SYI_PARXL
ID SYI_PARXL Reviewed; 945 AA.
AC Q13UW2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=Bxeno_A3589;
GN ORFNames=Bxe_A0807;
OS Paraburkholderia xenovorans (strain LB400).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=266265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LB400;
RX PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT shaped for versatility.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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; CP000270; ABE32127.1; -; Genomic_DNA.
DR RefSeq; WP_011489631.1; NZ_CP008760.1.
DR AlphaFoldDB; Q13UW2; -.
DR SMR; Q13UW2; -.
DR STRING; 266265.Bxe_A0807; -.
DR EnsemblBacteria; ABE32127; ABE32127; Bxe_A0807.
DR KEGG; bxb:DR64_2972; -.
DR KEGG; bxe:Bxe_A0807; -.
DR PATRIC; fig|266265.5.peg.3779; -.
DR eggNOG; COG0060; Bacteria.
DR OMA; HLGTAWN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000001817; 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; Reference proteome; Zinc.
FT CHAIN 1..945
FT /note="Isoleucine--tRNA ligase"
FT /id="PRO_1000022051"
FT MOTIF 66..76
FT /note="'HIGH' region"
FT MOTIF 622..626
FT /note="'KMSKS' region"
FT BINDING 581
FT /ligand="L-isoleucyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:178002"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 625
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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"
FT BINDING 911
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 928
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 931
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
SQ SEQUENCE 945 AA; 106008 MW; 2E23E36949D06FFB CRC64;
MSNKKADSKP QSRYPVNLLD TPFPMRGDLP KREPQWVKEW QERKVYETIR AASKGRKKFI
LHDGPPYANG DIHLGHAVNK ILKDMIVKAR NLAGFDAVYV PGWDCHGMPI EIQIEKQFGK
SLPAAEVMQK ARAYATEQIE KQKVGFRRLG VLGDWDNPYK TMNFTNEAGE IRALAKIMEK
GYVFRGLKPV NWCFDCGSAL AEAEVEYKDK TDPTIDVLFS FAEPEKTAQA FGLNALPRNE
GGIVIWTTTP WTIPANQALN LHPEIVYALV DTSRGLLILA QERVEACLKQ YGLEGTIVAT
TPGAKLVNLR FNHPLASAHP SYKRTSPVYL GDYVTTESGT GVVHSSPAYG VEDFVSCKAH
GMSDSDIINP VMGDGRYIES LALFGGLSIW AANPQIVEAL QGAGTLMRTE NYTHSYMHCW
RHKTPIIYRA TSQWFAGMDV KPNDTDRTLR ETALEGIENT AFYPAWGKQR LFSMIANRPD
WTLSRQRQWG VPMAFFVHKE TGELHPRTLE LLEEVAQRVE KAGIEAWQSL DPRELLGDEA
NMYEKNRDTL DVWFDSGTTH WHVLRGSHKD ELQFPADLYL EGSDQHRGWF HSSLLTASML
DGRPPYNALL THGFTVDGEG RKMSKSLGNG IDPHEVANRL GAEIIRLWIA STDYSGELAI
SEEILKRVTE GYRRIRNTLR FLLANLSDFD FAQHARPVED WLEIDRYAVA LSANLQNDIL
SHYEKYEFHP VVAKLQTFCS EDLGGFYLDV LKDRLYTTAA DSVARRAAQT ALYHIAHGLL
RLMAPFLSFT AEEAWKIFEP NSETIFTETY HAFPAVPEAG ALLDKWTLLR AARSDVTKAL
EEARVANLIG SSLQAEVEIR ASGARYDALT SLGDDLKFVL ITSAASVVKV DSEAEEGVEV
IASKYLKCER CWHYRADVGA NAEHPTLCGR CFSNLFGNGE TRSAA
