SYL_ZYMMO
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 03-AUG-2022, entry version 108.
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=ZMO1435;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Proteobacteria; 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 EnsemblBacteria; AAV90059; AAV90059; ZMO1435.
DR GeneID; 58027172; -.
DR KEGG; zmo:ZMO1435; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_5; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
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 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; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 3.
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; 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
