ID   SYL_ZYMMO               Reviewed;         846 AA.
AC   Q5NMK1;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 114.
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=ZMO1435;
OS   Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Zymomonadaceae; Zymomonas.
OX   NCBI_TaxID=264203;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RX   PubMed=15592456; DOI=10.1038/nbt1045;
RA   Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA   Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA   Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA   Kang H.S.;
RT   "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT   ZM4.";
RL   Nat. Biotechnol. 23:63-68(2005).
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; AE008692; AAV90059.1; -; Genomic_DNA.
DR   RefSeq; WP_011241216.1; NZ_CP035711.1.
DR   AlphaFoldDB; Q5NMK1; -.
DR   SMR; Q5NMK1; -.
DR   STRING; 264203.ZMO1435; -.
DR   KEGG; zmo:ZMO1435; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   Proteomes; UP000001173; 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   CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 2.20.28.290; -; 1.
DR   Gene3D; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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; 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   NCBIfam; TIGR00396; leuS_bact; 1.
DR   PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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..846
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152126"
FT   MOTIF           47..57
FT                   /note="'HIGH' region"
FT   MOTIF           621..625
FT                   /note="'KMSKS' region"
FT   BINDING         624
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   846 AA;  95428 MW;  3A727DDA60F0CB44 CRC64;
     MSESGFSQRF NPHVVDGRWQ KKWEESGCFH AKDNSDRPHS YILEMFPYPS GRIHMGHVRN
     YTMGDVLARY YRMKGHEVLH PMGWDAFGMP AENAAMERKI HPREWTMSNI ATMREQLKRI
     GFAIDWSREL ATCEPSYYGQ EQALFLDLYK AGLVYRKESA VNWDPIDNTV LANEQVIDGR
     GWRSGALVER KKLNQWFLKI TEFADDLLDG LKDLDQWPEK VRSMQENWIG RSQGMQFHFN
     FEVAPEGFDK IEVFTTRPDT LFGASFVAIA CDHPIAKALA EKNAALPEFI ADCQKMGTAA
     EDIETAEKKG FDTGLSLVHP LNPELKLPLF VANFVLMDYG TGAVFGCPAH DQRDLDFALK
     YNLPVKRVVA PSEAESNEAI GDKADTRAGI MVNSSFLDGL SSEEAKKTVI ARAEKEGWGK
     GTTVFRLRDW GVSRQRYWGT PIPIIHCDSC GAVPVPKDQL PVTLPDDINF DKPGNPLERH
     PTWKNVTCPK CGKPARRETD TLDTFVDSSW YFIRFASQPD DKPFDKATAE KWLPVGQYIG
     GVEHAILHLL YARFWTRALQ SIGRLDIKEP FTGLFTQGMV THETYKDPEG HWLSPEQIHK
     DEAGIFLTES GEKVTVGRVE KMSKSKKNVV EPAPILDQYG ADAVRWFMLS DSPPERDLAW
     TEAGIEGCWR FMQRLWRVAA IASEEASAGI DKDLQHRLHC SIKEVGEAIE GLSFNKAIAK
     IHDLVNAIEK AKASATRKEA ALTLFRLVAP MVPHLSEEAW HLLEKEGFVA EASWPEFDPA
     LTVEDEITIA VQVNGKLRDT LTVARDMPKD EAEKLALASE KVIKMLEGRS PKKVIVVPNR
     LVNIVA
//