ID   SYL_MARMS               Reviewed;         815 AA.
AC   A6VZE7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=Mmwyl1_2915;
OS   Marinomonas sp. (strain MWYL1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=400668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MWYL1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y.,
RA   Richardson P.;
RT   "Complete sequence of Marinomonas sp. MWYL1.";
RL   Submitted (JUN-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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000749; ABR71826.1; -; Genomic_DNA.
DR   RefSeq; WP_012070602.1; NC_009654.1.
DR   AlphaFoldDB; A6VZE7; -.
DR   SMR; A6VZE7; -.
DR   STRING; 400668.Mmwyl1_2915; -.
DR   PRIDE; A6VZE7; -.
DR   EnsemblBacteria; ABR71826; ABR71826; Mmwyl1_2915.
DR   KEGG; mmw:Mmwyl1_2915; -.
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   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; 2.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 2.
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..815
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000074837"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           574..578
FT                   /note="'KMSKS' region"
FT   BINDING         577
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   815 AA;  91770 MW;  A883C6875172BEBB CRC64;
     MQEQYNPQQI EQAAQSFWDE NKVFKAIADS SKEKFYCLSM FPYPSGRLHM GHVRNYTIGD
     VISRYQRMQG KNVLQPMGWD AFGLPAENAA IKHKTAPAKW TTENIAYMKG QLKELGFGYD
     WDREIATCTP EYYKWEQWFF TQLVEKGLAY KKTAAVNWCP EDQTVLANEQ VEDGCCWRCG
     TNVEKKEISQ WFIRITDYAE ELLNDLDQLD GWPEKVKAMQ RNWIGRSEGL EFSFAVEGKD
     ERLSVYTTRP DTIMGVTYVA VATQHPLSLE ASANNADLAA FIEESKKMST TEADMATVEK
     KGMDTGFKAI HPITGEAVPV YAANFVLMDY GSGAVMSVPA HDQRDFEFAK KYNLAIKQVV
     QPAGDEVIDL EKAAFTEKGV LCNSGEFDGL AFKEAFDAIA AWMVERNLGE VKVNYRLRDW
     GVSRQRYWGT PIPTINLKDG SVVPVPQDQL PVELPTDVIM DGVNSPIKNN PDFSSIMFNG
     EEAERETDTF DTFMESSWYF ARYCCPDSTD AMLTEEANYW LPVDQYVGGV EHAILHLLYS
     RFFHKLLRDA GLVNSDEPFK RLLTQGMVNK DGTKMSKSKG NTVDPQEMIE KYGADTVRLF
     MMFSAPPEQS LEWNDAGVDG ASRFLRRLWA LSYRHTNAGK VGELNIAELN GAQKALRRKT
     HETIQKVSDD IERRQTFNTA IAAVMELCNE ISKFEDSSEL GLAVEQEALE AATLLLSPIV
     PHIAHQLWSE LGHSDNIVNT PWPTLDEEAL IKDELTIVVQ VLGKKRAELT VSANADNKTI
     EAEALAHPSV AKLLEGKTVR KVIVVPGRLV NIVAN