ID   SYL_NOVAD               Reviewed;         848 AA.
AC   Q2G3C3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=Saro_3215;
OS   Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CCUG
OS   56034 / CIP 105152 / NBRC 16084 / F199).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=279238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700278 / DSM 12444 / CCUG 56034 / CIP 105152 / NBRC 16084 /
RC   F199;
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., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N.,
RA   Fredrickson J., Balkwill D., Romine M.F., Richardson P.;
RT   "Complete sequence of Novosphingobium aromaticivorans DSM 12444.";
RL   Submitted (JAN-2006) 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; CP000248; ABD27650.1; -; Genomic_DNA.
DR   RefSeq; WP_011446852.1; NC_007794.1.
DR   AlphaFoldDB; Q2G3C3; -.
DR   SMR; Q2G3C3; -.
DR   STRING; 279238.Saro_3215; -.
DR   PRIDE; Q2G3C3; -.
DR   EnsemblBacteria; ABD27650; ABD27650; Saro_3215.
DR   KEGG; nar:Saro_3215; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000009134; 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..848
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334784"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           51..61
FT                   /note="'HIGH' region"
FT   MOTIF           625..629
FT                   /note="'KMSKS' region"
FT   BINDING         628
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   848 AA;  94260 MW;  D2C85B84C8D6C88B CRC64;
     MTENTPGTSA PERFDPATAD TRWQRVWDEK QSFRADDSST KPRSYVLEMF PYPSGRIHIG
     HVRNYTMGDV LARYKRMRGF EVLHPMGWDA FGMPAENAAM EKGVHPGGWT RDNIANMKAQ
     LKRLGFALDW SREIATCEPE YYGQEQALFL DLYAAGLVYR KESTVNWDPV DMTVLANEQV
     IDGRGWRSGA LVEKRKLNQW FLKITDFADE LLEGLSTLDK WPEKVRVMQE NWIGKSQGLQ
     FRFDLSNGET VEVYTTRPDT IFGASFVAVA PDHPIAQGVA AINCEAANFI ALCKKGGTTA
     AELETAEKLG FDTGIGARHP LTGKYLPVYI ANFVLMEYGT GAIMAVPGHD QRDFDFATKY
     ALPILRVVAA DAADADKPFA GEAEAGDGVL VNSGFLDGMN VADAKAAVIV RAESEGWGEG
     KTVWRLRDWG VSRQRYWGTP IPFIHCEVCG VVPVPKKHLP VTLPEDVSFD VPGNPLDRHP
     TWKHVDCPQC GHPARRETDT LDTFVDSSWY FLRFASQPED RPFDPEEIKR WLPVEQYIGG
     IEHAILHLLY ARFWTRALAR IGKVEVTEPF GSLFTQGMVT HETYERRNPE NGQPIFFSPG
     EVERTGEGAT LKVDGAPVEI GRVIKMSKSK KNVVDPDEIV AKYGADAIRW FMLSDSPPER
     DLPWSEAGIE GCARFVQRLW RLFGQYDAAA TGEDKALDRK AHQTVHAVAS DIEALGFNKA
     VARIYELTGA VEKAAPSASR SDAIRKLLLL VAPMMPHLAE EAYARFGSSL IADAAWPEVD
     PALLVDDEVI VAVQVKGKLR DTLTVAKGTP KEDLERLALA SEKVQRALEG AEVKKVIVVP
     DRLVNLVA