ID   SYI_CHLTE               Reviewed;        1084 AA.
AC   Q8KFL5;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 110.
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}; OrderedLocusNames=CT0311;
OS   Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS   (Chlorobium tepidum).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX   NCBI_TaxID=194439;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX   PubMed=12093901; DOI=10.1073/pnas.132181499;
RA   Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA   DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA   Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.,
RA   Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V.,
RA   Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M.,
RA   White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA   Fraser C.M.;
RT   "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT   anaerobic, green-sulfur bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
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}.
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DR   EMBL; AE006470; AAM71557.1; -; Genomic_DNA.
DR   RefSeq; NP_661215.1; NC_002932.3.
DR   RefSeq; WP_010932003.1; NC_002932.3.
DR   AlphaFoldDB; Q8KFL5; -.
DR   SMR; Q8KFL5; -.
DR   STRING; 194439.CT0311; -.
DR   PRIDE; Q8KFL5; -.
DR   EnsemblBacteria; AAM71557; AAM71557; CT0311.
DR   KEGG; cte:CT0311; -.
DR   PATRIC; fig|194439.7.peg.301; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_1_1_10; -.
DR   OMA; HLGTAWN; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001007; 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; 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; 2.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00392; ileS; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc.
FT   CHAIN           1..1084
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098532"
FT   MOTIF           51..61
FT                   /note="'HIGH' region"
FT   MOTIF           624..628
FT                   /note="'KMSKS' region"
FT   BINDING         627
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1084 AA;  124097 MW;  5CAB0E7BBD050655 CRC64;
     MPATYPEYPS SLSYSAMEAQ IREFWIERNI FRKSLEKDAP KGIYSFYEGP PTVNGKPGVH
     HLFSRTIKDV VCRYHTMQGY QVPRKAGWDT HGLPVEISVE KKLGLKNKSH VEEYGVGEFN
     REARALVYHH IDDNREGWGK LTERMGYWVD MDSPYITCDN NYIESVWWAL KTIFDKGLIY
     KDYKIVPQDP KSETVLSSHE LALGYKEVQD PSVYIKFRLK DSGESILVWT TTPWTLISNV
     ALAVGRDIDY VRVKHRETGE VLILAESRLS VLVEKIGDES AWEVIDRCKG SDLEGRDYEP
     LFNYFSPERR AWYVVCGDFV STGEGTGIVH IAPAFGADDY ELSKQYQLPM LQPVARNGCF
     TAEVPDYEGM FFKDADKPIM QRLKEEGKLY RRETIQHTYP FSWRYDVPVI YYARESWYIR
     TTDIAPRMVA LNKTINWNPP EIGTGRFGNW LEENKDWALS RERFWGTPLP VWVAEDFAIG
     DGPDSGKLFA VGSVAELREG FIEIDGEEMN LGDALDKGLV ELDLHKPFVD RIWFIRDGKR
     FNRTPELIDV WFDSGSMPFA QLHYPFENKE LFDKTFPADF IAEGVDQTRG WFYTLHAIAT
     LIFDRPAYRN VVVNGHILDK SGQKMSKSKG NVVDPFESME QYGADAIRWY LMITSPPWRP
     KLFNAAEIEE EQRKFFRAFI NSYNFFVLYA NVDGFRYEEA DIPFTQRSEL DRWVLSSLNT
     LIAEVTSRME QYDLTGACRL IGDFTVDDLS NWYIRRSRKR FWKGEMGPDK LSAYQTLSTV
     LETLAKLMAP FVPFIAEKIW LDLKSVGGTS KAESVHLADW PVADESCIDA ALEERMKKAQ
     IITSLVRTMR EKAGIKVRQP LRRILLAAAE PGSRAAYELV SDIIKEEVNV QKIEYVEDED
     GSVISKKAKP NFKTLGPRFG KDMKLLAEEI RIMSHKQISR LEKEGSIEID LGGRICTVLR
     EDVDIVHEDI EGWLVAADDA HRIMVALDTE ITEELEMLGL ARELVSRIQT LRKESGLEIT
     DRIALTIAGS EKLLAAARKS ESYIMDETLA TSIVLLPLDD SQPGDGVEQV NNELCRLSLE
     KSGS