SYI_METBU
ID SYI_METBU Reviewed; 1058 AA.
AC Q12ZD1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=Mbur_0185;
OS Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS ACE-M).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX NCBI_TaxID=259564;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA Cavicchioli R.;
RT "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT burtonii: the role of genome evolution in cold adaptation.";
RL ISME J. 3:1012-1035(2009).
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; CP000300; ABE51195.1; -; Genomic_DNA.
DR RefSeq; WP_011498357.1; NC_007955.1.
DR AlphaFoldDB; Q12ZD1; -.
DR SMR; Q12ZD1; -.
DR STRING; 259564.Mbur_0185; -.
DR PRIDE; Q12ZD1; -.
DR EnsemblBacteria; ABE51195; ABE51195; Mbur_0185.
DR GeneID; 3997152; -.
DR KEGG; mbu:Mbur_0185; -.
DR HOGENOM; CLU_001493_1_1_2; -.
DR OMA; HLGTAWN; -.
DR OrthoDB; 4914at2157; -.
DR Proteomes; UP000001979; 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; IPR001412; aa-tRNA-synth_I_CS.
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; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00392; ileS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 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..1058
FT /note="Isoleucine--tRNA ligase"
FT /id="PRO_1000022153"
FT MOTIF 48..58
FT /note="'HIGH' region"
FT MOTIF 596..600
FT /note="'KMSKS' region"
FT BINDING 599
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1058 AA; 120483 MW; 33EE2B998BACB728 CRC64;
MIKEVTDQYN AKEIETKVHE FWEANNAYRS VREHRKGAKK FYFVDGPPYT TGHIHLGTAW
NKIIKDSILR YMSMNDHDIL DRAGWDMHGL PIEVKVEGAL GFESKKDIET YGVGNFIEKC
KEFALRQKDD MTEQFQTLGV WLDWEDPYMT LKDEYIEAAW WTLKQAQDKN LLETGKRVVN
WCPRCETAIA DAEVEYEDRE DPSTYIKFKL KDEDNTFVVI WTTTPWTIPS NIAVAVHPEF
EYSKVKAISE NSATEILIIA SELVENVLRI GRYLDYEILS TMSGKDLEGT VYEHPLADLV
PLQAEIEHRI CNADYVTADS TGCVHIAPGH GVDDFEVGVK NEFPIFCPVG PNGSYTHEAG
KYCGMNILDA NRVVMDDLLE RGLLMAERMI SHRYGHCWRC KTAIIYLATE QWFLKIGELK
EDMLEEIKKV NWTPEWAGSA RFKDWIEGAR DWCISRQRYW GIPIPVWKCS SCNSLTVVGT
RKELIERSGA DPHIELHRPY VDKVTIPCEC GGTMKRVEDV FDVWFDSAVA SWATLRFPHQ
KEKFNEWWPA DFITEGHDQT RGWFYSQLGA SMVAFGKAPY KNVLMHGFTL DGSGKKMSKS
IGNVIQPAEV IDKFGADTLR SYVLSASAPW EDLKFNWDEL ATVHRTNNIL WNVYRFPLPY
MALDDFDPQK VSYESVEAYL RSEDKWILSR MQTVIAEVNK AMDARLLHKA MRSINEFVLE
DLSRWYIQLI RPRTWVEADN PDKLAVYRVL YDVFVTTAKL IAPFMPHLAE EMYQNLVRNI
DENAPVTIHL CDWPVVNEAL VDTSLEAQMK VARSIVEASS NARQKVGRKL RWPVSRIVVS
PTDENTIAAV EGLRSVLMDQ TNAKDIETTK VGESWNELGV ESTPNPGAIG PVFKGNAGNI
SAAIGAMDAY DLKKGLAGGE MEISLADGTN VTITEKMVNF SETVPEDVGS AEFNCGVVFV
DAKLTHEIES EGYSREVIRR IQDMRKELDL DVDDSIRGHI QISDERVLDL VLDFENYIAK
EVRANVLVIG LDVETTGELA KEWNVEGIPM TIAISKEE
