ID   SYI_MYCPN               Reviewed;         861 AA.
AC   P75258;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   04-NOV-2026, entry version 143.
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=MPN_520; ORFNames=MP322;
OS   Mycoplasmoides pneumoniae (strain ATCC 29342 / M129 / Subtype 1)
OS   (Mycoplasma pneumoniae).
OC   Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC   Mycoplasmoides.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129 / Subtype 1;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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=tRNA(Ile) + L-isoleucine + ATP = L-isoleucyl-tRNA(Ile) + AMP +
CC         diphosphate; Xref=Rhea:RHEA:11060, Rhea:RHEA-COMP:9666, Rhea:RHEA-
CC         COMP:9695, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58045,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78528, ChEBI:CHEBI:456215; EC=6.1.1.5;
CC         Evidence={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}.
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DR   EMBL; U00089; AAB95970.1; -; Genomic_DNA.
DR   PIR; S73648; S73648.
DR   RefSeq; WP_010874876.1; NC_000912.1.
DR   AlphaFoldDB; P75258; -.
DR   SMR; P75258; -.
DR   STRING; 272634.MPN_520; -.
DR   PaxDb; 272634-MPN_520; -.
DR   EnsemblBacteria; AAB95970; AAB95970; MPN_520.
DR   KEGG; mpn:MPN_520; -.
DR   PATRIC; fig|272634.6.peg.577; -.
DR   HOGENOM; CLU_001493_7_1_14; -.
DR   OMA; AACGHYL; -.
DR   OrthoDB; 9810365at2; -.
DR   BioCyc; MPNE272634:G1GJ3-853-MONOMER; -.
DR   Proteomes; UP000000808; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0002161; F:aminoacyl-tRNA deacylase 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   FunFam; 3.40.50.620:FF:000305; Isoleucine--tRNA ligase; 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; IPR050081; Ile-tRNA_ligase.
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   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   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;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..861
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098424"
FT   MOTIF           57..67
FT                   /note="'HIGH' region"
FT   MOTIF           590..594
FT                   /note="'KMSKS' region"
FT   BINDING         549
FT                   /ligand="L-isoleucyl-5'-AMP"
FT                   /ligand_id="ChEBI:CHEBI:178002"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT   BINDING         593
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
SQ   SEQUENCE   861 AA;  99527 MW;  6A521066C0EE235D CRC64;
     MNLKKTLLMP QTAFEMQGKL TTKEQQFQAF WQSKRIYQKL HRQNKDKPQK ILHDGPPYAN
     GNIHVGHALN KILKDFVLRS WNLQGFGTVF IPGWDCHGLP IEHAVSKKDP QHYASLSLSE
     KRDLCKQFAL SQIAIQKAQF QRLGLLNDFS KYYKTIDESF QQNELDLFLQ AVKKDLIFQA
     LKPTYWSPVS RTSLAEAEIE YKEVKTIGLY LTFTVVQSAV LNSGTKLLVW TTTPWTLPTN
     QAIAVHPQFE YLLFTYNNEQ YVVLASLFES LKTKFGWTDA IQVQTISGSQ LQNTTYKHCL
     YDKVNPVLLG NHVLCNEGTG LVHTSPAYGL DDFYLCKQNK LNEALVSLDE KGVFNDTLND
     PVLTGLFYLK ANDVIIERLK QHHNFVFSES FLHREPHDWR SKTPVIYRAS KQLFIKTKSI
     QSKLKRQIKR VKFVNNKNKE RLQEMLLQRA EWCISRQRVW GLPIPLIYAD NQPLLDVTTI
     KYTIQQLKKY GIDSWFEKDI NFFLNPKKIQ PGVEYKKETD TLEVWFDSGS TYNVLISNKL
     NFPADLYLEG SDQYRGWFNS SASCGIIQTD QLPFKSLISH GFTLDEHGNK MSKSLGNVVD
     PLKLCDQYGA DILRLWVTNV DWQVDNRIGD NIIKQIVEQY RRIRNSLLRF ILGNLNHFNF
     GEMKDYRFAL EDKIVIHKTN ALVQELHQWL KQYNFLNCLK AINKFVLWLS GWYFEIIKDT
     LYCDAKTNPN RVAKQAVLNY IFTQLIGFLN IFIPHTAEDA WQNYLLPKKP VSVNLFAGPA
     MFKVANVKGL DRLHESFSAI KDRAYAAIEQ ARQNGVITKN NQVVLTLGVD STSAIDPTSC
     KTFSSLAKRK PGKYNEWPQR N
//