ID   SYL_BIFLD               Reviewed;         987 AA.
AC   B3DRD0;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 86.
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};
GN   OrderedLocusNames=BLD_0328;
OS   Bifidobacterium longum (strain DJO10A).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=205913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJO10A;
RX   PubMed=18505588; DOI=10.1186/1471-2164-9-247;
RA   Lee J.H., Karamychev V.N., Kozyavkin S.A., Mills D., Pavlov A.R.,
RA   Pavlova N.V., Polouchine N.N., Richardson P.M., Shakhova V.V.,
RA   Slesarev A.I., Weimer B., O'Sullivan D.J.;
RT   "Comparative genomic analysis of the gut bacterium Bifidobacterium longum
RT   reveals loci susceptible to deletion during pure culture growth.";
RL   BMC Genomics 9:247-247(2008).
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; CP000605; ACD97774.1; -; Genomic_DNA.
DR   RefSeq; WP_010080746.1; NZ_AABM02000001.1.
DR   AlphaFoldDB; B3DRD0; -.
DR   SMR; B3DRD0; -.
DR   GeneID; 69578373; -.
DR   KEGG; blj:BLD_0328; -.
DR   HOGENOM; CLU_004427_0_0_11; -.
DR   Proteomes; UP000002419; 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   CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   Gene3D; 3.40.50.620; HUPs; 3.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR   HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
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; IPR015413; Methionyl/Leucyl_tRNA_Synth.
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   NCBIfam; TIGR00396; leuS_bact; 1.
DR   PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF13603; tRNA-synt_1_2; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   PRINTS; PR00985; TRNASYNTHLEU.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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..987
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091291"
FT   MOTIF           69..80
FT                   /note="'HIGH' region"
FT   MOTIF           760..764
FT                   /note="'KMSKS' region"
FT   BINDING         763
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   987 AA;  110283 MW;  9E820921AEBAA7CC CRC64;
     MSDNEKSTQT EEPNFRYNAA LAQDIENKWQ KIWDEQGTFW AANVNGDLKD GKGRNAEGRT
     AYFAMDMFPY PSGKGLHVGH PLGYLASDVV SRYHRMKGEN VLHAMGYDAF GLPAEQYAVQ
     TGQHPRVTTE ANIANMSRQL HRMGLSFDNR RTFATIDPGY VRWTQWIFSR IYDSWYDEDA
     TNPSGSKGSA RPIAELVAKF ESGEKAIPGH ESDGKQWSDL TDAEQQDILN DFRLAYISKS
     PVNWCPGLGT VLANEEVTAE GKSERGNFPV FQRELRQWSM RITKYGHRLI ADLDGINWPE
     KVKLMQRNWI GESHGASVHF TVATADGDKD MEIYTTRPDT LFGTTFAVVS PEHHLLENVP
     AEWPADVPED WKGGYANPVE AVKAYRLAAE AKTAKDRVNE AGEKTGLFTG LYATNPITGA
     KLPLFTADYV LMDYGTGAIM AVPGGDQRDY DFAVKFGLPV IYTVTPLPDS GDDLANYEGK
     APFVSHDGIV INSSVEATEA KGDALSLNGL RVDDAIAKVN AWLESAGVGK GTVSYRLRDW
     LFSRQRYWGE PFPIVYGEDG TPHLLPDSAL PINLPDVPDY EPRTFDPMDA ESNPEAPLSR
     NEDWVKVELD LGDGKKTYYR DTNTMPNWAG SCWYYMRYID PTDTKHMVEK DEFDYWMGPN
     HNKYSGDEGG VDLYIGGVEH AVLHLLYSRF WHKVLFDLGY VDSAEPFHKL FNQGMIQAYA
     YTDDRGQYVP ADEVVEGPAD ASGEPTFTWN GEHANREFGK MGKSLKNIVT PDYMYENYGA
     DTFRLYEMSM GPLDESRPWN TRNVVGGMRF LQRLWRNVVD ETTGQAHVTE DTPDEKTLKL
     LNNTIAEVTA EMEGMRPNTA IAKLIVLNNH LTGLKAVPRA AVEPLILMLA PIAPHICEEM
     WSKLGHAESL SAEPWPVADE RYVGHDTVTA VVQIKGKVRA KLEVPVDIDP ADLEKQALAA
     VADRLGGKEP RKVIVKAPKI VSIVPAE
//