ID   SYI_CLOK5               Reviewed;        1034 AA.
AC   A5N3P1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 100.
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=CKL_3752;
OS   Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=431943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680;
RX   PubMed=18218779; DOI=10.1073/pnas.0711093105;
RA   Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H.,
RA   Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F.,
RA   Hagemeier C., Thauer R.K., Gottschalk G.;
RT   "The genome of Clostridium kluyveri, a strict anaerobe with unique
RT   metabolic features.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008).
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; CP000673; EDK35737.1; -; Genomic_DNA.
DR   RefSeq; WP_012104071.1; NC_009706.1.
DR   AlphaFoldDB; A5N3P1; -.
DR   SMR; A5N3P1; -.
DR   STRING; 431943.CKL_3752; -.
DR   KEGG; ckl:CKL_3752; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_1_1_9; -.
DR   Proteomes; UP000002411; 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..1034
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_1000088561"
FT   MOTIF           48..58
FT                   /note="'HIGH' region"
FT   MOTIF           588..592
FT                   /note="'KMSKS' region"
FT   BINDING         591
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1034 AA;  120017 MW;  2A93120AF7430F78 CRC64;
     MYKKIDNNKS FVQMEKDILK LWQDRKVVEK SFNSNKDGEY FTFYDGPPTA NGKPHIGHVL
     TRVIKDLIPR YKVMKGYKVL RKAGWDTHGL PVELEVEKSL GISGKPQIEK YGVEDFIKKC
     KDSVFTYVSQ WRKMSDRIGF WVDMDDPYVT YDNHYIESEW WALKQIWDKN LLYKGHKIVP
     YCPRCGTALS SHEVSQGYKD VKETSVYVKF KIKNEDKYIL AWTTTPWTLP NNMALTINKS
     YDYVEVINDG EHLILAEGLL EKLEGEYEVV KKFKGEEMLG IEYEPMFNFT PFEGKAHYVV
     HGDYVTLTDG TGIVHTAPAF GEDDSITCIK HNIPMINSVT TQGKFKDEVT PWKGLFVKDA
     DPKIIAYLKE KDILYKAEKF THSYPFCWRC DTTLLYYPRD TWFIRMSAMR DKLIRNTNDT
     NWYPDNIRTG RFGKFVEGVI DWGLSRERYW GTPLPIWECE CGHRECIGSI KELREKGINV
     PDDIELHKPY IDGVKLKCDK CHKEMERVPE VIDCWFDSGS MPFAQHHYPF ENRELFEKNF
     PAQFISEAVD QTRGWFYTLM AISTVLFDKS SFENCLVLGH VLDKHGLKMS KHKGNVLSPE
     VVLENEGADA TRWYFYTESA PWLPSRFYEE AVQDSQRKFL GTLWNVYSFY VLYADLDKFN
     PLEYSHFVSE NVMDKWVISR LNSLIKITEG NLDNYRITQA AESIGNFVDE LSNWYVRRNR
     TRFWNEELAE DKVGAYVTLY NVLNKLCLIA APFVPFMTEE IYQNLVLSLN KNVPESIHLC
     KWPEYDLNLV DSDLEKNMEE CYKIVKLGRS ARNAANIKNR QPLSEMLISV KTLPGYYGDI
     IKSELNIKNI VFNADLSKYV NFNIKPNLPV LGKKYGRMIP KIKQSISSMN QMDLAGKINN
     NEVVKIKIDE TEIELNSENL LITMEGLEGF AFAGEGSTGI VLETTITEEL KEEGNLREIL
     SKIQNMRKES GFEVADKIKL YVSDNEKLEE VVKKFEAQIK KETLAVEVAY NENREYSGCN
     INGEKFNIAV EVLK
//