ID   SYL_MYCGI               Reviewed;         949 AA.
AC   A4T4R2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=Mflv_0853;
OS   Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS   PYR-GCK)).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PYR-GCK;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium gilvum PYR-GCK.";
RL   Submitted (APR-2007) 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; CP000656; ABP43337.1; -; Genomic_DNA.
DR   RefSeq; WP_011891757.1; NC_009338.1.
DR   AlphaFoldDB; A4T4R2; -.
DR   SMR; A4T4R2; -.
DR   STRING; 350054.Mflv_0853; -.
DR   EnsemblBacteria; ABP43337; ABP43337; Mflv_0853.
DR   KEGG; mgi:Mflv_0853; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_11; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
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; 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   PANTHER; PTHR43740; PTHR43740; 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; 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..949
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334774"
FT   REGION          540..562
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           68..79
FT                   /note="'HIGH' region"
FT   MOTIF           722..726
FT                   /note="'KMSKS' region"
FT   BINDING         725
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   949 AA;  105013 MW;  84E6A5DB25C6AF7E CRC64;
     MTETPIAPLD DTPRFRYTAV LAGEIERAWQ QQWADSGTFH VDNPVGSLAP ADGSAVPADK
     MFVQDMFPYP SGEGLHVGHP LGYIATDVYA RYYRMTGRNV LHALGFDAFG LPAEQYAIQT
     GTHPRTRTEA NIVNFRRQLG RLGLGHDSRR SFATTDVDYY KWTQWIFLQI FNAWFDTDQN
     RARPIRELIA EFEAGTRQVG DGRSWADLDA GARADLVDAH RLVYLADSVV NWCPGLGTVL
     ANEEVTADGR SERGNFPVFR KRLRQWMMRI TAYSDRLLED LDVLDWPDKV KTMQRNWIGR
     STGAEVQFST AAGDIEVFTT RPDTLFGATY MVLAPEHDLV DRLVASAWPD GTDARWTFGA
     ATPAEAVAAY RAGIAAKSDL ERQENKTKTG VFLGAYATNP ANGQQVPVFI ADYVLAGYGT
     GAIMAVPSGD QRDWDFATEF GLPIVEVVAG GDVTVEAYSG DGTMVNSGFL DGMDVATAKQ
     AMTERLVADG RGRARVEYKL RDWLFARQRY WGEPFPVVYD SEGRAHGLPE GMLPVELPDV
     PDYSPVSFDP DDAGSEPSPP LGKVTDWVNV DLDLGDGLKP YTRDTNVMPQ WAGSSWYELR
     YTDPYNSEAL CAKENEAYWM GPRPAEHGPD DPGGVDLYVG GVEHAVLHLL YSRFWHKVLY
     DLGHVSSREP YRRLVNQGYI QAFAYTDSRG SYVPAAEVIE RDGKFVWPGP DGETEVNQEF
     GKIGKSLKNS VSPDEICDNY GADTLRVYEM SMGPLEASRP WATKDVVGAY RFLQRVWRLV
     VDENTGETLA TEDALDDDTL RLLHRTIAGT ADDYASLRNN TAAAKLIEYT NHLTKQSVTA
     RAALEPLVLM VAPLAPHLAE ELWKRLGHEG SLAHGPFPLA DERYLVEDTV EYPVQVNGKV
     RGRVTVPADA PADAVEAAAL AEEKVVAFLD GRTPKKVIVV AGRLVNVVV