SYI_ZYMMO
ID SYI_ZYMMO Reviewed; 941 AA.
AC Q5NQQ7; Q9RNJ5;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=ZMO0323;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RA Lee H.J., Kang H.S.;
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
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; AF180145; AAD56932.1; -; Genomic_DNA.
DR EMBL; AE008692; AAV88947.1; -; Genomic_DNA.
DR RefSeq; WP_011240252.1; NZ_CP035711.1.
DR AlphaFoldDB; Q5NQQ7; -.
DR SMR; Q5NQQ7; -.
DR STRING; 264203.ZMO0323; -.
DR EnsemblBacteria; AAV88947; AAV88947; ZMO0323.
DR GeneID; 58026180; -.
DR KEGG; zmo:ZMO0323; -.
DR eggNOG; COG0060; Bacteria.
DR HOGENOM; CLU_001493_7_1_5; -.
DR OMA; HLGTAWN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000001173; 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 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..941
FT /note="Isoleucine--tRNA ligase"
FT /id="PRO_0000098513"
FT MOTIF 69..79
FT /note="'HIGH' region"
FT MOTIF 630..634
FT /note="'KMSKS' region"
FT BINDING 589
FT /ligand="L-isoleucyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:178002"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 633
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 915
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 918
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 935
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT CONFLICT 92..94
FT /note="SQT -> TKP (in Ref. 1; AAD56932)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="E -> K (in Ref. 1; AAD56932)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="A -> S (in Ref. 1; AAD56932)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 941 AA; 106263 MW; 645DF7E9C0E82279 CRC64;
MSDQKSADAT QARDWRPTVF LPKTSFPMKA GLAKKEPEIL ARWQKEDLYQ QLREQRKGAE
RFILHDGPPY ANGDIHIGHA LNKILKDIIM RSQTLLGKDV PYIPGWDCHG LPIEWKVEEQ
FRKKKLNVDK DVNAVEFRQE CRKYAVHWVD TQRQEFKRLG VLGEWDNPYL TMNFEAEAII
AGELMRFSET GQIYRGAKPV LWSVVEKTAL AEAEVDYADV DSTTIDLAFK ITDSKIPELV
GGYAVIWTTT PWTIPANRAL AYGPDIDYVL VDLNGKHYLF AEALLEDSLK RIGHEGDAPV
LWRGKGAELD GSIAQHPMFE KGGFFAEPRP FLGGSHVTTE AGTGIVHMAP DYGEDDFLLC
KAHNIDPVFA VEDDGRYRKD WLWMGGEGLV ISPKINAADG PICSDLREVG ALLATSVLHH
SYPHSWRSKA KLIYRCTPQW FIALDRPVEK GAIAGKTLRE TALKAIDEVS WFPAKGKNRI
QTMVEGRPDW VISRQRAWGV PITLYVNRES GDYLRDPEVN ARILAAFRKE GADAWFKANH
QLFLGDKYRL EDYEPVNDIL DVWFDSGSTH AFVVEARYGE GTRAQLYLEG SDQHRGWFQS
SLLESCGSRG HAPYEAVLTH GFTLDGTGRK MSKSVGNVID PLKVINESGA DILRMWVAST
DYNEDVRISK EVLSGTSDGY RKLRNSFRYL LGALEGFSEE EKVDLADLPE LEKYILHLLA
ELDQALHESV NGFAFNRYLR LLSDFVNNDL SAFFFDIRKD RLYCDVGEAA PQGTEERRAY
RTVLDILFHA LVRYAAPILC FTAEEVWLHR FPDAGSVHLS VWPEVDGQWK NAVLGEKWAV
IREQRQIVTE KIEPLRREKI VGSSLEAEVT LPVDAATAKI LSSVDFSEIC ITAKINLVDA
SDAAITVDRT QNHKCGRCWQ HLPEVEEDGA LCDRCKSVVG E
