ID   SYL_GLUOX               Reviewed;         865 AA.
AC   Q5FTV3;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 125.
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=GOX0410;
OS   Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=290633;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=621H;
RX   PubMed=15665824; DOI=10.1038/nbt1062;
RA   Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA   Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT   "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT   oxydans.";
RL   Nat. Biotechnol. 23:195-200(2005).
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; CP000009; AAW60193.1; -; Genomic_DNA.
DR   RefSeq; WP_011251994.1; NZ_LT900338.1.
DR   AlphaFoldDB; Q5FTV3; -.
DR   SMR; Q5FTV3; -.
DR   STRING; 290633.GOX0410; -.
DR   KEGG; gox:GOX0410; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   Proteomes; UP000006375; 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; cd00812; LeuRS_core; 1.
DR   Gene3D; 2.20.28.290; -; 1.
DR   Gene3D; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
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; 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; 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; PF00133; tRNA-synt_1; 2.
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; Reference proteome.
FT   CHAIN           1..865
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000071111"
FT   MOTIF           48..58
FT                   /note="'HIGH' region"
FT   MOTIF           626..630
FT                   /note="'KMSKS' region"
FT   BINDING         629
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   865 AA;  96309 MW;  0CF6FE1B0AEE3F43 CRC64;
     MSDTTAPAFD FQDREPFWQN EWKRRNTFAV PDVPPADRPK YYVLEMFPYP SGQLHVGHVR
     NYTLGDVVAR YKRARGFAVM HPMGWDAFGL PAENAARERN VHPGKWTMDN IATMRGTLQR
     LGFSLDWDRE IATCLPEYYG KQQKLFTDML GAGLVERRDS LVNWDPVDET VLANEQVVDG
     RGWRSGALIE KKKLSQWFLK ITKFAQPLLD DLKTLDRWPE RVRTMQERWI GRSEGARVRF
     ALHQPPAGYD EDLDSVEVFT TRPDTLFGLS FIGISAEHPL ARKVAESNPQ AAAFIEECRR
     LGTSEEVIEA AEKRGFDTGL RVANPLDPEK TAPVWIANFV LMDYGTGAVF GCPCGDQRDL
     DFARKYDLPV PQVLLPPGQD AETFVLGKKA VSGDATLFNS GFLDGLDPAA ARTKVIERLE
     GLGAGKGVVN WRLRDWGISR QRYWGCPIPI IHCDTCGPVP VPDEQLPVIL PEDVTFDRPG
     NPLDHHPTWK HVNCPHCGKP AVRETDTFDT FVDSSWYFAR FTSPHAETPT VPAAANGWLP
     VDQYIGGIEH AILHLLYARF FTRAMHETGH LDVDEPFAGL FTQGMVTHES YRDDSGWLYP
     EEVERQGDQV VRRETGTPVQ VGRSEKMSKS KRNTVSPVDI IERYGADTAR WFVLSDSPPE
     RDMEWTAAGV AAAARFGQRL HRLVASVAAR DAADSAHGAT GDDLRRVTHR TIAAVGEALE
     AFTPNVAVAR LHELTSALAD AERIEGAGIA AARREAARVL CLLTAPMMPH LAEDMMAVLE
     PGSALVVERP WPEAEEKWLA VQSVTIGVQI LGKLRGTIEV PPNAPKEEVL AAAKSEPNVA
     RLLEGKRLVK EIHVPNRIVN FVVAG
//