ID SYI_SHIFL Reviewed; 938 AA. AC Q83MH2; Q7UDT9; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 25-MAY-2022, entry version 126. DE RecName: Full=Isoleucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02002}; DE EC=6.1.1.5 {ECO:0000255|HAMAP-Rule:MF_02002}; DE AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02002}; DE Short=IleRS {ECO:0000255|HAMAP-Rule:MF_02002}; GN Name=ileS {ECO:0000255|HAMAP-Rule:MF_02002}; GN OrderedLocusNames=SF0022, S0025; OS Shigella flexneri. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=623; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=301 / Serotype 2a; RX PubMed=12384590; DOI=10.1093/nar/gkf566; RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.; RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity RT through comparison with genomes of Escherichia coli K12 and O157."; RL Nucleic Acids Res. 30:4432-4441(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700930 / 2457T / Serotype 2a; RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003; RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.; RT "Complete genome sequence and comparative genomics of Shigella flexneri RT serotype 2a strain 2457T."; RL Infect. Immun. 71:2775-2786(2003). 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_02002}. 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_02002}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_02002}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_02002}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02002}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02002}. 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_02002}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC IleS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02002}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE005674; AAN41688.1; -; Genomic_DNA. DR EMBL; AE014073; AAP15570.1; -; Genomic_DNA. DR RefSeq; NP_705981.1; NC_004337.2. DR RefSeq; WP_001286898.1; NZ_WPGW01000005.1. DR AlphaFoldDB; Q83MH2; -. DR SMR; Q83MH2; -. DR STRING; 198214.SF0022; -. DR EnsemblBacteria; AAN41688; AAN41688; SF0022. DR EnsemblBacteria; AAP15570; AAP15570; S0025. DR GeneID; 1024586; -. DR KEGG; sfl:SF0022; -. DR KEGG; sft:NCTC1_00023; -. DR KEGG; sfx:S0025; -. DR PATRIC; fig|198214.7.peg.25; -. DR HOGENOM; CLU_001493_7_1_6; -. DR OrthoDB; 32262at2; -. DR Proteomes; UP000001006; Chromosome. DR Proteomes; UP000002673; 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; cd07960; Anticodon_Ia_Ile_BEm; 1. DR Gene3D; 3.40.50.620; -; 2. DR Gene3D; 3.90.740.10; -; 1. DR HAMAP; MF_02002; Ile_tRNA_synth_type1; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR002300; aa-tRNA-synth_Ia. DR InterPro; IPR033708; Anticodon_Ile_BEm. DR InterPro; IPR002301; Ile-tRNA-ligase. DR InterPro; IPR023585; Ile-tRNA-ligase_type1. 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 InterPro; IPR010663; Znf_FPG/IleRS. DR Pfam; PF08264; Anticodon_1; 1. DR Pfam; PF00133; tRNA-synt_1; 1. DR Pfam; PF06827; zf-FPG_IleRS; 1. DR PRINTS; PR00984; TRNASYNTHILE. DR SUPFAM; SSF47323; SSF47323; 1. DR SUPFAM; SSF50677; SSF50677; 1. DR TIGRFAMs; TIGR00392; ileS; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; KW Metal-binding; Nucleotide-binding; Protein biosynthesis; KW Reference proteome; Zinc. FT CHAIN 1..938 FT /note="Isoleucine--tRNA ligase" FT /id="PRO_0000098460" FT MOTIF 58..68 FT /note="'HIGH' region" FT MOTIF 602..606 FT /note="'KMSKS' region" FT METAL 901 FT /note="Zinc" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002" FT METAL 904 FT /note="Zinc" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002" FT METAL 921 FT /note="Zinc" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002" FT METAL 924 FT /note="Zinc" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002" FT BINDING 561 FT /note="Isoleucyl-adenylate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002" FT BINDING 605 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002" FT MOD_RES 183 FT /note="N6-acetyllysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002" FT CONFLICT 782 FT /note="R -> C (in Ref. 2; AAP15570)" FT /evidence="ECO:0000305" SQ SEQUENCE 938 AA; 104267 MW; AE849F07887B771D CRC64; MSDYKSTLNL PETGFPMRGD LAKREPGMLA RWTDDDLYGI IRAAKKGKKT FILHDGPPYA NGSIHIGHSV NKILKDIIVK SKGLSGYDSP YVPGWDCHGL PIELKVEQEY GKPGEKFTAA EFRAKCREYA ATQVDGQRKD FIRLGVLGDW SHPYLTMDFK TEANIIRALG KIIGNGHLHK GAKPVHWCVD CRSALAEAEV EYYDKTSPSI DVAFQAVDQD ALKAKFGVSN VNGPISLVIW TTTPWTLPAN RAISIAPDFD YALVQIDGQA VILAKDLVES VMQRIGVTDY TILGTVKGAE LELLRFTHPF MGFDVPAILG DHVTLDAGTG AVHTAPGHGP DDYVIGQKYG LETANPVGPD GTYLPGTYPT LDGVNVFKAN DIVVALLQEK GALLHVEKMQ HSYPCCWRHK TPIIFRATPQ WFVSMDQKGL RAQSLKEIKG VQWLPDWGQA RIESMVANRP DWCISRQRTW GVPMSLFVHK DTEELHPRTL ELMEEVAKRV EVDGIQAWWD LDAKEILGDE ADQYVKVPDT LDVWFDSGST HSSVVDVRPE FAGHAADMYL EGSDQHRGWF MSSLMISTAM KGKAPYRQVL THGFTVDGQG RKMSKSIGNT VSPQDVMNKL GADILRLWVA STDYTGEMAV SDEILKRAAD SYRRIRNTAR FLLANLNGFD PAKDMVKPEE MVVLDRWAVG CAKAAQEDIL KAYEAYDFHE VVQRLMRFCS VEMGSFYLDI IKDRQYTAKA DSVARRSCQT ALYHIAEALV RWMAPILSFT ADEVWGYLPG EREKYVFTGE WYEGLFGLAD SEAMNDAFWD ELLKVRGEVN KVIEQARADK KVGGSLEAAV TLYAEPELAA KLTALGDELR FVLLTSGATV ADYNDAPADA QQSEVLKGLK VALSKAEGEK CPRCWHYTQD VGKVAEHAEI CGRCVSNVAG DGEKRKFA //