ID   SYI_BDEBA               Reviewed;        1056 AA.
AC   Q6MKX0;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=Bd2257;
OS   Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS   HD100).
OC   Bacteria; Proteobacteria; Oligoflexia; Bdellovibrionales;
OC   Bdellovibrionaceae; Bdellovibrio.
OX   NCBI_TaxID=264462;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100;
RX   PubMed=14752164; DOI=10.1126/science.1093027;
RA   Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA   Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA   Schuster S.C.;
RT   "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT   genomic perspective.";
RL   Science 303:689-692(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; BX842652; CAE80087.1; -; Genomic_DNA.
DR   RefSeq; WP_011164689.1; NC_005363.1.
DR   AlphaFoldDB; Q6MKX0; -.
DR   SMR; Q6MKX0; -.
DR   STRING; 264462.Bd2257; -.
DR   PRIDE; Q6MKX0; -.
DR   EnsemblBacteria; CAE80087; CAE80087; Bd2257.
DR   KEGG; bba:Bd2257; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_1_1_7; -.
DR   OMA; KMMAPFT; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000008080; 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; IPR001412; aa-tRNA-synth_I_CS.
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; 2.
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..1056
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098523"
FT   MOTIF           56..66
FT                   /note="'HIGH' region"
FT   MOTIF           603..607
FT                   /note="'KMSKS' region"
FT   BINDING         606
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1056 AA;  119738 MW;  2B200E2A1FCA95CA CRC64;
     MTNANTRSTP YSAVKPDVNL AKQEETILDF WDQEKIFAQS LNPEGKKTYS FYDGPPFATG
     LPHYGHLLAG VLKDVVPRYW TMKGYTVPRR FGWDCHGLPV EYEINKTHKI ESRKDVFKMG
     VANYNDACRS IVKRYSTEWK TTVRRVGRWV DMENPYFTMD VSFMQSVWWV FQQLFNKGLI
     YEGYKVVPYS VGISTSLSNF EANQNYKMVQ DPAITVMFKL VNQPDTAIMA WTTTPWTLPS
     NLALAVGNDI EYVKVQEKAT GRKLIMAQAL LSSVFKKADE EVEVLQMMKG TELVGLTYEP
     LFPYFGDRAD KGAFRIISSD HVTTESGTGV VHMAPAFGEE DYYACAKAGI PMVNPVDDDG
     MFTMEVPDYA GKRVKEADKD IIADLKKRGN LFKQDTIQHS YPFCYRSDTP LIYRAVSSWF
     VAVEKIKEEL IANNKQTSWV PDHLRDGRFG NWLEGARDWA ISRNRFWGTP LPIWRNAEGE
     VMCIGSRAEL EKLSGQKVDD LHIEFVDKIT IPSPTGKSPL KRVDGVLDCW FESGSMPYAQ
     WGYPETSVED FKKAFPADFI AEGLDQTRGW FYTLSIIGTA LFNQAPFKNV VVNGLVLAED
     GRKMSKSLKN YPDPMEVLNQ HGADALRLYL IDSPVVKAQE LKFSEKGVYD IVRKILLRWW
     NSYSFFANYA NIDGFVPKGD AKKSPNILDQ WVLSRLNGLI ANTHKEMDAY RLYNVVPHLL
     QFIEDLTNTY IRFNRSLFWQ DGMPETKRYA YETLHEVLVT LSRLMAPFAP FMSEVTYKNL
     AQVLKDKKDS VHLESFPTAD LSMLRPELEE AVKAMDTLVT LGRNHREKIG VKAKIPLNEI
     KIIHRSAELL ETLKKFEPFF VDELNFRKVV YNPNEDQFVQ VTAKANFPVL GKRLGPKMKA
     VGAGIMSMSL ENILKLEGGG VVVIEGEEIS LSDVEIRRAP KGDNANLSVH QIVSIEVDPT
     VTPEQEREGL AREIMRKIQV ARKTADFQMD DKITLEIACD GALLDALNAH KDMITGETLT
     KNLNILALTA EPNGKHTETS DIDGQVIKIG VTNLPR