ID   SYI_CORDI               Reviewed;        1052 AA.
AC   Q6NGD7;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=DIP1589;
OS   Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype
OS   gravis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=257309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis;
RX   PubMed=14602910; DOI=10.1093/nar/gkg874;
RA   Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G.,
RA   Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D.,
RA   De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N.,
RA   Holroyd S., Jagels K., Moule S., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Thomson N.R., Unwin L., Whitehead S., Barrell B.G.,
RA   Parkhill J.;
RT   "The complete genome sequence and analysis of Corynebacterium diphtheriae
RT   NCTC13129.";
RL   Nucleic Acids Res. 31:6516-6523(2003).
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; BX248358; CAE50114.1; -; Genomic_DNA.
DR   RefSeq; WP_010935178.1; NC_002935.2.
DR   AlphaFoldDB; Q6NGD7; -.
DR   SMR; Q6NGD7; -.
DR   STRING; 257309.DIP1589; -.
DR   EnsemblBacteria; CAE50114; CAE50114; DIP1589.
DR   KEGG; cdi:DIP1589; -.
DR   PATRIC; fig|257309.4.peg.1570; -.
DR   HOGENOM; CLU_001493_1_1_11; -.
DR   OMA; KMMAPFT; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000002198; 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   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; 2.
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..1052
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098536"
FT   MOTIF           58..68
FT                   /note="'HIGH' region"
FT   MOTIF           627..631
FT                   /note="'KMSKS' region"
FT   BINDING         630
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1052 AA;  118486 MW;  0E045969A137FBCD CRC64;
     MSDAVGGVYP RVDMSGGTNV FPDMERQVLE YWKDDETFKA SLTNREENPE YVFYDGPPFA
     NGLPHYGHLL TGYVKDIVPR YQTMKGKLVN RVFGWDCHGL PAELEAEKQL GIKDKGEIEA
     MGLESFNNYC AKSVLEYTQE WKDYVTRQAR WVDFDNGYKT MDMDFMESVM WAFKTLYDKG
     LIYQGFRVLP YSWAEHTPLS NQETRLDDSY KMRQDPTLTV TFPITGVKDD SAADASLVGA
     YALAWTTTPW TLPSNLALAV NPQVNYVEVK VGDQGAEAIR GQRVLLAEAL VGAYAKELGE
     DHEVLTVRPG SELVGLTYQP IFSYFADHEN AFQILAAEYV TTEDGTGIVH QAPAFGEDDM
     NTCKEYGIEV VIPVDMDGKF TSLVPEYQGQ LVFDANKSII ADLKAAGRVV RHQTIEHSYP
     HSWRSGEPLI YMALPSWFVE VTKIRDRMVE LNKEIDWMPS HIRDGQFGKW LEGARDWNIS
     RNRYWGSPIP VWVSDDENYP RVDVYGSLEE LERDFGVRPE SLHRPHIDEL TRPNPDDPTG
     KSTMRRVPEV LDCWFESGSM PFAQKHYPFE NKDWFDTHSP ADFIVEYSGQ TRGWFYTLHV
     LATALFDRPA FKKVVAHGIV LGDDGTKMSK SRRNYPDVNE VFNRDGSDAM RWFLMSSPIL
     RGGNLIVTEQ GIREGVRQAL LPMWNAYSFL QLYSSKPAQW SVDSSDVLDR YILAKLHDVV
     AAVGDALDNT DIARACDEVR TFCDALTNWY VRRSRDRFWA GDTEHPEAFY TLYTVLETLT
     RVTAPLLPMV SEVIWRGLTG ERSVHLADFP QADQFPADDD LVRAMDEVRG VCSATSSVRK
     AHKLRNRLPL PKVTVALPES ARLADFADII RDEVNVKEVA LTSDVDSVGR FDVVVNAKVA
     GPRLCKDVQR AIKAVKSGNY ERRGDTVVAD GIELVAGEFT ERLVAADPDS TTQIDGVDGL
     VVLDMTLTEE LEAEGWAADV IRGLQDARKA SGFEVSDRIE VKLVVPEEKK EWALRHTDMI
     AGEVLATSFE VVTGEPAEHD IVAGVTATVQ KV