SYL_METBU
ID SYL_METBU Reviewed; 962 AA.
AC Q12WA2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=Mbur_1356;
OS Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS ACE-M).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX NCBI_TaxID=259564;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA Cavicchioli R.;
RT "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT burtonii: the role of genome evolution in cold adaptation.";
RL ISME J. 3:1012-1035(2009).
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; CP000300; ABE52274.1; -; Genomic_DNA.
DR RefSeq; WP_011499419.1; NC_007955.1.
DR AlphaFoldDB; Q12WA2; -.
DR SMR; Q12WA2; -.
DR STRING; 259564.Mbur_1356; -.
DR PRIDE; Q12WA2; -.
DR EnsemblBacteria; ABE52274; ABE52274; Mbur_1356.
DR GeneID; 3997572; -.
DR KEGG; mbu:Mbur_1356; -.
DR HOGENOM; CLU_004174_0_0_2; -.
DR OMA; AWNMAFQ; -.
DR OrthoDB; 4914at2157; -.
DR Proteomes; UP000001979; 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; -; 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; 2.
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..962
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000009371"
FT MOTIF 41..51
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 962 AA; 110794 MW; 735ABD6E1D31D010 CRC64;
MQQDYNSSNI EQKWQQKWNE SKVFEAEADD RDKYFITIPY PYLNGNLHAG HTRTFTIGDV
VARYKRMMGN NVLYPMGFHV TGTPIVGLAE LIQNRDPETM KVYTEFHGIP VETLKGMDTP
EKIVDYFSVE AERSMRSIGY SIDWRRKFTT TDPNYKKFIE WQFNLLYEKD LIVKGSHPVK
WCPNDDNPVE DHDILHGEEA TIIDYTLVKF KYDGMIIPCA TLRPETVFGV TNLWINPDLE
HVKIKVTFEG REEVWVVSKE AYRKLIFTDR EVEFIEDVDA SSLIGIKVTN PLNDAQVITL
PASFVKGENG SGIVMSVPSH APYDYLALRD LYDKDLREYG ITEDLRELKF ISLIKVKEFG
EFPAIEAVEQ FGVKDQDDPK AEEATKIVYR REFHGGVLKE NTGKYSGMAV SKIKDVLTRD
LIEMGIGEVF YEFSEPVVCR CGTPCVVNMV KGQWFLNYSN PEWKDKVYRC IENMDIIPED
LRVEFNNKVD WLKDKACARK KGLGTLLPFD NQWLIESLGD STIYMSYYII AKFIAMGIET
EQLVPELFDH VLLKKCSLET AAERSGIDAN IIEQISSDFE YWYPVDLRSS GKDLIPNHLL
FFLFHHVAIF DEDKWPRAIA INGFVSLEGK KMSKSKGPLL TLNDAITNYG ADISRMYILS
SAEQMQDADW KNSGIETARK QIERFYNFSK DIIGSGIPTC NVENLKGIDK WMLSRLQQRI
LETNEALDTI RTRNALQNAY FLLFNDIRWY QKRGGNALLC EVLDVWIRLM APFTPHICEE
IWEAIGHTDN DLISLADYPQ YDESLVDTQA EFTEELIGGT LSDVDEIIRV TKLTPKKAIL
YTSPEWKMET FKKALSMQKE GNLNPGILIK DLMRDPEMRS HGKEVPKFAQ KVVSDITAMN
EEKFDTLSNF DLDEKIALEE NLEFFKNELG CSVEIYSADN AEYDPENKAR FAYPLRPAIY
LE