ID SYI_SHEHH Reviewed; 940 AA. AC B0TJA9; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 08-APR-2008, sequence version 1. DT 27-MAR-2024, 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=Shal_1131; OS Shewanella halifaxensis (strain HAW-EB4). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=458817; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HAW-EB4; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C., RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Kim E., Zhao J.-S., Richardson P.; RT "Complete sequence of Shewanella halifaxensis HAW-EB4."; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. 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; Evidence={ECO:0000255|HAMAP- CC 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; CP000931; ABZ75700.1; -; Genomic_DNA. DR RefSeq; WP_012276244.1; NC_010334.1. DR AlphaFoldDB; B0TJA9; -. DR SMR; B0TJA9; -. DR STRING; 458817.Shal_1131; -. DR KEGG; shl:Shal_1131; -. DR eggNOG; COG0060; Bacteria. DR HOGENOM; CLU_001493_7_0_6; -. DR OrthoDB; 9810365at2; -. DR Proteomes; UP000001317; 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 CDD; cd00818; IleRS_core; 1. DR Gene3D; 1.10.730.20; -; 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_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 NCBIfam; TIGR00392; ileS; 1. DR PANTHER; PTHR42765:SF1; ISOLEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR42765; SOLEUCYL-TRNA SYNTHETASE; 1. 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; 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; Zinc. FT CHAIN 1..940 FT /note="Isoleucine--tRNA ligase" FT /id="PRO_1000088554" FT MOTIF 58..68 FT /note="'HIGH' region" FT MOTIF 605..609 FT /note="'KMSKS' region" FT BINDING 564 FT /ligand="L-isoleucyl-5'-AMP" FT /ligand_id="ChEBI:CHEBI:178002" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002" FT BINDING 608 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002" FT BINDING 903 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002" FT BINDING 906 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002" FT BINDING 923 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002" FT BINDING 926 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002" SQ SEQUENCE 940 AA; 105740 MW; 23069A4E8031C1A8 CRC64; MSDYKSTLNL PETEFPMRGN LANREPEMLK SWNENGLYQQ IRESRKDAKP FILHDGPPYA NGDIHIGHSV NKILKDIIIK SKTMSGFDAP YIPGWDCHGL PIELKVEQKV GKPGHKVTAA EFRQKCREYA AKQVDGQRED FIRLGVFADW QNPYLTMDFS TEANIVRSLS KVIENGHLHK GVKPVHWCTD CGSALAEAEV EYEDKMSPAI DVAFTAVDKS ALLAKFGLAD YAHNISMVIW TTTPWTLPAN RALAVAANVE YTLVEMVKDG QTQALVLATD LYESCIERFG AESHTVLGTV AGSDLELLRF NHPFYDFDVP VILGDHVTVD SGTGVVHTAP GHGQDDFVVG QKYGLEVANP VGDNGVYKPD TEIFAGLHVF KANKNVVELL EEKGALLSHV QIKHSYPHCW RHKTPIIFRA TPQWFISMDQ KGLRTQAISE IEQTKWIPDW GQSRIEKMVE NRPDWCISRQ RTWGVPITLF VHRETEELHP DSVSLMERVA ARIEQQGIQA WWDLDASELL GDEADQYRKV TDTLDVWYDS GSTFSTVVAA RPEFHGHDID LYLEGSDQHR GWFMSSLMIS TAMNGKAPYK QVLTHGFTVD GQGRKMSKSV GNVISPQHVT NKLGADILRL WVAATDYSGE MTVSDQILNR SADAYRRIRN TARFLLANIN GFDPVSDMVA IEDMVALDRW VVRRAAALQQ ELLEAYDEYN FHLVTQKLMQ FCSVELGSFY LDIIKDRQYT AKGDSNARRS CQSALYLISE AMVRWIAPIL SFTADEIWKL LPGERGEYVF TETWYEGLKS ITLESDLSDE YWDQLLAVRA EVNKVIENAR REKQIGGSLE AEVTLFADDA LSAVLEKLGD ELRFVLLTSK TEVVALAAAP SDAIGTELAS LKLSLKKSEA EKCERCWHHR EDVGTVTEHP TLCVRCVTNI EGDGEVRQFA //