SYI1_OCEIH
ID SYI1_OCEIH Reviewed; 918 AA.
AC Q8ER41;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Isoleucine--tRNA ligase 1 {ECO:0000255|HAMAP-Rule:MF_02002};
DE EC=6.1.1.5 {ECO:0000255|HAMAP-Rule:MF_02002};
DE AltName: Full=Isoleucyl-tRNA synthetase 1 {ECO:0000255|HAMAP-Rule:MF_02002};
DE Short=IleRS 1 {ECO:0000255|HAMAP-Rule:MF_02002};
GN Name=ileS1 {ECO:0000255|HAMAP-Rule:MF_02002}; OrderedLocusNames=OB1484;
OS Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS 3954 / HTE831).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=221109;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX PubMed=12235376; DOI=10.1093/nar/gkf526;
RA Takami H., Takaki Y., Uchiyama I.;
RT "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT and its unexpected adaptive capabilities to extreme environments.";
RL Nucleic Acids Res. 30:3927-3935(2002).
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; BA000028; BAC13440.1; -; Genomic_DNA.
DR RefSeq; WP_011065885.1; NC_004193.1.
DR AlphaFoldDB; Q8ER41; -.
DR SMR; Q8ER41; -.
DR STRING; 221109.22777167; -.
DR PRIDE; Q8ER41; -.
DR EnsemblBacteria; BAC13440; BAC13440; BAC13440.
DR KEGG; oih:OB1484; -.
DR eggNOG; COG0060; Bacteria.
DR HOGENOM; CLU_001493_7_1_9; -.
DR OMA; HLGTAWN; -.
DR OrthoDB; 32262at2; -.
DR PhylomeDB; Q8ER41; -.
DR Proteomes; UP000000822; 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 Gene3D; 3.90.740.10; -; 1.
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; Reference proteome; Zinc.
FT CHAIN 1..918
FT /note="Isoleucine--tRNA ligase 1"
FT /id="PRO_0000098432"
FT MOTIF 57..67
FT /note="'HIGH' region"
FT MOTIF 594..598
FT /note="'KMSKS' region"
FT BINDING 553
FT /ligand="L-isoleucyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:178002"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 597
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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 888
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 905
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 908
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
SQ SEQUENCE 918 AA; 104887 MW; CDCAD9A3F063C7B7 CRC64;
MDYKQTLLMP KTAFPMRGNL PNKEPERQKK WEETNQYAKT LERTKGRPLF VLHDGPPYAN
GDIHIGHALN KVLKDFIVRY KSMTGYHAPY IPGWDTHGLP IETALTKKKK IKRKEMDIAA
FRKLCEEYAL GQINNQREQF KQLGVRGDWD NPYITLTKDY EASQIKVFGD MARKGYIYKG
LKPVYWSPSS ESALAEAEIE YQDKRSPSIY VAFEVKGGQA LLSGGEKFII WTTTPWTLPA
NLGISLHADL TYIVVQVGEE KYIIAEALFD DVSESLGWEN PQVLQSFKGK EAEGIEAQHP
FYDRTSLVML GEHVTTDAGT GCVHTAPGHG EDDFYVSRSY GIDAFCPVDE KGVFTQEAPG
FEGLFYDEAN KIITEKLDAS GALLKLEFIT HSYPHDWRTK KPTIFRATSQ WFASIKDFRV
DILEEIKQVN WYPHWGETRL YNMVRDREDW CISRQRAWGV PIPVFYGEDG TPIITDETIN
HVSELFREHG SNIWFEKEAK ELLPEGFTSE HSPNGNFAKE TDIMDVWFDS GSSHEGVLLN
RQNHQRPANV YLEGSDQYRG WFNSSLSTSV AVTGKAPYKA VISHGFVLDG NGRKMSKSLG
NVIVPSKVQK QLGSDILRLW VSSVDYQADV RISDDILKQT SESYRKIRNT FRFLLANLAD
FNPNTDRVKE ENMEEVDRYM VHRLQNVLAE AHKNYNQYEF APVFQQIHHF CSVDLSSFYL
DFAKDILYIE AKDHPRRRSI QTGYYEVLTS LVKLIAPIIP HTAEEVWEYI PEPEAESVHL
TDIPEARDVA INEQTVDKWN HFMKIRDDVL KALEEARSEK VIGKSLEAKI SIAAKDEGTK
KVLDEMEHLH QYFIVSEAVI VDTLTDAKEG NVVNVQVEVH PGETCDRCWV SSETVGENKN
HPSLCSRCAD VVTKHYAD
