ID   SYL_HAEDU               Reviewed;         861 AA.
AC   Q7VM66;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 115.
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=HD_1132;
OS   Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=233412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=35000HP / ATCC 700724;
RA   Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA   Nguyen D., Wang J., Forst C., Hood L.;
RT   "The complete genome sequence of Haemophilus ducreyi.";
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; AE017143; AAP95994.1; -; Genomic_DNA.
DR   RefSeq; WP_010945043.1; NC_002940.2.
DR   AlphaFoldDB; Q7VM66; -.
DR   SMR; Q7VM66; -.
DR   STRING; 233412.HD_1132; -.
DR   EnsemblBacteria; AAP95994; AAP95994; HD_1132.
DR   KEGG; hdu:HD_1132; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000001022; 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; Reference proteome.
FT   CHAIN           1..861
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152022"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           619..623
FT                   /note="'KMSKS' region"
FT   BINDING         622
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   861 AA;  98050 MW;  E70ED792F8BCFB3E CRC64;
     MQQQYNPSAI ESKVQHFWEE NKVFKAVKDI TKEKYYCLSM LPYPSGRLHM GHVRNYTIGD
     VISRYQRMIG KNVLQPMGWD AFGLPAEGAA VKNNTAPAKW TYENIEYMKN QLKVLGFSYD
     WDREITTCRP EYYKWEQWFF TELYKKGLVY KKTSTVNWCP NDETVLANEQ VHEGCCWRCD
     TPVEQRDIPQ WFIKITDYAE ELLTQLDNLT QWPDQVKTMQ RNWIGRSEGV EITFKIAGSN
     ATLPVYTTRP DTFFGVSYLA VAAAHPLAEL ASTNNPALAE FIREAKNTKV AEAELATMEK
     KGMPTGLFAI HPLTGKEIPV WVANFVLMHY GTGAVMAVPA HDERDFDFAK KYGLQINQVI
     QPLDASTWDF SQAAFTEHGK LINSAEFDGL DFNHAFNAIA DKLESLGVGK RQVNFRLRDW
     GVSRQRYWGA PIPMMTTEQG EVVTVPLKDL PVILPENVVM DGVQSPIKSD PEWAKTTYEG
     QPALKETDTF DTFMESSWYY ARYTCPQYHQ GMLDADEANY WLPVDQYIGG IEHATMHLLY
     FRFFHKLLRD AGILTSDEPA TKLLCQGMVL ADAFYYTSPT NERIWVSPTQ VSLERDEKGR
     IINATDPAGH KLVHSGMTKM SKSKNNGIDP QEMVEKYGAD TVRLFMMFAS PAEMTLEWQE
     SGVEGAKRFL GRVWNLVYEY VQQPATQALN ALELNKAQKE LRRDVHKTIA KVSDDIGRRQ
     TFNTAIAAIM ELMNKLNKAP LESDQDKAVM AEALSAVVRM LYPITPHICF ELWQALGNQQ
     TIDFAPWVVS DETAMIEDEK LVVVQVNGKV RGKITVPANA SEDEVKITAK NDANVAKFLA
     DMQIVKEIYI PFKMLNFVVK V