SYI_FERPD
ID SYI_FERPD Reviewed; 912 AA.
AC Q9XDB4; H9UEA1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 3.
DT 03-AUG-2022, entry version 125.
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=Ferpe_1791;
OS Fervidobacterium pennivorans (strain DSM 9078 / Ven5).
OC Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC Fervidobacterium.
OX NCBI_TaxID=771875;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 9078 / Ven5;
RX PubMed=10224005; DOI=10.1128/aem.65.5.2084-2091.1999;
RA Bertoldo C., Duffner F., Jorgensen P.L., Antranikian G.;
RT "Pullulanase type I from fervidobacterium pennavorans ven5: cloning,
RT sequencing, and expression of the gene and biochemical characterization of
RT the recombinant enzyme.";
RL Appl. Environ. Microbiol. 65:2084-2091(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9078 / Ven5;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Noll K.M., Woyke T.;
RT "Complete sequence of Fervidobacterium pennivorans DSM 9078.";
RL Submitted (MAR-2012) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD30388.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF096862; AAD30388.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP003260; AFG35844.1; -; Genomic_DNA.
DR RefSeq; WP_014452273.1; NC_017095.1.
DR AlphaFoldDB; Q9XDB4; -.
DR SMR; Q9XDB4; -.
DR STRING; 771875.Ferpe_1791; -.
DR EnsemblBacteria; AFG35844; AFG35844; Ferpe_1791.
DR KEGG; fpe:Ferpe_1791; -.
DR PATRIC; fig|771875.3.peg.1818; -.
DR eggNOG; COG0060; Bacteria.
DR HOGENOM; CLU_001493_7_0_0; -.
DR OMA; HLGTAWN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000007384; 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 InterPro; IPR010663; Znf_FPG/IleRS.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR Pfam; PF06827; zf-FPG_IleRS; 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; Zinc.
FT CHAIN 1..912
FT /note="Isoleucine--tRNA ligase"
FT /id="PRO_0000098387"
FT MOTIF 57..67
FT /note="'HIGH' region"
FT MOTIF 590..594
FT /note="'KMSKS' region"
FT BINDING 549
FT /ligand="L-isoleucyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:178002"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 593
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 880
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 883
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 900
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 903
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT CONFLICT 525
FT /note="I -> M (in Ref. 1; AAD30388)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 912 AA; 105259 MW; A0C8FA7C5CE20B7E CRC64;
MDYKATLNLP QTNFQMKANL VNKEPEMLKF WEEKEIYKKT LETRANAPTY LLHDGPPYAN
GDIHLGTAMN KILKDFVTRY KTMRGYRVPF VPGWDTHGLP IEHRVTTSLG EEAKKKSPAE
IRKLCKEFAL KYVDIQREEF KRLGVKGDWE HPYITLDPDY EYHILDVFKT LVENGNVYRG
NKPVYWCPTC RTALAEAEIE YHDHESPSIY VKFQMVDKPD TYIVIWTTTP WTIPANVAIA
LHPDYTYVKI KVDEEYWIVA EGLLQKFAAD VGIDFEVVEK FVGKELEGKL TKHPLYDRTS
VVVLADYVTL EDGTGCVHTA PGHGEEDYQT GLKYNLPVLS PVDDEGRFTK EAGKYEGLKI
WDANKVIVED LKNNGSLIKA GKISHSYPHC WRCKGPVMFR ATPQWFISVD KNNLRGKVLE
EIKKVKWYPA WGETRITAMV QERPDWTISR QRVWGVPIPA VKCKDCGEVT LEPKVIEHFA
NIVKEKGTDA WFELDVNELI PADFKCPACG SKNFEKTHDT LDVWIDSGCS WEAVIRSKGE
RFPVDLYLEG DDQHRGWFQS SIFLSTAKAG TAPFKAVVTH GFIKDEQGRK MSKSLGNVID
PMEIVNKYGA DILRLWVAST DFFDNIRVGK NIIEQQVEVY RKLRNTLRYL LSNLYDFTEA
DLLPYEKLLP LDKWALGRLQ KFIEQITQYY EGFEYSKVYN ATVKYCTTEL SAVYLDILKD
RLYVEAKDSI YRRSAQTALH YILEALIKIL APIIPFTAEE AYQESHLKRY ESVHLEYWPE
VRKEFIDEAL LEEFDHLLLI RDDVLKALEN ARASDIIGHS LDAHVIIEAK NEELKNLLRK
YESLLEEFFI VSKVTLSENI SGLNGQFANV LVQRAEGQKC QRCWKYHPDT GKDLEHPETC
PRCSAVLRGE RK
