ID   SYL_PROM9               Reviewed;         856 AA.
AC   Q31AX4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 104.
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=PMT9312_0911;
OS   Prochlorococcus marinus (strain MIT 9312).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=74546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9312;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of Prochlorococcus marinus str. MIT 9312.";
RL   Submitted (JUL-2005) 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; CP000111; ABB49971.1; -; Genomic_DNA.
DR   RefSeq; WP_011376465.1; NC_007577.1.
DR   AlphaFoldDB; Q31AX4; -.
DR   SMR; Q31AX4; -.
DR   STRING; 74546.PMT9312_0911; -.
DR   EnsemblBacteria; ABB49971; ABB49971; PMT9312_0911.
DR   KEGG; pmi:PMT9312_0911; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_3; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000002715; 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.
FT   CHAIN           1..856
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009394"
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;  98666 MW;  0ADE75F2D85B2663 CRC64;
     MISPDKQYET DTNLYNPSEI EKKWQSIWTE NNLYKTDELT ENSDKFYALS MFPYPSGNLH
     MGHVRNYVIT DLIARFQRFK GKSVLHPMGW DAFGLPAENA AIERGISPSV WTKKNISHMK
     SQLKLLGLSV DWDREFATCD ENYYIWTQYL FLELYKAGLV YQKESEVNWD PIDNTVLANE
     QVDSEGKSWR SGALVEKKLL KQWFLRITNY ADELLKDLEK LDNWPERVKI MQDNWIGKSI
     GTNINFNINT NPEKKITVFT TRPDTLFGVT YLAISINHSL IKNISDQETI QDIENLKQYL
     KNNKNNELEK IGIKTSLIAI NPVNSEPIPI WVASYVLDEY GTGAVMGVPA HDLRDFEFAK
     KNNIDIKHVI IKDKSEKTKE LDEAYVENGY LINSNHFNGI ANTIAKLKIS EEGVNNGWAE
     NKIQYRLRDW LISRQRYWGC PIPIVNCKKC GSVPLNQSEL PVALPKDIDI SANKINALGD
     NYNWINTTCP KCGIAAKKET DTMDTFMCSS WYFLRYPSSR CSTKPFEKIE INNWLPVDQY
     VGGVEHAILH LLYARFFTKA LRDNELFEID EPFKKLLTQG MVQSAAYKNN KTGKYISPSD
     INDLSNPTDP IDNSKLEVLF EKMSKSKYNG IDPESVIKKY GADTARMFIL FKAPPEKDLE
     WGDSDVEGQF RFLSRIWKLY ISCSKDINSK SKSYPNKEKT LIKSMNIAIK EITNDISNNQ
     FNTAISELMK FYNSLSNNIN DVNNNLKIDA LKTFCILLAP FAPHISEEIW LLIGFKNSVH
     LEHWPSFNAE ALKEDSYVLV IQVNGKVRDK ININNEMNED QIKELTLKRP NILKWTQDKE
     IRKIIIVKGK IMNIVV