ID   SYI_CORGL               Reviewed;        1054 AA.
AC   Q8NNP0; Q6M3S6;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 119.
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};
GN   OrderedLocusNames=Cgl2148, cg2359;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA   Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA   Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA   Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA   Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT   impact on the production of L-aspartate-derived amino acids and vitamins.";
RL   J. Biotechnol. 104:5-25(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; BA000036; BAB99541.1; -; Genomic_DNA.
DR   EMBL; BX927154; CAF20488.1; -; Genomic_DNA.
DR   RefSeq; NP_601350.1; NC_003450.3.
DR   RefSeq; WP_011014916.1; NC_006958.1.
DR   AlphaFoldDB; Q8NNP0; -.
DR   SMR; Q8NNP0; -.
DR   STRING; 196627.cg2359; -.
DR   KEGG; cgb:cg2359; -.
DR   KEGG; cgl:Cgl2148; -.
DR   PATRIC; fig|196627.13.peg.2086; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_1_1_11; -.
DR   OMA; KMMAPFT; -.
DR   Proteomes; UP000000582; 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..1054
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098538"
FT   REGION          522..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   1054 AA;  117404 MW;  C3333C86C8554B1F CRC64;
     MSEAVGGVYP QVDLSGGSSR FPEMEENVLS YWKKDDTFQA SIDQRDGAED YVFYDGPPFA
     NGLPHYGHLL TGYVKDIVPR YQTMRGYRVP RVFGWDTHGL PAELEAEKQL GIKDKGEIEA
     MGLAKFNEYC ATSVLQYTKE WEEYVTRQAR WVDFENGYKT MDLSFMESVI WAFKELYDKG
     LIYQGFRVLP YSWAEHTPLS NQETRLDDSY KLRQDPTLTV TFPVTGVVEG SSANAGLVGA
     LALAWTTTPW TLPSNLALAV NPAVTYALVE VAEDGEAEFV GKRVLLAKDL VGSYAKELGA
     EAVIVSEHPG SELVGLTYEP IFGYFRDHAN GFQILGAEYV TTEDGTGIVH QAPAFGEDDM
     NTCNAAGIEP VIPVDIDGKF TGLVPEYQGQ LVFDANKDII KDLKAAGRVV RHQTIEHSYP
     HSWRSGEPLI YMALPSWFVN VTEIRDRMVE VNQDIEWMPA HIRDGQFGKW LEGARDWNIS
     RSRYWGSPIP AWVSDNDEYP RVDVYGSLDE LEADFGVRPK SLHRPDIDEL TRPNPDDPTG
     KSTMRRVTDV LDVWFDSGSM PFAQVHYPFE NKEWFDTHAP ADFIVEYIGQ TRGWFYLLHV
     LSTALFDRPA FKKVVAHGIV LGDDGLKMSK SKGNYPNVNE VFDRDGSDAM RWFLMSSPIL
     RGGNLIVTEK GIREGVRQAQ LPMWNAYSFL QLYTSKNATW SVDSTDVLDR YILAKLHDLV
     AETQAALDGT DIAKACDLVR NFCDALTNWY VRRSRDRFWA GDEAHPEAFN TLYTVLETLT
     RVAAPLLPMT TEVIWRGLTG ERSVHLTDFP SAESFPADAD LVRTMDEIRG VCSAASSVRK
     AHKLRNRLPL PGLTVALPDS ARLADFASII RDEVNVKNVD LTSDVDSVGT FEVVVNAKVA
     GPRLGKDVQR VIKAVKAGNY TREGDVVVAD GIELNEGEFT ERLVAANPDS TAQIDGVDGL
     VVLDMEVTEE LEAEGWAADA IRGLQDARKN SGFEVSDRIS VVVSVPEDKK EWITTHADHI
     AAEVLATSFE IVTDALDGET HDIVAGVTAK VTKN