ID   SYI_RHILO               Reviewed;         993 AA.
AC   Q983N4;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 2.
DT   03-AUG-2022, entry version 122.
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}; OrderedLocusNames=mlr8250;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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   -!- 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   -!- SEQUENCE CAUTION:
CC       Sequence=BAB53846.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; BA000012; BAB53846.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q983N4; -.
DR   SMR; Q983N4; -.
DR   STRING; 266835.14027577; -.
DR   EnsemblBacteria; BAB53846; BAB53846; BAB53846.
DR   KEGG; mlo:mlr8250; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_7_1_5; -.
DR   Proteomes; UP000000552; 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: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   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 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   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..993
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098453"
FT   MOTIF           64..74
FT                   /note="'HIGH' region"
FT   MOTIF           662..666
FT                   /note="'KMSKS' region"
FT   BINDING         621
FT                   /ligand="L-isoleucyl-5'-AMP"
FT                   /ligand_id="ChEBI:CHEBI:178002"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT   BINDING         665
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
SQ   SEQUENCE   993 AA;  111343 MW;  F99288C8BF91E089 CRC64;
     MTDTVETIDY SKTLYLPQTD FPMRAGLPEK EPVLVKRWQD MDLYAKLRES AAGRTKYVLH
     DGPPYANGNI HIGHALNKIL KDVITRSFQM RGYDSTYVPG WDCHGLPIEW KIEEQYRAKG
     KNKDEVPVNE FRKECREFAA HWITVQGGEF QRLGVIGDFK NPYTTMAFHA ESRIAGELLK
     FALSGQLYRG SKPVMWSVVE RTALAEAEIE YQDYESDTIW AKFPVANLVV ANVVDGQPAE
     LNPDLSDRSL DLLDAHVVIW TTTPWTIPGN RAVSYSPRVA YGLYEVTAAE NAFGPEPGEK
     LIFADALAAE SQAKAKITLK RLHHVSAEQL GNLVLSHPFK GLGGGYEFPV PMVAGDHVTD
     DAGTGFVHTA PGHGREDFDA WMDAAPQLRA RGIDTVIPFT VDDAGFFTRD APGFGPDREG
     GAARVIDDNG KKGNANQAVI DELIKRNALF ARGRLKHSYP HSWRSKKPVI FRNTPQWFVY
     MDKDLGDGTT LRSRALKAID DTRFVPAAGQ NRIRAMIEER PDWVLSRQRA WGVPIAVFAD
     EDGNVLKDEA VNQRIMDAFE EEGADAWFAA GAKERFLGNH DASKWKQVMD ILDVWFDSGS
     THVFTLEDRP DLKWPADVYL EGSDQHRGWF HSSLLESCGT RGRAPYDTVV THGFTMDEDG
     RKMSKSLGNT VVPQDVIKQS GADILRLWVV TTDYWEDQRL GKNVLQTNID AYRKLRNTIR
     WMLGTLAHDD GETVPLEAMP ELERLMLHRL AELDEVVRQG YDAFEFKRIT RALVDFMVVE
     LSAFYFDIRK DALYCDAPSS VKRKASVQVV RHLFDCLVKW LAPMLPFTME EAWLDRHPDA
     VSVHLDQFPE IPADWKNEAL AEKWRKVRQV RRVVTGALEI ARAQKVIGSS LEAVPVVTIN
     DAALEAAIAD VDMAEMAITS DLVIAHGQAP EGAFTLDDVR GVAVVVEKAE DRGLVKCARS
     WRYTADVGQD PAFPDVSARD AAVLHELKAL GRL