ID   SYL_PROM0               Reviewed;         856 AA.
AC   A3PCW8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, 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=P9301_09701;
OS   Prochlorococcus marinus (strain MIT 9301).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9301;
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; CP000576; ABO17593.1; -; Genomic_DNA.
DR   RefSeq; WP_011862941.1; NC_009091.1.
DR   AlphaFoldDB; A3PCW8; -.
DR   SMR; A3PCW8; -.
DR   STRING; 167546.P9301_09701; -.
DR   EnsemblBacteria; ABO17593; ABO17593; P9301_09701.
DR   KEGG; pmg:P9301_09701; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_3; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000001430; 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; 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; 3.
DR   Pfam; PF13603; tRNA-synt_1_2; 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..856
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009392"
FT   MOTIF           53..63
FT                   /note="'HIGH' region"
FT   MOTIF           622..626
FT                   /note="'KMSKS' region"
FT   BINDING         625
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   856 AA;  98780 MW;  CA4C08EB051D04E3 CRC64;
     MISPDQQYET DTNLYNPSEI EKKWQSIWTE NNLYKTDELT DNSDKFYALS MFPYPSGNLH
     MGHVRNYVIT DLIARFQRFK GKSVLHPMGW DAFGLPAENA AIERGISPSV WTKKNISHMK
     SQLKLLGLSV DWDREFATCD ENYYVWTQYL FLELYKAGLV YQKESEVNWD PIDNTVLANE
     QVDSEGKSWR SGAIVEKKLL KQWFLRITNY ADELLKDLEK LDNWPERVKI MQDNWIGKSI
     GTNINFNINT HPEKKLTVFT TRPDTLFGVT YLAISVNHSL IKNISDQETI QHIENLKKYL
     KKNKNNELEK IGIKTSLIAI NPVNSEPIPI WVASYVLDEY GTGAVMGVPA HDLRDFEFAK
     KNNIDIKQVI IKDKSEQNKE LDEAYVENGY LINSNQYDGV ANTIAKLKIS EEGVNNRWAE
     NKTQYRLRDW LISRQRYWGC PIPIVNCKKC GSVPLNQSEL PVALPKDIDI SANKINALGD
     NKNWVNTTCP KCGIAAKKET DTMDTFMCSS WYFLRYPSSK CPNKPFEKIE INKWLPVDQY
     VGGVEHAILH LLYARFFTKA LRDNQLFEID EPFKKLLTQG MVQAAAYKNN KTGKYVSPSD
     INDLSNPTDP IDNTKLEILF EKMSKSKYNG IDPESVIKKY GADTARMFIL FKAPPEKDLE
     WGDTDVEGQF RFLSRIWKLY INCAKNVNIK SNSYPDKEKS LIKSMNIAIK EISNDILNNQ
     FNTAISELMK FYNSLSNSIN DVNNNLKIDA LKTFCILLAP FAPHIAEEIW HLIGFKKSVH
     LEHWPSFNAE ALKEDSYELV IQVNGKVREK VNINHDMNED QIKELTLKRP NILKWTKDKE
     IRKIIIVKGK IMNIVV