ID   SYI_DEHMC               Reviewed;        1014 AA.
AC   Q3ZY20;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 109.
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=cbdbA1012;
OS   Dehalococcoides mccartyi (strain CBDB1).
OC   Bacteria; Chloroflexota; Dehalococcoidia; Dehalococcoidales;
OC   Dehalococcoidaceae; Dehalococcoides.
OX   NCBI_TaxID=255470;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBDB1;
RX   PubMed=16116419; DOI=10.1038/nbt1131;
RA   Kube M., Beck A., Zinder S.H., Kuhl H., Reinhardt R., Adrian L.;
RT   "Genome sequence of the chlorinated compound-respiring bacterium
RT   Dehalococcoides species strain CBDB1.";
RL   Nat. Biotechnol. 23:1269-1273(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; Evidence={ECO:0000255|HAMAP-
CC         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; AJ965256; CAI83123.1; -; Genomic_DNA.
DR   RefSeq; WP_011309474.1; NC_007356.1.
DR   AlphaFoldDB; Q3ZY20; -.
DR   SMR; Q3ZY20; -.
DR   KEGG; deh:cbdbA1012; -.
DR   HOGENOM; CLU_001493_1_1_0; -.
DR   Proteomes; UP000000433; 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   CDD; cd00818; IleRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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   NCBIfam; TIGR00392; ileS; 1.
DR   PANTHER; PTHR42780:SF1; ISOLEUCINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR42780; SOLEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF19302; DUF5915; 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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; Zinc.
FT   CHAIN           1..1014
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098541"
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;  116166 MW;  FAC5A5AA9D9830A7 CRC64;
     MFKAVNPRQN FPQMEEEILK IWQDKGIFKK SIENRRDGKR FTLYEGPPTA NGRPGIHHVL
     SRVFKDVIPR YKVMKGYYAP RIGGWDTHGL PVELEVEKEL GFTSKNDIEK YGIAEFNTRC
     RSSVFKYVSE WNKLTERIAY WVDLDNAYIT MDNKYIESGW WALKQMWDKG LVYQGHRVTP
     HCPRCGTSLS SHEVAQGYKD NTEDPSVFVK FEINHESLAQ TGLGQKWVNP SDKPLYLLAW
     TTTPWTLPAN TALAVSATDE YAILDMADYY MVLAKPRLSS LKLTENPIVG ECLGSDLKGL
     TYKPLFDPRE FGISVKNMQD NSEIDALEPL SYPVITTSYV SMDDGTGIVH TAPAYGELDY
     ESGVKYGLKF VHHVDLQGRI TGNYPFAGKF VKEADKDISR NLKERGLMFR NERMHHTYPF
     CWRCDSPLIY YAKQSWYIRT TAVRDELIKG NQQINWYPEH IKDGRFGDWL ENNIDWAFSR
     ERYWGTPVPI WRCEKCGQTE CVGGIDELKA KPNFKGMQEK LDIHRPYADE WTYDCAKCGG
     NMKRVTEVMD CWYDSGAMPV AQYHYPFEPE SRTIASDGRF PADYICEAVD QTRGWFYSLH
     AISTLIFGRP CYQNVICLGH ILDERGEKMS KSKNNVIQPA AVLDKYGADA VRWYFYTAAP
     PGNARRFSEK LVGEVTRQFL LMLWNIYSFF VTYANIDNFT PSEKYLAGEV PELDRWILSE
     LNQLVLDVDK GLDNYDPTQA GRRIEDFVGY LSNWYVRRSR RRFWKSENDA DKLSAYQALY
     TCLVTLSKLL APFTPFVAEE LYQNLVLLVD QSALESVHLT DFPVADKALI DEQLDNEIRL
     VMKVSSMGRS ARSKAALKVR QPLAEVRVVL SSPAERTGLM RLAEQVLEEL NVKALVAEEP
     GTAIPQENYV ASTEGAYTVA VYTGLSPELL AEGSAREIVH RLQTMRKSAE FEIADYINTH
     YQADEYLESV IRTHAEYIKK ETLSNQIVNG NAPEGAYTES LDIDGHPLSL WVVR
//