SYI_BRUAB
ID SYI_BRUAB Reviewed; 972 AA.
AC P0C123; Q579P3;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=BruAb2_0197;
OS Brucella abortus biovar 1 (strain 9-941).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=262698;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9-941;
RX PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT "Completion of the genome sequence of Brucella abortus and comparison to
RT the highly similar genomes of Brucella melitensis and Brucella suis.";
RL J. Bacteriol. 187:2715-2726(2005).
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; AE017224; AAX75641.1; -; Genomic_DNA.
DR RefSeq; WP_002966382.1; NC_006933.1.
DR AlphaFoldDB; P0C123; -.
DR SMR; P0C123; -.
DR PRIDE; P0C123; -.
DR EnsemblBacteria; AAX75641; AAX75641; BruAb2_0197.
DR GeneID; 3827171; -.
DR KEGG; bmb:BruAb2_0197; -.
DR HOGENOM; CLU_001493_7_1_5; -.
DR OMA; HLGTAWN; -.
DR Proteomes; UP000000540; 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_0000098361"
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; 110042 MW; 439543DEDCC20013 CRC64;
MTDTTKIDYS KTLYLPQTEF PMRAGLPQRE PLFVQRWEEM NLYKKLREQA KDRPLYVLHD
GPPYANGNIH IGHALNKILK DVITRSFQMR GYNSNYVPGW DCHGLPIEWK IEEKYRAAGK
NKDEVPINEF RKECREFASN 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
