SYI_DEHMC
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 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=cbdbA1012;
OS Dehalococcoides mccartyi (strain CBDB1).
OC Bacteria; Chloroflexi; 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;
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; AJ965256; CAI83123.1; -; Genomic_DNA.
DR RefSeq; WP_011309474.1; NC_007356.1.
DR AlphaFoldDB; Q3ZY20; -.
DR SMR; Q3ZY20; -.
DR PRIDE; Q3ZY20; -.
DR KEGG; deh:cbdbA1012; -.
DR HOGENOM; CLU_001493_1_1_0; -.
DR OMA; HLGTAWN; -.
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; 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
