ID   SYI_RHOPA               Reviewed;        1005 AA.
AC   Q6N1M8;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=RPA4377;
OS   Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=258594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-98 / CGA009;
RX   PubMed=14704707; DOI=10.1038/nbt923;
RA   Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA   Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA   Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA   Harrison F.H., Gibson J., Harwood C.S.;
RT   "Complete genome sequence of the metabolically versatile photosynthetic
RT   bacterium Rhodopseudomonas palustris.";
RL   Nat. Biotechnol. 22:55-61(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_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   -!- 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; BX572607; CAE29818.1; -; Genomic_DNA.
DR   RefSeq; WP_011159911.1; NC_005296.1.
DR   AlphaFoldDB; Q6N1M8; -.
DR   SMR; Q6N1M8; -.
DR   STRING; 258594.RPA4377; -.
DR   PRIDE; Q6N1M8; -.
DR   EnsemblBacteria; CAE29818; CAE29818; RPA4377.
DR   GeneID; 66895511; -.
DR   KEGG; rpa:RPA4377; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_7_1_5; -.
DR   OMA; HLGTAWN; -.
DR   PhylomeDB; Q6N1M8; -.
DR   BioCyc; RPAL258594:TX73_RS22325-MON; -.
DR   Proteomes; UP000001426; 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: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;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..1005
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098454"
FT   MOTIF           70..80
FT                   /note="'HIGH' region"
FT   MOTIF           670..674
FT                   /note="'KMSKS' region"
FT   BINDING         629
FT                   /ligand="L-isoleucyl-5'-AMP"
FT                   /ligand_id="ChEBI:CHEBI:178002"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT   BINDING         673
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
SQ   SEQUENCE   1005 AA;  111555 MW;  D69677F6600805C9 CRC64;
     MSDKPKTDAA QSGNDYSKTL FLPQTEFPMR AGLPQREPEL LKRWEEMDLY GKLRESARGR
     AKFVLHDGPP YANGNIHIGH ALNKILKDVV TKSQQMLGFD SNYVPGWDCH GLPIEWKIEE
     ENYRSKGKPK PNFKDSAAII AFRKECRAYA DKWLNVQREE FKRLGVIGDW DHPYATMNYA
     AEAQIARELM KFAANGTLYR GSKPVMWSVV EKTALAEAEV EYEDYTSDTV WVKFPVKTGD
     ASTKDASVVI WTTTPWTLPG NRAISFSSKI AYGLYKVTDA PADNWAKTGD LLILADGLAE
     SVFKQARVVA YEKVSDVGAD VLKASECAHP LQGLAGGYEF TVPLLDGDHV TDDTGTGFVH
     TAPGHGREDF DIWMHNARAL EARGISSVIP YTVDENGALT EQAPGFTGKR VINDKGEKGD
     ANEAVIQALI ARGALLARGK LKHQYPHSWR SKKPVIFRNT PQWFIAMDKD IVDDGVAKPG
     DTLRARALQA ISVTQWVPPA GQNRINGMIS GRPDWVISRQ RAWGVPIAVF IKDKGDGSVE
     ILQDEIVNQR IAEAFMQEGA DAWYAEGAAE RFLGDRAAEG WRKVDDILDV WFDSGSTHAF
     VLEDAQNFPG LAGIRRKVDG GADTVMYLEG SDQHRGWFHS SLLESCGTRG RAPYDVVLTH
     GFTLDEQGRK MSKSLGNTTD PAKVIASSGA DILRLWVCAT DYADDQRIGP EILKNVVETY
     RKLRNSIRWM LGTLHHYHRD EAVAFADMPE LERLMLHQLA EQSATVRAAY AEFDYKTVVA
     SLAAFMNTEL SAFYFDIRKD TLYCDPPSSL ARKAALTTID IICDAILKWL APVLSFTADE
     AWSMYRPDAE PSVHLTLFPL DLGEYRDDAL AKKWTLIRAV RRVVTGALEV ERAAKRIGSS
     LEASPMIYLP EAFMGDIFDV DWAEICITSN AMVEILRGND TPPADAFRLP ELADVAVVVE
     RAQGTKCARS WKILSSVGSD AEYPDVSPRD AQALREWKAL GGAAA