ID   SYL_SPHAL               Reviewed;         849 AA.
AC   Q1GNP7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=Sala_3020;
OS   Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256)
OS   (Sphingomonas alaskensis).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=317655;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13593 / LMG 18877 / RB2256;
RX   PubMed=19805210; DOI=10.1073/pnas.0903507106;
RA   Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S.,
RA   DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A.,
RA   Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V.,
RA   Robb F.T., Kjelleberg S., Cavicchioli R.;
RT   "The genomic basis of trophic strategy in marine bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(2009).
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; CP000356; ABF54725.1; -; Genomic_DNA.
DR   RefSeq; WP_011543288.1; NC_008048.1.
DR   AlphaFoldDB; Q1GNP7; -.
DR   SMR; Q1GNP7; -.
DR   STRING; 317655.Sala_3020; -.
DR   EnsemblBacteria; ABF54725; ABF54725; Sala_3020.
DR   KEGG; sal:Sala_3020; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000006578; 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   Gene3D; 3.40.50.620; -; 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   PANTHER; PTHR43740; PTHR43740; 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; 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; Reference proteome.
FT   CHAIN           1..849
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334824"
FT   MOTIF           44..54
FT                   /note="'HIGH' region"
FT   MOTIF           620..624
FT                   /note="'KMSKS' region"
FT   BINDING         623
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   849 AA;  93674 MW;  5A37DBD21B7297D6 CRC64;
     MTRETRFGAL AADARWQKAW EAANSFATTD SGQKPKAYIL EMFPYPSGRI HMGHVRNYAM
     GDVLARFKRM TGHDVLHPMG WDAFGMPAEN AAMEKGVHPG GWTRANIDAM RAQLKRLGLA
     IDWSRELATC EPDYYGQEQA LFLDLHAAGL VYRKESYVNW DPVDMTVLAN EQVIDGRGWR
     SGALVEKKKL SQWFLKITDF ADELLEGLGS LDKWPDKVRL MQENWIGKSQ GLEFSFKFAG
     GAPAFAVFTT RPDTLYGASF AAISPDHPLA EKLAKDSPEL AAFIAECRRQ GTSAEQLETA
     EKLGFDTGLA VEHPLDPDWH LPVWVVNYVL MDYGTGAIFG CPAHDQRDLD FAHKYELPVH
     RVIADGDETA QHFTGSEAYT GPGKLVNSHF LDGMSIDEAK AAVITRAEHE GWGKGTTVWR
     LRDWGVSRQR YWGTPIPFIH CAACGTVPVP KSQLPVTLPD DVDFSVPGNP LDRHPTWKHV
     ACPICEGAAL RETDTLDTFV DSSWYFLRFA SAPTDKPFDP EVIRRWLPVD QYIGGIEHAI
     LHLLYARFWT RALNKLGMID IEEPFASLFT QGMVTHETYS RPQGEGLPPL YFTPDEVERG
     ADGATLIADG APVEVGRVIK MSKSKKNVVD PDAILDQYGA DAVRWFMLSD SPPERDLPWS
     EAGIEGAWRF VQRLWRLFGE TENVGDGGED KGLARKLHQT IAGVAADIEA LGFNKAVAKI
     HALANEIEKA KPSATRAEAC AKLILLVAPM MPHLAEEAWT ALPASQRTTP MVADAAWPAA
     DPALLIDDEV TIAIQMAGKL RDTMTVAKGA DKAALEAAAL ARPRIVELLG GAAPKKVIVV
     PDRLVNILP