ID   Q6KHA5_MESM1            Unreviewed;       630 AA.
AC   Q6KHA5;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 131.
DE   RecName: Full=leucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013164};
DE            EC=6.1.1.4 {ECO:0000256|ARBA:ARBA00013164};
GN   Name=leuS {ECO:0000313|EMBL:AAT28025.1};
GN   OrderedLocusNames=MMOB5390 {ECO:0000313|EMBL:AAT28025.1};
OS   Mesomycoplasma mobile (strain ATCC 43663 / 163K / NCTC 11711) (Mycoplasma
OS   mobile).
OC   Bacteria; Mycoplasmatota; Mycoplasmoidales; Metamycoplasmataceae;
OC   Mesomycoplasma.
OX   NCBI_TaxID=267748 {ECO:0000313|EMBL:AAT28025.1, ECO:0000313|Proteomes:UP000009072};
RN   [1] {ECO:0000313|EMBL:AAT28025.1, ECO:0000313|Proteomes:UP000009072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43663 / 163K / NCTC 11711
RC   {ECO:0000313|Proteomes:UP000009072};
RX   PubMed=15289470; DOI=10.1101/gr.2674004;
RA   Jaffe J.D., Stange-Thomann N., Smith C., DeCaprio D., Fisher S., Butler J.,
RA   Calvo S., Elkins T., FitzGerald M.G., Hafez N., Kodira C.D., Major J.,
RA   Wang S., Wilkinson J., Nicol R., Nusbaum C., Birren B., Berg H.C.,
RA   Church G.M.;
RT   "The complete genome and proteome of Mycoplasma mobile.";
RL   Genome Res. 14:1447-1461(2004).
RN   [2] {ECO:0007829|PDB:3ZIU}
RP   X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS).
RX   PubMed=23431144; DOI=10.1073/PNAS.1218374110;
RA   Li L., Palencia A., Lukk T., Li Z., Luthey-Schulten Z.A., Cusack S.,
RA   Martinis S.A., Boniecki M.T.;
RT   "Leucyl-tRNA synthetase editing domain functions as a molecular rheostat to
RT   control codon ambiguity in Mycoplasma pathogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:3817-3822(2013).
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:0000256|ARBA:ARBA00001372};
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594}.
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DR   EMBL; AE017308; AAT28025.1; -; Genomic_DNA.
DR   RefSeq; WP_011265059.1; NC_006908.1.
DR   PDB; 3ZIU; X-ray; 2.07 A; A/B=1-630.
DR   PDBsum; 3ZIU; -.
DR   AlphaFoldDB; Q6KHA5; -.
DR   SMR; Q6KHA5; -.
DR   STRING; 267748.MMOB5390; -.
DR   KEGG; mmo:MMOB5390; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_14; -.
DR   OrthoDB; 9810365at2; -.
DR   BRENDA; 6.1.1.4; 10542.
DR   Proteomes; UP000009072; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR002302; Leu-tRNA-ligase.
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   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; 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.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:3ZIU};
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000313|EMBL:AAT28025.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AAT28025.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009072}.
FT   DOMAIN          10..431
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          478..595
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   630 AA;  74275 MW;  BFFD6A92E79B2F2E CRC64;
     MYNHNEIEKK WQTRWEKTKA FKTTNKSKDK FYALDMFPYP SGSGLHVGHP EGYTATDIIS
     RYKRLKGFDV LHPIGWDAFG LPAEQYALSS GKHPQPFTLK NIENFRRQLK SLGFSFDYEK
     EVNTTDPSYY RWTQWIFKQI YKKGLAEIRE VDVNWCPGLG TVLANEEIVE NDKGEMVSER
     GSFPVYKKPM KQWVLKITNY ADRLLEDLNL LDWPDSLKKL QTNWIGKEEI DGKITYKLQD
     WIFARQRYWG EPFPVYFDED NNVYLIDELV ELPHMENIMP SGTGEGPLAT NTEWVQYKKN
     NKIFKRDTNT MPQWAGSCWY YLAYIMKQED GTYLPIDSKK AYEAFSKWLP VDLYIGGQEH
     AVLHLLYARF WHKILYDLKI VPTKEPFQKL INQGMILGKD GQKMSKSLGN VVNPDEIIQN
     FGADTLRVYE MFMGPLTDTK KWNESTVEAT YKWILRVKRI FQIFIEDKSK INSLHKDDQF
     ISEHNLLIKE ITQDIEDLKF NIMISKLMIF VNSLYKKEKI YSLKPLKDFA IMFSTIAPHI
     SEELLESLGE KEIMFQSWPT YENNKILLTK DIVAIQVNGK LRETFEIEND WDEKRVIEEA
     KKLPNVKKHL ENKIIKKEIY IAKKILNFII
//