella fastidiosa.";
RL J. Bacteriol. 185:1018-1026(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-
CC tRNA(Leu); Xref=Rhea:RHEA:11688, Rhea:RHEA-COMP:9613, Rhea:RHEA-
CC COMP:9622, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57427,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78494, ChEBI:CHEBI:456215; EC=6.1.1.4;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00049};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00049}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00049}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO29080.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE009442; AAO29080.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_004088586.1; NC_004556.1.
DR AlphaFoldDB; Q87C65; -.
DR SMR; Q87C65; -.
DR EnsemblBacteria; AAO29080; AAO29080; PD_1230.
DR GeneID; 58016766; -.
DR KEGG; xft:PD_1230; -.
DR HOGENOM; CLU_004427_0_0_6; -.
DR OMA; TFMVLAP; -.
DR Proteomes; UP000002516; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.620; -; 2.
DR Gene3D; 3.90.740.10; -; 1.
DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR002302; Leu-tRNA-ligase.
DR InterPro; IPR025709; Leu_tRNA-synth_edit.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR PANTHER; PTHR43740; PTHR43740; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 3.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR PRINTS; PR00985; TRNASYNTHLEU.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00396; leuS_bact; 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.
FT CHAIN 1..879
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000152123"
FT MOTIF 45..55
FT /note="'HIGH' region"
FT MOTIF 637..641
FT /note="'KMSKS' region"
FT BINDING 640
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 879 AA; 99824 MW; 4C2EE01B8FDC497E CRC64;
MPTEANTYDP QRIESTAQHY WDSTHAFEVN EHSNKPKYYC LSMLPYPSGA LHMGHVRNYT
IGDVISRYKR MTGHNVLQPM GWDAFGLPAE NAAIKNKVAP AQWTYKNIER MRTQLKSLGY
AINWSREFAT CQPDYYVHEQ HMFTRLMRKG LAYRRNALVN WDPVDQTVLA NEQVIDGRGW
RSGAPVEKRE IPQWFLRITD YAQELLDGLN TLDDWPEPVK TMQRNWIGRS EGLEIRFEVR
DVDNNALEAL RVFTTRPDTL FGVTFVSIAP EHPLALHAAK SNPGLAGLLT QMKQGGLSEA
ELKTQEKRGM DTGLKAIHPI TNEQLPVWVA NFVLMAYGTG AVMAVPGHDQ RDQEFANKYG
LPIRQVIALK EPKNQDESTW EPDVWRDWYA DKTREFELIN SAEFDGLDYQ GAFEVLAERF
ERQGRGQRRV NYRLRDWGVS RQRYWGCPIP VIYCPTCGAV PVPENQLPVI LPENVAFSGT
GSPIKTDPEW RKTTCPECGG PAERETDTFD TFMESSWYYA RYTSPNAREM LDKRANYWLP
VDQYIGGIEH AILHLMYFRF YHKLMRDARL VDSDEPAINL LTQGMVIAET FYRKNPDGSK
DWINPADVNV ECDERGRITG ATLISDGQPV LIGATEKMSK SKNNGVDPQI MVTKYGADTV
RLFSMFAAPP EQSLEWNETG VEGMARFLRR LWTQVHHHAS HGPATALDIT ALDTAQKAIR
CKTHNTIARV EDDYGRRRSF NTAIAAVMEL SNTLARFDDT TTQSHAVRQE ALETMVLLLN
PITPHTSHAL WQTLGHPETL LEDLPFPKVD TTALVRETAI LAVQINGKLR GTIEVATDAP
REHIENNALT EPNTARFLEG LTVLKIIIVP GKIVNIVAR
