ID   SYI_BORBU               Reviewed;        1042 AA.
AC   O51773;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 138.
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=BB_0833;
OS   Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS   (Borrelia burgdorferi).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA   Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA   Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA   van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA   Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA   Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA   Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL   Nature 390:580-586(1997).
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; AE000783; AAC67179.1; -; Genomic_DNA.
DR   PIR; H70203; H70203.
DR   RefSeq; NP_212967.1; NC_001318.1.
DR   RefSeq; WP_010889833.1; NC_001318.1.
DR   AlphaFoldDB; O51773; -.
DR   SMR; O51773; -.
DR   STRING; 224326.BB_0833; -.
DR   PRIDE; O51773; -.
DR   EnsemblBacteria; AAC67179; AAC67179; BB_0833.
DR   KEGG; bbu:BB_0833; -.
DR   PATRIC; fig|224326.49.peg.1225; -.
DR   HOGENOM; CLU_001493_1_1_12; -.
DR   OMA; HLGTAWN; -.
DR   Proteomes; UP000001807; 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; 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.
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..1042
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098525"
FT   MOTIF           48..58
FT                   /note="'HIGH' region"
FT   MOTIF           594..598
FT                   /note="'KMSKS' region"
FT   BINDING         597
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1042 AA;  122332 MW;  6C0F7D820CA32F75 CRC64;
     MFKKVENKAN FPKIEEKILK FWNDNKIFEK SIKQREGCEE FTFYDGPPFA TGLPHFGHFV
     PNTIKDIIPR YQTMQGKYVK RNFGWDTHGL PVEYEVEKKL GISGKYEIEN YGIENFNKEC
     RKIVLRYTEE WKNIILRLGR WVDFEKGYKT MDISFMESVW WVFKNLYEKG LIYESYYVLP
     YSPKLATPLS NFEVNLGEYK EVNDPSLTIK FKIKDKNEYL LVWTTTPWTL PSNLGIAVGQ
     EIEYSKIFDK TKEEILILGS KKLNSYYDDE NSYTIIEKFK GSKLEGIEYE PIFNYFLEQK
     DKGAFKVHTA DYVTTDDGTG IVHIAPFGEE DYRILKKHTN VDIIDPLDAE CKFTNQVKDF
     KGLFVKDADK KIIENLKLRN FLFKRENYLH RYPFCYRTNC PIIYRPISSW FVNVEKIKTK
     LLEVNEKINW MPAHLKKGRF GKWLENAKDW AISRNRFWGN PIPIWICSKT GKKICIGSKK
     ELENLSGQKI EDLHKDQIDK ITWPSKDGGK FIRTSEVLDC WFESGAMPYA SNHYPFTNEI
     NFKNIFPADF IAEGLDQTRG WFYTLTILGT ALFENTAFKN VIVNGLVLSS DGRKMSKSFK
     NYTDPMQVIN TFGADALRLY LIMSPVVKAD DLKYSDNGVR DVLKNIIIPI WNAYSFFTTY
     AIIDKFKPPK NLSLAKNNNL DKWIISELES LKKILNTEID KYNLTKSIES LLEFIDKLNN
     WYIRRSRRRF WKSENDKDKN DAYETLYYAI KTLMILLAPF IPFITEEIYQ NLKTDEDKQS
     IHLNDYPKAN ENFINKTIEE KINLARKITS MARSLRSLHN IKIRMPISTI YIVTKNQNEQ
     NMLMEMQEII LDEINAKEMK IKANEEELIT YKAKANFKEL GKKLGKDMKA VSTEISKLKN
     EDIIKIINGT SYEIKVANAK HYLSLNDIIL EREEKENLKV INEESITIGI DSLITKELYL
     EGLTREFVRQ IQNLRKEKNF DVSDRINLYI ENNETLKEML NKFEKYIKTE TLALNIILNK
     SKLEKKINLA DDIFTLIGIE KC