ID   SYL_PSYWF               Reviewed;         885 AA.
AC   A5WGH9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=PsycPRwf_1830;
OS   Psychrobacter sp. (strain PRwf-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=349106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PRwf-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Psychrobacter sp. PRwf-1.";
RL   Submitted (MAY-2007) 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; CP000713; ABQ94770.1; -; Genomic_DNA.
DR   RefSeq; WP_011961047.1; NC_009524.1.
DR   AlphaFoldDB; A5WGH9; -.
DR   SMR; A5WGH9; -.
DR   STRING; 349106.PsycPRwf_1830; -.
DR   PRIDE; A5WGH9; -.
DR   EnsemblBacteria; ABQ94770; ABQ94770; PsycPRwf_1830.
DR   KEGG; prw:PsycPRwf_1830; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
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   Gene3D; 3.90.740.10; -; 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   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.
FT   CHAIN           1..885
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334799"
FT   MOTIF           53..63
FT                   /note="'HIGH' region"
FT   MOTIF           631..635
FT                   /note="'KMSKS' region"
FT   BINDING         634
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   885 AA;  99051 MW;  7CCF3ED1AB03D728 CRC64;
     MSTTAPEQNN PNHYHPQAIE AEQQAKWAAD KRFEVSNDIS KDANTRYMLS MFPYPSGKLH
     MGHVRNYTIS DVLSRYYRLK GDQVLQPMGW DAFGMPAENA AIANQVAPAK WTFSNIDNMR
     AQLKTLGLSI DWSREFATCT PEYYRWEQWF FLQLYKKGLV YKKLATVNWD PVDNTVLANE
     QVVDGKGWRS GAPVEKRDIP MYYFKITDYA DELLDDLDKL EGQWPSDVIT MQRNWIGRSQ
     GMEVHFPYKN SDDISTLDVF TTRPDTLMGV TYVAVAAEHR LAKLAAEKDP KIAEFCELCK
     KGSVAEADLA KAEKIGMDTG LTVTHPLTGE EVPVWVANYV LMSYGSGAVM AVPAHDERDF
     EFANKYNLPI KTVIKTPEDH EGAYTERGTL VNSGEFDGLD FDGSFEAMLA KLEPQKLAAR
     KIQYRLRDWG VSRQRYWGCP IPMINCEYCG NVPVDEADLP IKLPTDVVPD GRGNPLKNIP
     EFVNTTCPKC GGPAERETDT FDTFMESSWY YARFASPNDD TQMVEKAAAD KWLPVDQYVG
     GVEHAVMHLL YARFYHKLMR DEGLVSGDEP FKNLLTQGMV LAGTLYRDNP EGGKTYYFAD
     DVEISYDDRG QPTQAILKAD GQPVTIGKIE KMSKSKNNGV DPQTTIDQYG ADTVRLYTLF
     AAPADQTLEW SDDSLKGPYN FLKKVWRETQ SHLEATQELG LQVANLPAAS SIDASQLDSL
     AKGLRRKTHE VITKIDNDLG ERLSLNTPVS SLMELANEIG TFISKNQQIN EHTLAVQHEA
     LVTLLTLLSV YAPHIGEHLL EKLGVDTTRL RYPEADSAAL VQDTITMVVQ VNGKVRGKME
     VAPGTDAESL KAQAKAIESV AKYLTGDIKK EIVVPNKLVN IVVAG