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 07-SEP-2016, entry version 93. 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; Enterobacteriales; 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., RA Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., RA Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., RA Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., RA 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., RA Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., RA Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., RA Schwartz D.C., Blattner F.R.; RT "Complete genome sequence and comparative genomics of Shigella RT flexneri serotype 2a strain 2457T."; RL Infect. Immun. 71:2775-2786(2003). CC -!- FUNCTION: Catalyzes the attachment of isoleucine to tRNA(Ile). As CC IleRS can inadvertently accommodate and process structurally CC similar amino acids such as valine, to avoid such errors it has CC two additional distinct tRNA(Ile)-dependent editing activities. CC One activity is designated as 'pretransfer' editing and involves CC the hydrolysis of activated Val-AMP. The other activity is CC designated 'posttransfer' editing and involves deacylation of CC mischarged Val-tRNA(Ile). {ECO:0000255|HAMAP-Rule:MF_02002}. CC -!- CATALYTIC ACTIVITY: ATP + L-isoleucine + tRNA(Ile) = AMP + CC diphosphate + L-isoleucyl-tRNA(Ile). {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- CC 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 CC aminoacylation and one for editing. The misactivated valine is CC translocated from the active site to the editing site, which CC sterically excludes the correctly activated isoleucine. The single CC editing site contains two valyl binding pockets, one specific for CC each substrate (Val-AMP or Val-tRNA(Ile)). {ECO:0000255|HAMAP- CC Rule:MF_02002}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. 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_LM651928.1. DR ProteinModelPortal; Q83MH2; -. DR STRING; 198214.SF0022; -. DR PaxDb; Q83MH2; -. DR PRIDE; Q83MH2; -. 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; 18700968; VBIShiFle31049_0026. DR eggNOG; ENOG4105C07; Bacteria. DR eggNOG; COG0060; LUCA. DR HOGENOM; HOG000246402; -. DR KO; K01870; -. DR OMA; PIPFFLH; -. 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-HAMAP. DR GO; GO:0004822; F:isoleucine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR CDD; cd07960; Anticodon_Ia_Ile_BEm; 1. DR Gene3D; 1.10.730.10; -; 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; KW Complete proteome; Cytoplasm; Ligase; Metal-binding; KW Nucleotide-binding; Protein biosynthesis; Zinc. FT CHAIN 1 938 Isoleucine--tRNA ligase. FT /FTId=PRO_0000098460. FT MOTIF 58 68 "HIGH" region. FT MOTIF 602 606 "KMSKS" region. FT METAL 901 901 Zinc. {ECO:0000255|HAMAP-Rule:MF_02002}. FT METAL 904 904 Zinc. {ECO:0000255|HAMAP-Rule:MF_02002}. FT METAL 921 921 Zinc. {ECO:0000255|HAMAP-Rule:MF_02002}. FT METAL 924 924 Zinc. {ECO:0000255|HAMAP-Rule:MF_02002}. FT BINDING 561 561 Aminoacyl-adenylate. {ECO:0000255|HAMAP- FT Rule:MF_02002}. FT BINDING 605 605 ATP. {ECO:0000255|HAMAP-Rule:MF_02002}. FT MOD_RES 183 183 N6-acetyllysine. {ECO:0000255|HAMAP- FT Rule:MF_02002}. FT CONFLICT 782 782 R -> C (in Ref. 2; AAP15570). FT {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 //