SYI_BRUSU
ID SYI_BRUSU Reviewed; 972 AA.
AC Q8FX81; G0KF41;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=BRA0202, BS1330_II0199;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(2011).
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; AE014292; AAN33408.1; -; Genomic_DNA.
DR EMBL; CP002998; AEM19685.1; -; Genomic_DNA.
DR RefSeq; WP_006191694.1; NZ_KN046805.1.
DR AlphaFoldDB; Q8FX81; -.
DR SMR; Q8FX81; -.
DR EnsemblBacteria; AEM19685; AEM19685; BS1330_II0199.
DR GeneID; 45053276; -.
DR KEGG; bms:BRA0202; -.
DR KEGG; bsi:BS1330_II0199; -.
DR PATRIC; fig|204722.22.peg.2986; -.
DR HOGENOM; CLU_001493_7_1_5; -.
DR OMA; HLGTAWN; -.
DR PhylomeDB; Q8FX81; -.
DR Proteomes; UP000007104; 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; 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.
FT CHAIN 1..972
FT /note="Isoleucine--tRNA ligase"
FT /id="PRO_0000098364"
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; 109989 MW; 273BAD80544BD61A CRC64;
MTDTTKIDYS KTLYLPQTEF PIRAGLPQRE PLFVQRWEEM NLYKKLREQA KDRPLYVLHD
GPPYANGNIH IGHALNKILK DVITRSFQMR GYNSNYVPGW DCHGLPIEWK IEEKYRAAGK
NKDEVPINEF RKECRELASN WIKVQTEEFK 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 TTLRSRALKA
IDETRFVPAA 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
