ID   SYI_CUTAK               Reviewed;        1114 AA.
AC   Q6AB89;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 124.
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=PPA0216;
OS   Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS   acnes).
OC   Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC   Cutibacterium.
OX   NCBI_TaxID=267747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16379 / KPA171202;
RX   PubMed=15286373; DOI=10.1126/science.1100330;
RA   Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA   Strittmatter A., Hujer S., Duerre P., Gottschalk G.;
RT   "The complete genome sequence of Propionibacterium acnes, a commensal of
RT   human skin.";
RL   Science 305:671-673(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE017283; AAT81977.1; -; Genomic_DNA.
DR   RefSeq; WP_002536188.1; NZ_CP025935.1.
DR   AlphaFoldDB; Q6AB89; -.
DR   SMR; Q6AB89; -.
DR   STRING; 267747.PPA0216; -.
DR   EnsemblBacteria; AAT81977; AAT81977; PPA0216.
DR   KEGG; pac:PPA0216; -.
DR   PATRIC; fig|267747.3.peg.226; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_1_1_11; -.
DR   OMA; PSWYIRT; -.
DR   Proteomes; UP000000603; 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   Gene3D; 3.90.740.10; -; 1.
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; Zinc.
FT   CHAIN           1..1114
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098555"
FT   MOTIF           61..71
FT                   /note="'HIGH' region"
FT   MOTIF           640..644
FT                   /note="'KMSKS' region"
FT   BINDING         643
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1114 AA;  124981 MW;  22FBA25983231947 CRC64;
     MTDVNPVRSD NCRQYNNVPP QIDLPAMDHE IIDLWARQHT FDKSLEATKD GQPWTFFEGP
     PTANGQPGTH HVEARVFKDI FPRFKTMQGF RVDRKAGWDC HGLPVELAVE KELGFSGKPD
     IEKYGVEPFN AKCRESVTRH VDAFSELTER MGYWVNMDEA YWTMSPSYVE SVWWGLKRIW
     DKGLLGEDHR VAPYCPRCGT TLSDHELAQG YQDDRDPSIY VRFPVTSGPL AGRAKLLVWT
     TTPWTLVSNT AVAVHPEVRY VVAHRDPVPE GSDAVATASA EDPASQDLII AEPLFEKVLG
     EGWSLTGESF LGSQMELWTY ERPYNFLEWP KTERVTVDGR PTPADANFVV LADYVTVEDG
     TGLVHQAPAF GADDLQTCRR YGLPLVNPIR PDGTFEESVP LVGGQFFKTA DKPLCEDLDR
     RGVLFRLEMH WHSYPHCWRC DTHLIYYAQP SWYIRTTKVK EQLLAQNEVT TWYPETIKHG
     RFGDWLENNI DWAVSRSRYW GTPLPLWRND DDRSDVICVE SLAELSQYVG RDLTGMDPHR
     PFIDEVTFTR DGHTYHRVPE VADAWLDSGS MPFAQWGYPH VPGSKEKFES HYPGDFICEA
     IDQTRGWFYT MMAVGTLVFD ESSYRNVLCL GHILAEDGRK MSKHLGNILL PIPLMDSHGA
     DALRWFMAAD GSPWSARRVG DETIQETVRK VLLTYWNTVS FQVLYARANG WSPAQGTQHD
     ADPARGFGGV VPPAVGSRGF GGVVPPAVTE RHVLDRWLVS ATNVLVRDVT EALNNFDTQR
     VGNLIAQFVD ELSNWYVRRS RRRFWDGDEG ALWTLHETLE TLTKLMAPMV PFITERVWQD
     LFVTTNPHGP ESVHLASWPV ADDSLIDESL SESMDLARRI VELGRGARAE AKAKIRQPLS
     RALISGAALA KLDEDLQAEI RSELNVMALD SFTAAGDLVD HCAKGNFRAL GKKYAKATPK
     VAAAIAAADP EWLASELAIK GSVEMDVPEV EGGKAVVTAD DVIVSERPRE GWSVVNEQGE
     TVALDLEITP ELARAGQARE VIRFVQDSRK KAGLDVSDRI TLAWSASADL ATAIEEHAEQ
     ISQEVLAVQM SREPRADDWA VEPDLGLAVK VVKV