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;
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; 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
//
