ID   SYL_SULDN               Reviewed;         822 AA.
AC   Q30Q82;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-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=Suden_1572;
OS   Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) (Thiomicrospira
OS   denitrificans (strain ATCC 33889 / DSM 1251)).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Sulfurimonadaceae; Sulfurimonas.
OX   NCBI_TaxID=326298;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33889 / DSM 1251;
RX   PubMed=18065616; DOI=10.1128/aem.01844-07;
RA   Sievert S.M., Scott K.M., Klotz M.G., Chain P.S.G., Hauser L.J., Hemp J.,
RA   Huegler M., Land M., Lapidus A., Larimer F.W., Lucas S., Malfatti S.A.,
RA   Meyer F., Paulsen I.T., Ren Q., Simon J., Bailey K., Diaz E.,
RA   Fitzpatrick K.A., Glover B., Gwatney N., Korajkic A., Long A.,
RA   Mobberley J.M., Pantry S.N., Pazder G., Peterson S., Quintanilla J.D.,
RA   Sprinkle R., Stephens J., Thomas P., Vaughn R., Weber M.J., Wooten L.L.;
RT   "Genome of the epsilonproteobacterial chemolithoautotroph Sulfurimonas
RT   denitrificans.";
RL   Appl. Environ. Microbiol. 74:1145-1156(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; CP000153; ABB44849.1; -; Genomic_DNA.
DR   RefSeq; WP_011373201.1; NC_007575.1.
DR   AlphaFoldDB; Q30Q82; -.
DR   SMR; Q30Q82; -.
DR   STRING; 326298.Suden_1572; -.
DR   KEGG; tdn:Suden_1572; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_7; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000002714; 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; 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; IPR002302; Leu-tRNA-ligase.
DR   InterPro; IPR025709; Leu_tRNA-synth_edit.
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; PF13603; tRNA-synt_1_2; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 2.
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..822
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091373"
FT   MOTIF           46..56
FT                   /note="'HIGH' region"
FT   MOTIF           590..594
FT                   /note="'KMSKS' region"
FT   BINDING         593
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   822 AA;  94408 MW;  202B10DAC105403F CRC64;
     MIYNSKELEK KWQEYWAKNR SFEPSEDFTK ETGCPRGKKY ILSMFPFPSG RLHMGHVRNY
     TISDAFARYY RQEGFNVLHP IGFDSFGMPA ENAAIKNGSH PKKWTYDNID YMKGEFKSLG
     FSFSKDRELA TSDELYTKFE QGFIIDMYEK GLLYRKKGFL NWCPSCHTVL ANEQVIDGSC
     WRCDSSVVKK DMNQYYFKIT QYGDELLADL SKLESGWPKQ VLTMQENWIG KSNGLEFKLS
     FDEKSLEKLD NKFDTFSVFT TRPDTIYGVS YAALAPEHEI VSYMIENALV GSDTIEKIKE
     MKNASSIERQ KEKSGIALNL HVVHPLTKKL IPIWVANFVL MDYGSGAVMA VPAHDERDFD
     FAKKYNLPIK AVIKPFDGES SIESAFTEVG ELFDSEMFNG LNSKDAQLKI IEHFEEKKIG
     KKTTNYKLKD WGVSRQRYWG APIPFVHCDS CGIVMEKKEN LPIALPEDIE ITGEGNPLEK
     HPTWKYCKCP KCDKDAIRET DTMDTFVESS WYFLRFCASP KNWLNEAFSK EQIKYWMGVD
     HYIGGIEHAI LHLLYARFFT KVFRDLGYLE FDEPFNKLLT QGMVLKDGAK MSKSKGNTVD
     PDAIIEKYGA DTARLFILFA APPTQELEWN DNAVEGAFKF IKRFYERSVN AIKTNTIPKI
     NHASLSKEEK FARKKVYEAL VRSREVYGEK YTFNTMIAGV MEAMNALNLQ TNSDVWSEAY
     WILTSIMEPV IPHVCSEISS VKFSLKNLSS QIVVQEVFVE DSLMLGVTVN GKRRCEIEVP
     TEATQDEILQ IARESASKWL EGKTIIKEIV VPKKLVNLVI KD
//