ID   SYL_METAC               Reviewed;         961 AA.
AC   Q8TQD3;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 122.
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=MA_1611;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(2002).
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; AE010299; AAM05024.1; -; Genomic_DNA.
DR   RefSeq; WP_011021621.1; NC_003552.1.
DR   AlphaFoldDB; Q8TQD3; -.
DR   SMR; Q8TQD3; -.
DR   STRING; 188937.MA_1611; -.
DR   PRIDE; Q8TQD3; -.
DR   EnsemblBacteria; AAM05024; AAM05024; MA_1611.
DR   GeneID; 1473499; -.
DR   KEGG; mac:MA_1611; -.
DR   HOGENOM; CLU_004174_0_0_2; -.
DR   InParanoid; Q8TQD3; -.
DR   OMA; AWNMAFQ; -.
DR   OrthoDB; 4914at2157; -.
DR   PhylomeDB; Q8TQD3; -.
DR   Proteomes; UP000002487; 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; IBA:GO_Central.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IBA:GO_Central.
DR   Gene3D; 3.40.50.620; -; 1.
DR   Gene3D; 3.90.740.10; -; 1.
DR   HAMAP; MF_00049_A; Leu_tRNA_synth_A; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR020791; Leu-tRNA-lgase_arc.
DR   InterPro; IPR004493; Leu-tRNA-synth_Ia_arc/euk.
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; PTHR45794; PTHR45794; 2.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00395; leuS_arch; 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..961
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152130"
FT   MOTIF           41..51
FT                   /note="'HIGH' region"
FT   MOTIF           632..636
FT                   /note="'KMSKS' region"
FT   BINDING         635
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   961 AA;  110402 MW;  8DC8CE4760800A86 CRC64;
     MEQDYKPHEI EEKWQKKWNE SLIFQADPDK REKFFITIPY PYLNGNLHAG HTRTFTIGDV
     VARHKRMLGY NVLYPMGFHV TGTPIVGLAE LIASRDPQTM DVYEHLHGIP GDILPTLDTP
     EKIVDYFKRE AEKAMRMIGY SIDWRRKFTT TDPTYKKFIE WQYIRLEEKG LIVKGSHPVK
     WCPNDNNPVE DHDILYGEEA TIVEYTLIKF RYNDLVLPCA TLRPETTFGV TNLWVNPDVD
     YVKARVEKDG NEEFWVVSKE AFRKLTFTDR TVEYVEDVPA KSIIGIKLTN PITGDEVISL
     PASFVKPENG SGIVMSVPAH APFDYLALRD LYDADLSEYG ITEDLRDIKL ISLIQVPEFG
     EFPAKEIVES MGIANQKAPK AEEATKIVYR REFHGGVLKE ITGKYRGYPV SKIKDVLTRD
     LIASNAGETF YEFSEPVVCR CGTPCVVNMV KGQWFLNYSN PEWKAKVYKC LSQMRIIPEE
     YRVEFENKVD WLKDKACARR KGLGTRLPFD KEWLIESLGD STIYMSYYII ARFLERGDLA
     LEQLTLSFFD YVLLGIGDSA AVSAETGLKQ ELVEEIRSHF NYWYPVDLRS SGKDLVPNHL
     LFFLFHHVAL FEEEKWPRAL AVNGFVSLEG QKMSKSKGPI LTLESAVSAY GADITRMYIL
     STAEQTQDAD WQKTGIDSAR RQVDRFYSFA KDVIESGKRA TLSTELKLID RWMLSRMQKY
     IMETNIALDS IQTREAIQNS FFLLINDVRW YQRRGGEALL YYVLDNWVRL MAPFTPHLCE
     EIWEAMGHED PISLAQYPLD NEDLIDEGAE LAEEAVKSTL NDIEEIVRVT KMTPQKVYLY
     TAPAWKAEAI RCACELQIEA PLEVGALIKT LMANPELKRF GKEIPKFVQK IIPEFKSGGA
     ERYETFAYLG LDEQALLKES ASFLEKEIGC PVEIYSADSP EYDPQKKSRF AEPLRPAIYI
     E