ID   SYL_AFIC5               Reviewed;         879 AA.
AC   B6JAI4; F8BS31;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   27-MAR-2024, entry version 90.
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=OCAR_4363, OCA5_c01660;
OS   Afipia carboxidovorans (strain ATCC 49405 / DSM 1227 / KCTC 32145 / OM5)
OS   (Oligotropha carboxidovorans).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Afipia.
OX   NCBI_TaxID=504832;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5;
RX   PubMed=18539730; DOI=10.1128/jb.00614-08;
RA   Paul D., Bridges S., Burgess S.C., Dandass Y., Lawrence M.L.;
RT   "Genome sequence of the chemolithoautotrophic bacterium Oligotropha
RT   carboxidovorans OM5T.";
RL   J. Bacteriol. 190:5531-5532(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5;
RX   PubMed=21742883; DOI=10.1128/jb.05619-11;
RA   Volland S., Rachinger M., Strittmatter A., Daniel R., Gottschalk G.,
RA   Meyer O.;
RT   "Complete genome sequences of the chemolithoautotrophic Oligotropha
RT   carboxidovorans strains OM4 and OM5.";
RL   J. Bacteriol. 193:5043-5043(2011).
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; CP001196; ACI91509.1; -; Genomic_DNA.
DR   EMBL; CP002826; AEI04898.1; -; Genomic_DNA.
DR   RefSeq; WP_012561540.1; NC_015684.1.
DR   AlphaFoldDB; B6JAI4; -.
DR   SMR; B6JAI4; -.
DR   STRING; 504832.OCA5_c01660; -.
DR   KEGG; oca:OCAR_4363; -.
DR   KEGG; ocg:OCA5_c01660; -.
DR   PATRIC; fig|504832.7.peg.175; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000007730; 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   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   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..879
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091340"
FT   MOTIF           43..53
FT                   /note="'HIGH' region"
FT   MOTIF           636..640
FT                   /note="'KMSKS' region"
FT   BINDING         639
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   879 AA;  98025 MW;  9C29A2C1EF90A0A5 CRC64;
     MSTERYNARE VEPRWQQIWD EKGVFASRND DSRPKYYVLE MFPYPSGRIH MGHVRNYTMG
     DVVARYRRAK GHNVLHPMGW DAFGMPAENA AMQNKTHPAK WTYANIAAMK KQLKSMGLSL
     DWAREIATCD PSYYKHQQRM FLDFLKAGLV ERKQSKVNWD PVDQTVLANE QVIDGRGWRS
     GALVEQRELT QWFFKISDYS EELLTALDTL DRWPEKVRLM QKNWIGRSEG LLVRFALDAA
     TAPAGESEVE VFTTRPDTLF GAKFVALSPD HPLAAEVAKA NPKLEAFIAE CHRHGTAQAE
     IDTAEKLGFD TGLRARHPFD PDWLLPVYVA NFVLMDYGTG AIFGCPAHDQ RDLDFVNKYG
     LGNTPVVCPE GQDPKSFVIT DTAYDGDGRM INSRFLDGMT IADAKEDVAK RLETATLPRA
     NGGGNAPVAK RQVNYRLRDW GISRQRYWGC PIPIIHCESC GIVPVPVKDL PVKLPDDIEF
     DRPGNPLDRH PTWKHVACPQ CGGKARRETD TMDTFVDSSW YFARFTDPWN ENAPTTRKVV
     DAMMPVDQYI GGIEHAILHL LYSRFFTRAM KATGHVGFDE PFAGLFTQGM VVHETYKNAD
     GSWAAPSEIK IEGTGDARHA TLIDTGAPVE IGSIEKMSKS KRNTIDPDDI IGTYGADTAR
     WFMLSDSPPD RDVIWSEEGV QGANRFVQRV WRLVNLAAPH LPKDSAAAGT SADTKPLRST
     AHRTLADVSQ AIERLRFNTA IAKLYAFVGP LNEAIDDPRL KADPAWAASV REALDMLVRM
     IAPMMPHLAE QCWEALGGQG LVSEAAWPEV DPVLLVEDTI TLPVQINGKK RADVTVGRNA
     PNPEIEAAVL ALDAVKTALA GATPRKIIVV PQRIVNVVV
//