SYL_MYCLE
ID SYL_MYCLE Reviewed; 972 AA.
AC Q50192;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 2.
DT 03-AUG-2022, entry version 131.
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=ML0032;
GN ORFNames=MLB1770.20, MLCB628.03;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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; Y14967; CAA75192.1; -; Genomic_DNA.
DR EMBL; Z70722; CAA94727.1; -; Genomic_DNA.
DR EMBL; AL583917; CAC29540.1; -; Genomic_DNA.
DR PIR; T10023; T10023.
DR RefSeq; NP_301156.1; NC_002677.1.
DR RefSeq; WP_010907481.1; NC_002677.1.
DR AlphaFoldDB; Q50192; -.
DR SMR; Q50192; -.
DR STRING; 272631.ML0032; -.
DR EnsemblBacteria; CAC29540; CAC29540; CAC29540.
DR KEGG; mle:ML0032; -.
DR PATRIC; fig|272631.5.peg.40; -.
DR Leproma; ML0032; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_11; -.
DR OMA; TFMVLAP; -.
DR Proteomes; UP000000806; 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 Gene3D; 3.90.740.10; -; 1.
DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
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 PANTHER; PTHR43740; PTHR43740; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR Pfam; PF09334; tRNA-synt_1g; 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..972
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000152046"
FT MOTIF 78..89
FT /note="'HIGH' region"
FT MOTIF 741..745
FT /note="'KMSKS' region"
FT BINDING 744
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
FT CONFLICT 659..668
FT /note="GGAEHAVLHL -> AEPNMRCYIC (in Ref. 1; CAA94727)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 972 AA; 108408 MW; 65286839DA51AFAE CRC64;
MTELPTTVPG YNSAVAQTDS DAMRYRYTAE LAGRIESTWQ DNWARLQTFN VPNPVGSLAP
PDGSVVPADK LFVQDMFPYP SGDGLHVGHP LGYIATDVYA RYFRMTGHNV LHAMGFDAFG
LPAEQYAMQT GTHPRILTEA NVVNFRHQLG RLGLGHDSRR TFSTTDVEFY KWTQWIFLQI
YNAWFDVAAN KARPIAELIA EFDSGERRLV DGRDWATLSA GERADVIDNC RLVYRADSMV
NWCPGLGTVL ANEEVTADGR SDRGNFPVFR KRLRQWMMRI TAYADRLLDD LDLLDWPEQV
KTMQRNWIGR SSGATVLFSA ILSRSDAATT EVDVEVFTTR PDTMFGVTYL VLAPEHNLVD
ELVATVWPDR TDPRWTYGAA TPGAAVAAYR RAIVAKSDLD RQESKEKTGV FLGRYATNPA
TGKPVPIFVA DYVLVGYGTG AVMAVPGHDP RDWDFAHKFH LPIVEVIAGS DISEAAYVGD
GVLVNSGYLD GMDVATAQEA ITARLESEGR GHARIEFKLR DWLFARQRYW GEPFPIIYDS
DGRPHALDEA ALPVELPDVP YYSPVLFDPD DADSEPSPPL AKATEWVHVE LDLGDGLKPY
SRDTNVMPQW AGSSWYELRY TDPHNSERLC AKENEAYWMG PRPTEHGIDD PGGVDLYVGG
AEHAVLHLLY ARFWHKVLYD LGHVSSREPY RRLINQGYIQ AFAYTDAHGS YVPANQVFQR
GDGFFCPGPD GEIEVFQEFG KIGKSLKNSV SPDEICDEYG ADTLRVYEMS MGPLEASRPW
ATKDVVGAYR FLQRVWRLVV DERTGETRVV DTAGELDTYT LRTLHRTIAG VSQDYAALRN
NTATAKLIEY TNHLTKEHRG SVPRVAVEPL VLMLAPLAPH LAEELWLRLG HTTSLANGPF
PQADPAYLVD DTVEYPVQVN GKIRGRIVVA ADADYDTLKT VALADDKVQQ FLAGATPRKV
IVVAGRLISL VI
