ID   SYL_PROM3               Reviewed;         878 AA.
AC   A2C9U0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 100.
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=P9303_15061;
OS   Prochlorococcus marinus (strain MIT 9303).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=59922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9303;
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; CP000554; ABM78250.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2C9U0; -.
DR   SMR; A2C9U0; -.
DR   STRING; 59922.P9303_15061; -.
DR   KEGG; pmf:P9303_15061; -.
DR   HOGENOM; CLU_004427_0_0_3; -.
DR   BioCyc; PMAR59922:G1G80-1303-MONOMER; -.
DR   Proteomes; UP000002274; 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; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
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   NCBIfam; TIGR00396; leuS_bact; 1.
DR   PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 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; 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.
FT   CHAIN           1..878
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009393"
FT   MOTIF           56..66
FT                   /note="'HIGH' region"
FT   MOTIF           630..634
FT                   /note="'KMSKS' region"
FT   BINDING         633
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   878 AA;  98546 MW;  D9528F8690422D93 CRC64;
     MTESFPSTSA SSHSSARYDP IELETRWQKE WLRQGLDRTP VAETNQKRFY ALSMFPYPSG
     KLHMGHVRNY VITDVIARVQ RMRGDAVLHP MGWDAFGLPA ENAAIARNVD PGDWTDQNIA
     QMRAQLDRLG LSIDWDRQQA TCHQDYYRWT QWLFLELFAG GLAYQKEATV NWDPIDKTVL
     ANEQVDGEGR SWRSGALVEQ RQLKQWFLRI TDYADALIDD LDELTGWPER VRTMQANWIG
     RSHGAEIKFR VAGQTNSIIT VFTTRPDTLH GASYVVLAPE HPLVEALTSP QQRIAVTAFC
     DLISQLSVKD RTAEDQPKRG VPIGAQVINP VNGESLPVWI ADYVLADYGS GAVMGVPAHD
     ERDFIFARSH ELPIRIVVQM PDSDEHHNDG QAWTGAGVLV NSGAFDGLST EEGKVAITTH
     GASKGWAQSK VQYRLRDWLI SRQRYWGCPI PIIHCASCGI VPVPQEDLPV TLPRDIDLSG
     KGGSPLAQEQ DWVEVKCPIC GEKAHRETDT MDTFMCSSWY YLRFADPLNS QRPFDKDIVD
     EWLPVDQYVG GIEHAILHLL YARFFTKALH DRNLIGFKEP FNTLLTQGMV QGLTYRNTKN
     GSYISPELVS DEGDPRDPES GDKLEILFEK MSKSKYNGVD PAVVIDRYGA DTARMFILFK
     APPEKDLEWD DADVEGQFRF LQRLIRLIDS FVWPKTDEDN ASISSANLTI SSADLSEEEI
     NMRRATHMAI EAITEDLSGD IQLNTAISEL MKLSNSLGGK LDKVRTEVAA EALSVLVRLM
     APFAPHLAEE FWMKLHGQGS IHQQSWPIID PSALVLETIE LVIQVKGKVR GTIQVPANAD
     KTALEELALK SDIAVKWLEG QSPRRVIIVP GKLVNLVP
//