ID   SYI_BIFLO               Reviewed;        1103 AA.
AC   Q8G3I2;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 113.
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=BL1777;
OS   Bifidobacterium longum (strain NCC 2705).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=206672;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCC 2705;
RX   PubMed=12381787; DOI=10.1073/pnas.212527599;
RA   Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA   Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT   "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT   the human gastrointestinal tract.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
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; Evidence={ECO:0000255|HAMAP-
CC         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; AE014295; AAN25560.1; -; Genomic_DNA.
DR   RefSeq; NP_696924.1; NC_004307.2.
DR   RefSeq; WP_011068832.1; NC_004307.2.
DR   AlphaFoldDB; Q8G3I2; -.
DR   SMR; Q8G3I2; -.
DR   STRING; 206672.BL1777; -.
DR   EnsemblBacteria; AAN25560; AAN25560; BL1777.
DR   KEGG; blo:BL1777; -.
DR   PATRIC; fig|206672.9.peg.1832; -.
DR   HOGENOM; CLU_001493_1_1_11; -.
DR   OrthoDB; 9810365at2; -.
DR   PhylomeDB; Q8G3I2; -.
DR   Proteomes; UP000000439; 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   CDD; cd00818; IleRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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   NCBIfam; TIGR00392; ileS; 1.
DR   PANTHER; PTHR42780:SF1; ISOLEUCINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR42780; SOLEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF19302; DUF5915; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   PRINTS; PR00984; TRNASYNTHILE.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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..1103
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098524"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           65..75
FT                   /note="'HIGH' region"
FT   MOTIF           649..653
FT                   /note="'KMSKS' region"
FT   BINDING         652
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1103 AA;  124066 MW;  B09FBEA401C18C28 CRC64;
     MSENVYPKAN EGGETAHVAP NPSFPDMEET VLDYWDKDDT FQKSVERNPS GDHSQNEFVF
     FDGPPFANGL PHYGHLLTGY AKDVIPRYQT MKGRKVNRVF GWDTHGLPAE LEAQKELGID
     SVDQIEKMGI DKFNDACRAS VLKYTNEWQN YVHRQARWVD FEHGYKTLNI PYMESVMWAF
     KQLYDKGLAY QGYRVLPYCP KDRTPLSAHE LRMDADVYQD RQDTTVSVAV KMRDEDDAYA
     VFWTTTPWTV PTNFAIVVGG DIDYVEVRPT EGKFAGKKFY LGKDLLPHYE KELGENYEVV
     RELKGSELEG RRYYPVFPYF AGDEAESEGH VPGPNGYTIF TADYVDTVEG TGLVHQAPYG
     EDDMNTLNAK GIKSTDVLDD GCRFTAQCPD YEGDFVFDAN LPILRNLRAG DGPLAEIPEE
     RRAILFQEKS YVHSYPHCWR CATPLIYKPV SSWFVSVTKI KPRLLELNQQ INWIPGNVKD
     GQFGKWLANA RDWSISRNRF WGSPIPVWVS DDPKYPRVDV YGSLEELKAD FGDYPRDKDG
     NINMHRPWID NLVRVNPDDP TGKSHMHRIS DVLDCWFESG SMSFAQFHYP FENKEKFEQH
     FPADYIVEYI GQTRGWFYLL HVMATALFDR PAFKNVICHG IVLGSDGQKM SKHLRNYPDV
     NGVFDKYGSD AMRWFLMSSP ILRGGNLIVT ADGIRDTVRQ VMLPVWSSYY FFTLYANAAN
     GGAGFDARQL RADEVAGLPE MDRYLLARTR RLVLAAEKSL NEFAISDACD AVSDFIDVLT
     NWYIRNTRDR FWNEDASAFN TLYTVLEAFM RVLAPLAPME AESVWRGLTG GESVHLAEWP
     FVVDEKTGAD TELGRVLVDD PALVDAMEKV REVVSGTLSL RKAAKIRVRQ PLSKLTVVAG
     NVEAVKAYDD LLKAELNIKN IEFSTLQDAA AHGLKIVHEL RVNARAAGPR LGKQVQFAIK
     ASKSGDWHVD AASGAPVVST PSGDLALVEG EYELINRVEE ENATEAAASV SAALPTGGFV
     ILDTALDADL LAEGYARDVI RSVQDARKAA DLDIADRISL VLTVPAVDVA KVEQFRDLIA
     HETLATSFEV KEGAELGVEV VKA
//