SYI_CUPTR
ID SYI_CUPTR Reviewed; 966 AA.
AC B3R6E8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=RALTA_A2521;
OS Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP
OS 107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=977880;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 / R1;
RX PubMed=18490699; DOI=10.1101/gr.076448.108;
RA Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V.,
RA Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C.,
RA Masson-Boivin C.;
RT "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT comparative genomics of rhizobia.";
RL Genome Res. 18:1472-1483(2008).
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; CU633749; CAQ70452.1; -; Genomic_DNA.
DR RefSeq; WP_012353750.1; NC_010528.1.
DR AlphaFoldDB; B3R6E8; -.
DR SMR; B3R6E8; -.
DR STRING; 977880.RALTA_A2521; -.
DR EnsemblBacteria; CAQ70452; CAQ70452; RALTA_A2521.
DR GeneID; 29761966; -.
DR KEGG; cti:RALTA_A2521; -.
DR eggNOG; COG0060; Bacteria.
DR HOGENOM; CLU_001493_7_1_4; -.
DR OMA; HLGTAWN; -.
DR OrthoDB; 32262at2; -.
DR BioCyc; CTAI977880:RALTA_RS12255-MON; -.
DR Proteomes; UP000001692; Chromosome 1.
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; Zinc.
FT CHAIN 1..966
FT /note="Isoleucine--tRNA ligase"
FT /id="PRO_1000189144"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 69..79
FT /note="'HIGH' region"
FT MOTIF 640..644
FT /note="'KMSKS' region"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 599
FT /ligand="L-isoleucyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:178002"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 643
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 929
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 932
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 949
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 952
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
SQ SEQUENCE 966 AA; 108366 MW; F81651D467BAC7F6 CRC64;
MSDDKRAKSD KNEKNKYPVN LLDTPFPMRG DLPKREPQWV KQWQDKQLYK KIRAARKGAK
KFVLHDGPPY ANGDIHIGHA VNKVLKDMII KARGLTGLDA VYVPGWDCHG MPIEIQIEKK
FGKGLPVQEV QAKARAYATE QIKRQMVDFE RLGVLGDWDH PYLTMNYRNE ADELRALGKI
MEKGYVFRGL KPVNWCFDCG SALAEAEVEY KDKVDLSIDV GFPFAEADKL AHAFKVPVEQ
IDARPGWIVI WTTTPWTIPS NQALNVHPEV EYALVDTPRG HLILATERVE EQLKVYALEG
KVIATATGAA LSEIRFHHPL AKMDGGYDRL SPIYLGDYVT TDTGSGIVHS APAYGVEDFQ
SCKAHGMPDS DIISPVMGNG VYAGTLPLFG GLSIWDANPR IVEALQESGN LFNSHKYTHS
YMHCWRHKTP IIYRATSQWF AGMDVDPAEE NGKPVPTLRE TALAGIDATE FYPAWGKQRL
HNMIANRPDW TLSRQRQWGV PMAFFVHKET GALHPRTPEL LEAIAKRVEQ QGIEAWQTLD
PAELLGDEAS QYEKNRDTLD VWFDSGTTHW TVIRGSHRDD LYDPSADEAD GRLADLYLEG
SDQHRGWFHS SLLTASMLYG KPPYKALLTH GFTVDGEGRK MSKSIGNTVS PQDIANKMGA
EIIRLWVAST DYSGELSISD EILKRVVESY RRIRNTLRFL LSNLSDYDHG KHALPAAEWL
EIDRYAVALT AQLQKEVLSH YEAYEFHPVV AKLQTFCSED LGGFYLDVLK DRLYTTAPDS
KARRAAQNAL YHITQAMLHW MAPFLSFTAE EAWQVFAHGT AHTDTIFTST YYAVPEVDDA
DDLLQKWHTL REVRAEVTRQ LEAVRVEGEI GSSLQAELTI QAGGPVLEAL QSLGDDLRFV
LLTSAAKVTA APEAGDLLVT VTPSAHAKCE RCWHYRADVG HNPDHPTLCG RCDSNLFGAG
EHRSHA
