ID   SYI_BRUME               Reviewed;         972 AA.
AC   Q8YB57;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 128.
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};
GN   OrderedLocusNames=BMEII1043;
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=224914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094;
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA   Haselkorn R., Kyrpides N.C., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen Brucella
RT   melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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; AE008918; AAL54285.1; -; Genomic_DNA.
DR   PIR; AB3640; AB3640.
DR   RefSeq; WP_004681446.1; NZ_GG703779.1.
DR   AlphaFoldDB; Q8YB57; -.
DR   SMR; Q8YB57; -.
DR   GeneID; 29595769; -.
DR   KEGG; bme:BMEII1043; -.
DR   KEGG; bmel:DK63_2213; -.
DR   PATRIC; fig|224914.52.peg.2319; -.
DR   eggNOG; COG0060; Bacteria.
DR   PhylomeDB; Q8YB57; -.
DR   Proteomes; UP000000419; Chromosome II.
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; 1.10.730.20; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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   NCBIfam; TIGR00392; ileS; 1.
DR   PANTHER; PTHR42765:SF1; ISOLEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42765; SOLEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   PRINTS; PR00984; TRNASYNTHILE.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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.
FT   CHAIN           1..972
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098363"
FT   MOTIF           63..73
FT                   /note="'HIGH' region"
FT   MOTIF           644..648
FT                   /note="'KMSKS' region"
FT   BINDING         603
FT                   /ligand="L-isoleucyl-5'-AMP"
FT                   /ligand_id="ChEBI:CHEBI:178002"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT   BINDING         647
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
SQ   SEQUENCE   972 AA;  110128 MW;  24AB8579DC331C18 CRC64;
     MTDTTKIDYS KTLYLPQTEF PMRAGLPQRE PLFVQRWEEM NLYKKLREQA KDRPLYVLHD
     GPPYANGNIH IGHALNKILK DVITRSFQMR GYNSNYVPGW DCHGLPIEWK IEEKYRAAGK
     NKDEVPINEF RKECREFASN WIRVQTEEFK RLAILGDFEN PYTTMNFHAE ARIAGELLKF
     AASGQLYRGS KPVMWSVVER TALAEAEVEY HDIESDMIWV KFPVAGEVAT ENDLSGSAVV
     IWTTTPWTIP GNRAVSYSSR IEYGLFEITE AENDFGPRPG ERLVFADKLV EECCAKAKLQ
     FKRLRSVSAE ELGKIVLDHP LKGFGGGYEF VVPMLDGDHV TDDAGTGFVH TAPSHGREDF
     EAWMDNARQL EARGIDPNIP FPVGDDGFYT KDAPGFGPDR EGGPARVIDD NGKKGDANKV
     VIEQLIAADK LFARGRLKHS YPHSWRSKKP VIFRNTPQWF VYMDKNLGDG TTLRSRALKV
     IDETRFVPTA GQTRLRSMIE GRPDWVLSRQ RAWGVPICVF VDEEGNILQD DAVNKRIMDA
     FEKEGADAWF ADGARERFLG ARAGEGWTQV RDILDVWFDS GSTHTFTLED RPDLKWPADV
     YLEGSDQHRG WFHSSLLESC GTRGRAPYNA VVTHGFTMDE HGKKMSKSLG NTVTPQDVIK
     ESGADILRLW VMTTDYWEDQ RLGKSIIQTN IDAYRKLRNT IRWMLGTLAH DEGENVAYAD
     LPELERLMLH RLTELDELVR SGYDTFDFKR IARALVDFMN VELSAFYFDI RKDALYCDAP
     SSIRRKAALQ TVREIFVRLT TWLAPMLPFT MEEAWLDRYP QSVSIHAEQF RPTPAEWRDD
     VLAEKWRKVR AVRRVVTGAL ELERADKRIG SSLEAAPVVY IADKSLSDSL EGLDFAEICI
     TSGISVSDAA APEGAFTLGD VKGVAVVPER AKGEKCARSW RYTTDVGADP EFPEVSARDA
     AALRELQALG KL
//