ID   SYL_METCA               Reviewed;         887 AA.
AC   Q608N7;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=MCA1453;
OS   Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylococcus.
OX   NCBI_TaxID=243233;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33009 / NCIMB 11132 / Bath;
RX   PubMed=15383840; DOI=10.1371/journal.pbio.0020303;
RA   Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S.,
RA   Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E.,
RA   Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J.,
RA   Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R., Salzberg S.L.,
RA   Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., Grindhaug S.H.,
RA   Holt I.E., Eidhammer I., Jonasen I., Vanaken S., Utterback T.R.,
RA   Feldblyum T.V., Fraser C.M., Lillehaug J.R., Eisen J.A.;
RT   "Genomic insights into methanotrophy: the complete genome sequence of
RT   Methylococcus capsulatus (Bath).";
RL   PLoS Biol. 2:1616-1628(2004).
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; AE017282; AAU92547.1; -; Genomic_DNA.
DR   RefSeq; WP_010960729.1; NC_002977.6.
DR   AlphaFoldDB; Q608N7; -.
DR   SMR; Q608N7; -.
DR   STRING; 243233.MCA1453; -.
DR   PRIDE; Q608N7; -.
DR   EnsemblBacteria; AAU92547; AAU92547; MCA1453.
DR   KEGG; mca:MCA1453; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000006821; 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   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; Reference proteome.
FT   CHAIN           1..887
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152042"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           624..628
FT                   /note="'KMSKS' region"
FT   BINDING         627
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   887 AA;  99746 MW;  72535449F9AD8F20 CRC64;
     MEETYNPKTV EETAQRIWEE SGVFRAREDS GREKFYCLSM FPYPSGRLHM GHVRNYTIGD
     VIARYQRMRG KNVLQPMGWD AFGLPAENAA MQNGVTPAAW TDANADYMRK QLKSLGLAVD
     WDREIATCKP EYYRWEQWLF TRLFEKGLIY KKTAPVNWDP VDQTVLANEQ VIDGRGWRSG
     ALVEKRDIPM YFMRITAYAE ELLAELDDLP GWPEQVKTMQ RNWIGKSHGC EVHFPYEDGS
     DVLKVYTTRP DTLMGATYVA VAAEHPLALE AARDNPELAA FIEECRHGGT AEADLATMEK
     KGMATGRFVV HPLNGEKLPV WIANYVLWGY GEGAVMAVPA HDERDFEFAN KYGLPIKTVI
     VSTVGAYETV DTKGGWIDAY AEHGRCTNSG KYDGLAFQQA FDAIAADLEA KGLGQKRTQF
     RLRDWGISRQ RYWGCPIPII HCLSCGDVPV PAEQLPVVLP EDVTIDVGSP LKKMPEWYST
     TCPKCGGAAE RETDTMDTFV ESSWYYARYT CPDNTEAMLD RRADYWLPVD QYVGGIEHAI
     LHLLYARFFH KLMRDAGLVH CDEPFTNLLT QGMVVAPTFY REEGGKKHYF GPTEVELSTD
     ERGRPLGATL KSDGAPVTVG HIEKMSKSKN NGVDPEALID RYGADTVRLF TMFAAPPDQS
     LEWSDSGVEG AFRFLKRLWT RAAFSVNTAF SQYGRDELRV TDWALVPLAP NHKEARRMIH
     ATLKQANFDF VRHQFNTVVS AAMKILNTLA DDKGFWNCDH LPEGDEKDAF RRSAAVVAFE
     GYSLLTRLLY PIAPHICDAL WRQLMPGTDI LDAGWPEVDE AALAQDEIEL VVQVNGKLRG
     KITVPADASR ETVEQIALAD AQVLRFVEGK PPKRVIVVPG KLVNVVA