ID   SYI_MYCLE               Reviewed;        1059 AA.
AC   Q9X7E5;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Isoleucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02003};
DE            EC=6.1.1.5 {ECO:0000255|HAMAP-Rule:MF_02003};
DE   AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02003};
DE            Short=IleRS {ECO:0000255|HAMAP-Rule:MF_02003};
GN   Name=ileS {ECO:0000255|HAMAP-Rule:MF_02003}; OrderedLocusNames=ML1195;
GN   ORFNames=MLCB458.10;
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   -!- FUNCTION: Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS
CC       can inadvertently accommodate and process structurally similar amino
CC       acids such as valine, to avoid such errors it has two additional
CC       distinct tRNA(Ile)-dependent editing activities. One activity is
CC       designated as 'pretransfer' editing and involves the hydrolysis of
CC       activated Val-AMP. The other activity is designated 'posttransfer'
CC       editing and involves deacylation of mischarged Val-tRNA(Ile).
CC       {ECO:0000255|HAMAP-Rule:MF_02003}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-
CC         isoleucyl-tRNA(Ile); Xref=Rhea:RHEA:11060, Rhea:RHEA-COMP:9666,
CC         Rhea:RHEA-COMP:9695, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58045, ChEBI:CHEBI:78442, ChEBI:CHEBI:78528,
CC         ChEBI:CHEBI:456215; EC=6.1.1.5; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_02003};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02003};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02003}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02003}.
CC   -!- DOMAIN: IleRS has two distinct active sites: one for aminoacylation and
CC       one for editing. The misactivated valine is translocated from the
CC       active site to the editing site, which sterically excludes the
CC       correctly activated isoleucine. The single editing site contains two
CC       valyl binding pockets, one specific for each substrate (Val-AMP or Val-
CC       tRNA(Ile)). {ECO:0000255|HAMAP-Rule:MF_02003}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       IleS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02003}.
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DR   EMBL; AL049478; CAB39575.1; -; Genomic_DNA.
DR   EMBL; AL583921; CAC31576.1; -; Genomic_DNA.
DR   PIR; E87058; E87058.
DR   RefSeq; NP_301871.1; NC_002677.1.
DR   RefSeq; WP_010908192.1; NC_002677.1.
DR   AlphaFoldDB; Q9X7E5; -.
DR   SMR; Q9X7E5; -.
DR   STRING; 272631.ML1195; -.
DR   EnsemblBacteria; CAC31576; CAC31576; CAC31576.
DR   KEGG; mle:ML1195; -.
DR   PATRIC; fig|272631.5.peg.2194; -.
DR   Leproma; ML1195; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_1_1_11; -.
DR   OMA; KMMAPFT; -.
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:0004822; F:isoleucine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd07961; Anticodon_Ia_Ile_ABEc; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   Gene3D; 3.90.740.10; -; 1.
DR   HAMAP; MF_02003; Ile_tRNA_synth_type2; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR033709; Anticodon_Ile_ABEc.
DR   InterPro; IPR002301; Ile-tRNA-ligase.
DR   InterPro; IPR023586; Ile-tRNA-ligase_type2.
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; PTHR42780; PTHR42780; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   PRINTS; PR00984; TRNASYNTHILE.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00392; ileS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc.
FT   CHAIN           1..1059
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098548"
FT   MOTIF           59..69
FT                   /note="'HIGH' region"
FT   MOTIF           637..641
FT                   /note="'KMSKS' region"
FT   BINDING         640
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1059 AA;  119809 MW;  67FC7659E9399E39 CRC64;
     MTNSAYPRTD LGADQRGGSP NFPALEAQVL DYWSNDDTFR ASIARCDDAP EYVFYDGPPF
     ANGLPHYGHL LTGYVKDIVP RYRTMCGYKV ERRFGWDTHG LPAELEVERQ LGITDKSQID
     AMGIAAFNEA CRKSVLRYTE EWQAYVTRQA RWVDFDNDYK TLDLSYMESV IWAFKQLWDK
     GLAYESYRVL PYCWRDETPL SNHELRMDDD VYQSRQDPAV TLGFKVLGGD DEDLVGAYLL
     VWTTTPWTLP SNLAVAVHPD VTYVDVRAGD RRFVLAQARL TAYARELGDE PEVLATYRGA
     DLLGRHYLPP FQYFYESARN AFQVLPGDFV TTDDGTGIVH IAPAYGEDDM ATADKVGIVP
     VTPVDSNGCF DATVPDYQGQ HVFEANAQII RDLKNQSGSA AVNGAVLLRH ETYEHPYPHC
     WRCRNPLIYR AVSSWFVAVT EFRDRMVELN QQITWYPEHV KDGQFGKWLQ GARDWSISRN
     RYWGTPIPVW KSDDPDYPRI DVYGSLDELE RDFGVRPTNL HRPYIDELTR PNPDDPTGLS
     TMRRIPDVFD VWFDSGSMPY AQVHYPFEND DWFDGFDSAD SDKQVDAHYP GDFIVEYIGQ
     ARGWFYTLHV LATALFDRPA FKTCIAHGVV LGSNGQKMSK SLRNYPDVTE IFDRDGSDAM
     RWFLMASPIL RGGNLIITEP GIREGMRQVL LPLWNAYSFL ALYAPKIGTW HTDVSHVLDR
     YILAKLAVLR DDLSQAMEVC DISGACEQLR QFTEPLTNWY LRRSRARFWD EDVDAIDTLH
     TVLEVTARLA APLLPLITEI IWRSVTGGRS VHLTDWPQAN QLPADPDLVA VMDQVRQVCS
     AASSLRKAKK LRVRLPLPKL VVAVYNSQRL KPYIDLIGDE LNVKQIELTD AIDTYGRFEF
     TVNARVAGPR LGRDVQAAIK VVKAGEGVAN PDGTLTAGPV VLQPDEYSSR LVAANPEFTA
     ELPDGSGLVV LDDTVTPELE AEGWAKDRIR ELQELRKLIG LDVSDRIRVL MSVPAERADW
     ARVHRDFIAR EILATSFEFG EPADSVAIGD GVRVSLLKV