ID   SYI_CLOAB               Reviewed;        1035 AA.
AC   Q97ES0;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   27-MAR-2024, entry version 116.
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=CA_C3038;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK80978.1; -; Genomic_DNA.
DR   PIR; G97273; G97273.
DR   RefSeq; NP_349638.1; NC_003030.1.
DR   RefSeq; WP_010966319.1; NC_003030.1.
DR   AlphaFoldDB; Q97ES0; -.
DR   SMR; Q97ES0; -.
DR   STRING; 272562.CA_C3038; -.
DR   GeneID; 44999525; -.
DR   KEGG; cac:CA_C3038; -.
DR   PATRIC; fig|272562.8.peg.3221; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_1_1_9; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000000814; 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   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; 2.
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..1035
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098533"
FT   MOTIF           48..58
FT                   /note="'HIGH' region"
FT   MOTIF           589..593
FT                   /note="'KMSKS' region"
FT   BINDING         592
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1035 AA;  119411 MW;  5FC26B022AFDAA86 CRC64;
     MYKKVDSSKS FVDIERDVLK LWHEKEIVKK SFNSNQDGEY FSFYDGPPTA NGRPHVGHII
     TRVMKDLIPR YKVMKGYKVP RKAGWDTHGL PVELEIEKKL GISGKPQIEE YGIEKFVKEC
     KESVFSYVSL WKDMSEKLGY WVDMENPYVT YHNDYIESVW WALKQMWDKD LLYKGHKIVP
     YCPRCGTALS SHEVAQGYKD VKEATAFVKF KVKGEENKYI LAWTTTPWTL PSNVALAINK
     AYDYVEVINN GEHLILAKAL LTVLEGEYEV VSEFKGEKLL GMEYEQLFKF ANPDKKAFYV
     VHGDFVTLSD GTGIVHIAPA YGEDDNMLGK KYDLPLINLV NGEGKFVDEV EPWKGLFVKK
     ADPKILEYMK ENGTLYKSEK FTHSYPHCWR CDTPLLYYPR DSWFVRMTSL RDKLVENNNK
     IHWYPDNIRT GRFGKFVENV IDWGISRDRY WGTPLPIWQC ECGHRDCVGS IEELKEKGIN
     VPENIELHKP YIDEVKLTCP KCGKPMTRTE EVIDCWFDSG SMPFAQLHYP FENKEVFENT
     FPAQFISEAV DQTRGWFYTL LAISTSIFDK SSFENCIVLG HVLDKHGLKM SKHKGNVVDP
     FDVLDNQGAD ACRWHFYTSS APWLPTRFSQ EDVAETQRKF LSTLWNVYSF YVLYAEIDKF
     NPNDYKDFVS GNVMDKWIVS RLNTLTKDVG NYLDSYGITQ AALEIQDFVD DLSNWYVRRN
     RSRYWTQELT DDKVGAYVTL YRVLVTLSKV AAPFIPFMTE QIYQSLVTSI NEGAEESVHL
     CKWPEYDESL IDSSLEEEMK LAISIVKLGR SARNGANIKN RQPLYEMRVS TKALPDYYGD
     IIRDELNVKK VEFGADLSKY VNFEIKPNLP VLGKSYGKLI PKIRKEISSM DQMKLAERVR
     SGEAVKIDVD GTEIELNSEN LLVTMQGLEG FAFAGIGEIG IVLETTITDE LREEGYLREV
     LSKVQNMRKE SGFEVADKIE IYVSGNEKLE NVIRKFEDTI KKETLATDII YSENKEAAIY
     NINGEELNVF VKKNC
//