ID   SYL_SYNFM               Reviewed;         829 AA.
AC   A0LK15;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 109.
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=Sfum_2084;
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Thermodesulfobacteriota; Syntrophobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB;
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., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J.,
RA   Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-2006) 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; CP000478; ABK17767.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0LK15; -.
DR   SMR; A0LK15; -.
DR   STRING; 335543.Sfum_2084; -.
DR   KEGG; sfu:Sfum_2084; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_7; -.
DR   InParanoid; A0LK15; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000001784; 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; 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; 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; Reference proteome.
FT   CHAIN           1..829
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009454"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           584..588
FT                   /note="'KMSKS' region"
FT   BINDING         587
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   829 AA;  93354 MW;  5AA680E8AE916D5A CRC64;
     MDYKYAPKRI EKKWQEHWER EKLFEVSEIP GREKFYLLEM FPYPSGRIHM GHVRNYSIGD
     VVARFLRMRG YNVLHPMGWD AFGMPAENAA IKAKTHPARW TYENIAYMRS QLKQLGFSYD
     WSREFATCDV SYYRWEQLFF LKMYEKGLAY KRSAYVNWCG TCLTVLANEQ VEGGACWRCD
     QPVVQKEMEQ WFFKITDYVE ELLDYTHRLP GWPERVLTMQ QNWIGKSLGS KLLFPLASGD
     GSITVFTTRA DTLFGATFMS LAPEHPLVEG LCRGNPQESE VLRFVQAAKQ AKRNDREAEL
     LEKEGVFTGS CCINPVTGAK MPIYVANFVV MEYGTGAVMA VPAHDQRDFE FARKYGLPVK
     VVIKPADAAA APAAQELSAA FEDDGVLVDS GAYSGMASAE ARTAITADLA GKGLGEQTVQ
     YRLRDWGISR QRYWGAPIPI VYCDKCGTVP VPEKDLPVVL PTDVALLPNG ASPLPAHAPF
     LNTDCPRCGG PARRETDTMD TFVESSWYFA RFACARYDQG PLDLPKVKYW MPVDQYIGGI
     EHAVLHLLYS RFFVKVLRDM GALEVDEPFR NLLTQGMVIK DGAKMSKSKG NVVDPDDMIK
     AYGADTVRLF CLFASPPEKD LEWSDQGVEG SFRFLSRIWR LVSDNLDALR SAPRHNGGGA
     LPEPLEALHR KTHQTIKKVT EDIRDRFHFN TAIAAIMELV NQIYQVVEGG SRAGNIWPVV
     KEAVEALILL VSPMAPHIAE EIWHELGHTR SVLLEPWPEW SGKALQAEEV MLVVQVNGRL
     RSRITVPSDA TPEQMEAAAL ADSRVQEFIA GKPVRKVVVV PKKIINVVV
//