ID   SYI_DEHM1               Reviewed;        1014 AA.
AC   Q3Z7P5;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=DET1038;
OS   Dehalococcoides mccartyi (strain ATCC BAA-2266 / KCTC 15142 / 195)
OS   (Dehalococcoides ethenogenes (strain 195)).
OC   Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales;
OC   Dehalococcoidaceae; Dehalococcoides.
OX   NCBI_TaxID=243164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2266 / KCTC 15142 / 195;
RX   PubMed=15637277; DOI=10.1126/science.1102226;
RA   Seshadri R., Adrian L., Fouts D.E., Eisen J.A., Phillippy A.M., Methe B.A.,
RA   Ward N.L., Nelson W.C., DeBoy R.T., Khouri H.M., Kolonay J.F., Dodson R.J.,
RA   Daugherty S.C., Brinkac L.M., Sullivan S.A., Madupu R., Nelson K.E.,
RA   Kang K.H., Impraim M., Tran K., Robinson J.M., Forberger H.A., Fraser C.M.,
RA   Zinder S.H., Heidelberg J.F.;
RT   "Genome sequence of the PCE-dechlorinating bacterium Dehalococcoides
RT   ethenogenes.";
RL   Science 307:105-108(2005).
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; CP000027; AAW39707.1; -; Genomic_DNA.
DR   RefSeq; WP_010936733.1; NC_002936.3.
DR   AlphaFoldDB; Q3Z7P5; -.
DR   SMR; Q3Z7P5; -.
DR   STRING; 243164.DET1038; -.
DR   PRIDE; Q3Z7P5; -.
DR   EnsemblBacteria; AAW39707; AAW39707; DET1038.
DR   KEGG; det:DET1038; -.
DR   PATRIC; fig|243164.10.peg.979; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_1_1_0; -.
DR   OMA; HLGTAWN; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000008289; 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   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; 2.
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.
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..1014
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098540"
FT   MOTIF           48..58
FT                   /note="'HIGH' region"
FT   MOTIF           628..632
FT                   /note="'KMSKS' region"
FT   BINDING         631
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1014 AA;  116015 MW;  DBA88E1091CC8AE2 CRC64;
     MFKAVNPRQN FPQMEEDILK LWQDKGVFKK SIENRRDGKR FTLYEGPPTA NGRPGIHHVL
     SRVFKDVIPR YKVMKGYYAP RIGGWDTHGL PVELEVEKEL GFTSKNDIEK YGIAEFNARC
     RSSVFKYVSE WNKLTERIAY WVDLDNAYIT MDNNYIESGW WALKQMWDKG LVYQGHRVTP
     HCPRCGTSLS SHEVAQGYKD NTEDPSVFVK FEIAKESLAK AGLAKKWAYP ADKPLYLLAW
     TTTPWTLPAN TALAVSAADQ YAILDMTDYY MILAKPRLSA LKLAENPVAG ECLGSDLSGL
     FYKPLFDPRE FGIPVRNMQD NSETGVSEEL LYPVITTSYV SMDDGTGIVH TAPAYGELDY
     ESGVKYGLKF VHHVDLQGRI TGSYPFAGKF VKEADKDISR NLKERGLMFR NERMHHTYPF
     CWRCDSPLIY YAKQSWYIRT TAVRDELIKG NQQINWYPEH IKDGRFGDWL ENNIDWAFSR
     ERYWGTPVPI WRCEKCGRTE CVGGIDELKA KPNFKGMQEK LDIHRPYVDE WTYDCDKCGG
     NMKRVTEVMD CWYDSGAMPV AQYHYPFEPE SRSIAKDGRF PADYICEAVD QTRGWFYSLH
     AISTLIFNRP CYQNVICLGH ILDERGEKMS KSRNNVIQPA TVLDKYGADA VRWYFYTAAP
     PGNARRFSEK LVGEVTRQFL LMLWNVYSFF VTYANIDSFT PSEKYLEGEV PELDRWILSE
     LNQLVLDVDK GLDNYDPTQA GRRIEDFVGY LSNWYVRRSR RRFWKSENDA DKLSAYQALY
     TCLVTLSRLL APFTPFVAEE LYQNLVLSAD PSALESVHLT DFPVADTALI DEQLDNEIRL
     VMKVSSMGRS ARSKAALKVR QPLAEVRVVL ASAGERTGLM RLAEQVLEEL NVKALAVEEP
     GTVIPEKNYA ASTEGAYTVA VYTGLSPELL AEGTAREIVH RLQTMRKSAG FEIADYINTH
     YQADEYLDSV IRMHSEYIKK ETLSNQLIKG NAPEGAYAES LDIDGHSLSL WVAR