ID   SYI_METTM               Reviewed;        1045 AA.
AC   P26499; D9PYN2;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 132.
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=MTBMA_c17620;
OS   Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS   14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS   thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=79929;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=2037598; DOI=10.1016/s0021-9258(18)99261-6;
RA   Jenal U., Rechsteiner T., Tan P.-Y., Buehlmann E., Meile L., Leisinger T.;
RT   "Isoleucyl-tRNA synthetase of Methanobacterium thermoautotrophicum Marburg.
RT   Cloning of the gene, nucleotide sequence, and localization of a base change
RT   conferring resistance to pseudomonic acid.";
RL   J. Biol. Chem. 266:10570-10577(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=20802048; DOI=10.1128/jb.00844-10;
RA   Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H.,
RA   Gottschalk G., Thauer R.K.;
RT   "Complete genome sequence of Methanothermobacter marburgensis, a
RT   methanoarchaeon model organism.";
RL   J. Bacteriol. 192:5850-5851(2010).
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;
CC         Evidence={ECO:0000255|HAMAP-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}.
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; M59245; AAA72950.1; -; Genomic_DNA.
DR   EMBL; CP001710; ADL59330.1; -; Genomic_DNA.
DR   RefSeq; WP_013296540.1; NC_014408.1.
DR   AlphaFoldDB; P26499; -.
DR   SMR; P26499; -.
DR   STRING; 79929.MTBMA_c17620; -.
DR   PRIDE; P26499; -.
DR   EnsemblBacteria; ADL59330; ADL59330; MTBMA_c17620.
DR   GeneID; 9705473; -.
DR   KEGG; mmg:MTBMA_c17620; -.
DR   PATRIC; fig|79929.8.peg.1699; -.
DR   HOGENOM; CLU_001493_1_1_2; -.
DR   OMA; HLGTAWN; -.
DR   OrthoDB; 4914at2157; -.
DR   Proteomes; UP000000345; 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   Gene3D; 3.40.50.620; -; 2.
DR   Gene3D; 3.90.740.10; -; 1.
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   PANTHER; PTHR42780; PTHR42780; 1.
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   1: Evidence at protein level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm;
KW   Direct protein sequencing; Ligase; Metal-binding; Nucleotide-binding;
KW   Protein biosynthesis; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..1045
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098579"
FT   MOTIF           49..59
FT                   /note="'HIGH' region"
FT   MOTIF           591..595
FT                   /note="'KMSKS' region"
FT   BINDING         594
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
FT   MUTAGEN         589
FT                   /note="G->D: Resistance to mupirocin (pseudomonic acid A)."
SQ   SEQUENCE   1045 AA;  121362 MW;  5A935B0FE300077E CRC64;
     MPIQEAEKSY KPHVIEEKVQ SFWEERDIYE RVKELREEGP RYSFLDGPPY CSGRIHLGTA
     WNKIMKDSYL RFKSMRGFNV RRQPGWDTHG LPIEHKVEGI LGVRSKKDIE DKIGIEEFVR
     KCREFAMENK AVMTSQFQRL GVWMDWDDPY VTFDPAYMES CWWTLKRAHE KDLLLRDLRV
     ITWCPRCETA LALAEIDYHE KEDPSIYVKF PVSGDTYILV WTTTPWTLPA NMAVAVHPDF
     DYAHTRLDGE TYIMAEALVE KVLGEEAEII KTVRGSELEG LTYRHPLDEE VPCHRDMEHR
     VILGDHVTLT EGTGCVHTAP GHGPEDFEIG KEYGLPVFCP VDEAGVFTED AGKYRGLFVK
     DADSDIIDDL RSKNLLLRAE TISHRYGFCW RCKTPIIYLA TEQWFLKITE IKDKMLSELD
     RVQWIPSWAG ESRFRNWIEN ARDWTISRQR YWGIPIPIWV CEDCDSIHVV GSIGELRELA
     VEGQLEGDFI HRPHVDRIIL ECGRCGGRMK RTPDVLDVWI DSGVAGWAAL HYPREKELFS
     EWFPYDFITE GHDQTRGWFY SQLGCGVIAL DETPYRRVLM HGFTLDEEGR KMSKSLGNVV
     EPEDVIEKYG ADVLRFYLLW ANKPWEDLKF VWDELKNVNK MFNILWNVYV FATTYMSLDR
     FQPGDHELED LHFRDEDRWI ISRVNSVALK VTEALDNLHF HRATREIHDF IVEDLSRWYI
     RLIRSRTWIE RDDPDKLAAY HSLYTALKTL IVTLSPIAPH VCEDIYQNLV RGAEPDSPES
     IHMLDWMVSE DAVDGKLEAE MDIVREIIEA CARARDTARY KLRWPVREIV VVSEDDKVLE
     AAESLKGVIA EQANAKSIRT STEFPDMRII AKPNPATLGP KLRQDMPPVM RKLEEADGAE
     VKAALESEGS FRVDLDGRII VLEPDDIIFE TELPENIVNA QFEGGSVFVD TELTPEIMSE
     AMARELVRRI QDMRKDLDLD VEARIEVSVK CSPEFRELTE PQREFVENEV RASHLSFDYT
     ELEYTKEWKI SDENLIISIK PSDKV