ID   SYI_TREDE               Reviewed;        1100 AA.
AC   Q73JB2;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Isoleucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02003};
DE            EC=6.1.1.5 {ECO:0000255|HAMAP-Rule:MF_02003};
DE   AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02003};
DE            Short=IleRS {ECO:0000255|HAMAP-Rule:MF_02003};
GN   Name=ileS {ECO:0000255|HAMAP-Rule:MF_02003}; OrderedLocusNames=TDE_2663;
OS   Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153
OS   / KCTC 15104).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=243275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104;
RX   PubMed=15064399; DOI=10.1073/pnas.0307639101;
RA   Seshadri R., Myers G.S.A., Tettelin H., Eisen J.A., Heidelberg J.F.,
RA   Dodson R.J., Davidsen T.M., DeBoy R.T., Fouts D.E., Haft D.H., Selengut J.,
RA   Ren Q., Brinkac L.M., Madupu R., Kolonay J.F., Durkin S.A., Daugherty S.C.,
RA   Shetty J., Shvartsbeyn A., Gebregeorgis E., Geer K., Tsegaye G.,
RA   Malek J.A., Ayodeji B., Shatsman S., McLeod M.P., Smajs D., Howell J.K.,
RA   Pal S., Amin A., Vashisth P., McNeill T.Z., Xiang Q., Sodergren E.,
RA   Baca E., Weinstock G.M., Norris S.J., Fraser C.M., Paulsen I.T.;
RT   "Comparison of the genome of the oral pathogen Treponema denticola with
RT   other spirochete genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:5646-5651(2004).
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_02003}.
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_02003};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02003};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02003}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02003}.
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_02003}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       IleS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02003}.
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DR   EMBL; AE017226; AAS13180.1; -; Genomic_DNA.
DR   RefSeq; NP_973261.1; NC_002967.9.
DR   RefSeq; WP_002680710.1; NC_002967.9.
DR   AlphaFoldDB; Q73JB2; -.
DR   SMR; Q73JB2; -.
DR   STRING; 243275.TDE_2663; -.
DR   PRIDE; Q73JB2; -.
DR   EnsemblBacteria; AAS13180; AAS13180; TDE_2663.
DR   GeneID; 2741108; -.
DR   KEGG; tde:TDE_2663; -.
DR   PATRIC; fig|243275.7.peg.2517; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_1_1_12; -.
DR   OMA; HLGTAWN; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000008212; 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; cd07961; Anticodon_Ia_Ile_ABEc; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   HAMAP; MF_02003; Ile_tRNA_synth_type2; 1.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR033709; Anticodon_Ile_ABEc.
DR   InterPro; IPR002301; Ile-tRNA-ligase.
DR   InterPro; IPR023586; Ile-tRNA-ligase_type2.
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   PANTHER; PTHR42780; PTHR42780; 1.
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.
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..1100
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098568"
FT   MOTIF           48..58
FT                   /note="'HIGH' region"
FT   MOTIF           626..630
FT                   /note="'KMSKS' region"
FT   BINDING         629
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1100 AA;  125760 MW;  90A17F4C6F320E8D CRC64;
     MYKPVDPKVD FAKQEEDVLK FWEKNDVFKK SVSSRDGRDN YIFFDGPPFA TGLPHFGHFV
     PGTIKDIIPR YKTMKGFRVE RRFGWDCHGL PVENLIEKEL GLNSKTDIEK YGIDKFNEAC
     RASVLRYVKE WKQTITRLGR WVDFENDYKT MEPAFMESIW WVMKSLWEKG LLYEGYYILP
     YCPRCSTVLS NHELNLGGYK DVHDPAITVR FKTLSPVKTS PAGKAFEGKN ALPSDTYLLA
     WTTTPWTLPS NLGLAVGADI DYALIEYDGA HYIMAVPRLE AYFAKSGKEE AKEYKLIWTK
     KGAELEGLRY EPLFPYFKNL AADENGKNAE AGQGAFRVLI GDFVTTEDGT GIVHTAPGFG
     EDDNRIFKDT GVPTVCPVDA ECKFTHEVSD YQGLFVKDAD KQIMERLKTE GKLFKKAQIL
     HSYPHCWRCS SPLIYRAVAS WFVSVTKIKD KLLNANSKIN WQPDHIKTGR FGKWLEGARD
     WAISRNRYWG NPIPIWKCPD CGETICVGSR EELKELSGVF PEDMHKHFVD KISIPCKKCG
     GTMKRVSEVL DCWFESGSMP YAQQHYPFEN KEHFEKNFPA DFISEGLDQT RGWFYTLTIL
     AAALFDEPAF KNCIVNGLVL AEDGKKMSKS LRNYTDPNEV IKQFGADALR LFLMNSNVVK
     ADDLKYSDEG VRDVLKGILI PFWNSYSFYI TYANIDGVKP PHNAKVDGKD EGVEEFLAKL
     NNPLDLWILS VTEKLVADVT EALDKYDLSQ AIPPMVEYID LLNNWYIRRS RRRFWKSEND
     GDKSQAYETL YRALKKFSLV AAPVVPFITE SIWQNLRTES DALSIHLADY PDYNEKIRNS
     ELEFKMKTVQ KAVSMGRALR YQFNLKIRQP LKAVEIVTLN PEEKRVLLEM EESIIEELNV
     KEVIFHEKED ELVEYSAKAN FKVLGKELGP LMKKAAAIIE QMNSSEIQNI MEGATLSIDI
     EGKSVEITAD KIVINRIEKA SLKIVNEGTL TVGLNTELTE ELLMEGYIRD LVRGIQTLRK
     ECGLDVTDRI KLYLSASQKN ADNKELEKAF ELFKDYVCDE TLTVQSSWLK TGELTKLGSI
     KTSLVEAGDY EWEIGIEKNN