ID   SYL_PROMT               Reviewed;         862 AA.
AC   Q46L15;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 117.
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=PMN2A_0321;
OS   Prochlorococcus marinus (strain NATL2A).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=59920;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NATL2A;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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; CP000095; AAZ57813.1; -; Genomic_DNA.
DR   RefSeq; WP_011293855.1; NC_007335.2.
DR   AlphaFoldDB; Q46L15; -.
DR   SMR; Q46L15; -.
DR   STRING; 59920.PMN2A_0321; -.
DR   PRIDE; Q46L15; -.
DR   EnsemblBacteria; AAZ57813; AAZ57813; PMN2A_0321.
DR   KEGG; pmn:PMN2A_0321; -.
DR   HOGENOM; CLU_004427_0_0_3; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   PhylomeDB; Q46L15; -.
DR   Proteomes; UP000002535; 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..862
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334792"
FT   MOTIF           51..61
FT                   /note="'HIGH' region"
FT   MOTIF           624..628
FT                   /note="'KMSKS' region"
FT   BINDING         627
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   862 AA;  99302 MW;  171CA10B0D90CA7C CRC64;
     MNNTTSDIND QRYEPREVEA YWQKEWASDD LYRTNTEVNK ENTFYALSMF PYPSGSLHMG
     HVRNYVITDV LARYKRMKGF NVLHPMGWDS FGLPAENAAI EREISPSTWT DKNISQMKDQ
     LDRLGLSIDW SKEVTTCKEE YYKWTQYIFN QLHKNNLAYQ KKATVNWDPI DQTVLANEQV
     DAEGKSWRSG AKVEKKELNQ WFLRITSFAE DLNKDLIKLN DWPDRVRVMQ KNWIGKSIGA
     EITFEIKNSD QKITAFTTRI DTVYGVSYLV LASNHPLIDQ LISSNDIDKL NDFRQTQEKL
     SDLERNSDTR QKLGMYLGVD AINPANNKEI PIWIGDYVIM EYGTGAVMGV PAHDSRDYQF
     AKSYDLPIQY VIKPNIDEDE SYLNAEFVDK GIMINSDKFN GIESDIAKTQ ILEFGSNSNW
     AKPKITYKLR DWLISRQRYW GCPIPIINCK KCGQVRVPDN DLPVVLPIDI KLTGKGKSPL
     TTKTEWINTC CPKCGTEAKR ETDTMDTFMC SSWYFLRYIN PDNCEKPFLK SEIDKWLPVK
     QYVGGIEHAI LHLLYSRFLT KALKKCGLIN IDEPFKKLLT QGMVQAVTFK NPNTNKYFSK
     DQIKDIDNPK DPLTGENIEI IYEKMSKSKY NGVDPSVVID KYGADTARMF ILFKAPPEKD
     LEWDDSDVEG QYRFIQRLWK FVINTFKLTN NNSRSNIEKE KSKDEEALRL INIAIKEITD
     DLDNLQFNTA ISELMKVVNG LSLIVNYCSN ETLNKVISIL VKITSPFSPH IAEELWKTIG
     NTQSIHLQSW PEFDAGAIEQ DTFKLMIQIN GKVRGSINAS KNLSKENLED LAIKTEAAIK
     WMDGKEPKRI IVVPNKLVNI VI