SYI_MESFL
ID SYI_MESFL Reviewed; 908 AA.
AC Q6F175;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Isoleucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02002};
DE EC=6.1.1.5 {ECO:0000255|HAMAP-Rule:MF_02002};
DE AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02002};
DE Short=IleRS {ECO:0000255|HAMAP-Rule:MF_02002};
GN Name=ileS {ECO:0000255|HAMAP-Rule:MF_02002}; OrderedLocusNames=Mfl389;
OS Mesoplasma florum (strain ATCC 33453 / NBRC 100688 / NCTC 11704 / L1)
OS (Acholeplasma florum).
OC Bacteria; Tenericutes; Mollicutes; Entomoplasmatales; Entomoplasmataceae;
OC Mesoplasma.
OX NCBI_TaxID=265311;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33453 / NBRC 100688 / NCTC 11704 / L1;
RA Birren B.W., Stange-Thomann N., Hafez N., DeCaprio D., Fisher S.,
RA Butler J., Elkins T., Kodira C.D., Major J., Wang S., Nicol R., Nusbaum C.;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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_02002}.
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_02002};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02002};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_02002};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02002}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02002}.
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_02002}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC IleS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02002}.
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DR EMBL; AE017263; AAT75748.1; -; Genomic_DNA.
DR RefSeq; WP_011183288.1; NC_006055.1.
DR RefSeq; YP_053632.1; NC_006055.1.
DR AlphaFoldDB; Q6F175; -.
DR SMR; Q6F175; -.
DR STRING; 265311.Mfl389; -.
DR PRIDE; Q6F175; -.
DR EnsemblBacteria; AAT75748; AAT75748; Mfl389.
DR GeneID; 2898000; -.
DR KEGG; mfl:Mfl389; -.
DR PATRIC; fig|265311.5.peg.389; -.
DR eggNOG; COG0060; Bacteria.
DR HOGENOM; CLU_001493_7_1_14; -.
DR OMA; HLGTAWN; -.
DR Proteomes; UP000006647; 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; cd07960; Anticodon_Ia_Ile_BEm; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR HAMAP; MF_02002; Ile_tRNA_synth_type1; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033708; Anticodon_Ile_BEm.
DR InterPro; IPR002301; Ile-tRNA-ligase.
DR InterPro; IPR023585; Ile-tRNA-ligase_type1.
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 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..908
FT /note="Isoleucine--tRNA ligase"
FT /id="PRO_0000098414"
FT MOTIF 59..69
FT /note="'HIGH' region"
FT MOTIF 595..599
FT /note="'KMSKS' region"
FT BINDING 554
FT /ligand="L-isoleucyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:178002"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 598
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 882
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 885
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 898
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 901
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
SQ SEQUENCE 908 AA; 104380 MW; 8DC53125D359C17A CRC64;
MKNIYKDTLL IGQTDFDMRA GLKDKEPVIQ EMWDAKKIYD QKQKLNEGKP LFMLHDGPPY
ANGDLHIGHA LNKTLKDMII RWKNANGYLA PFIMGWDTHG LPIETAVTKM GIDRKQTPAV
EFRDMCKDYA LKQVANQANQ FKRLGIFSNS DVKYVTLTHD FEVSELRLFQ KMYEKEMVYK
ALKPIYWSPS SESALAESEI EYKDVKSPTI FVAMKVVEGN AKIDTDTEIV IWTTTPWTIP
SNQMAAVGEN IEYNIVKAND RKFILASSLV NKVAEQIGWE TFEILDTLKG PEIVGVKYAH
PLYEQKINPV VIGHHVTDEA GTGIVHTAGG FGEDDYIIVK QHGIEPFAPI DDQGKFTNEI
AEFDEKLVGV FYEDANKIVG MDLEAKQRLL KLKFVSHSYP HDWRTKKPVI YRCTSQWFIG
LDKAKNQILA NVDQITTKPE WAKKRLYQVL EDRTDWTISR QRLWGVPIVA FYDQNDKLVL
NNEILAFAID KIAELGTNAW FDKPADTFLP EAYRNKNLKK EKDILDVWFD SGSSAIALSE
RFKNLPLPYD LYLEGNDQYR GWFNASMINS TIYSGKSPYK KLISHGMTVD EKGNKMSKSL
GNGIDPIEFA NTQGADILRL WVASTDYTDD QKIGPEIIKQ IGESYRKIRN TMRFILANLF
DFDPSKDYQT NLTEVDRYAL NNLSVVKNKA SEAYDNLSYN QVYNLVVNYV TKDLSSFYLD
FIKDILYIEK NDSIRRRQVQ TVLYEQLWML IDLLRPILIH TIEEVYQAMV NLNKTDSVHL
LDNKKQDFIE SNEFVTKWNN IMVLRDDVNK ALEIAREQKI INKGFEATVK VCLKDEFKNI
ESTTELEKIF IVNSLSFTND CSGLSEQKIA FVGVELKNGT KCERCWGIFD TLINNEICER
CNSVVESL
