SYI_BRUME
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 03-AUG-2022, entry version 120.
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=BMEII1043;
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Proteobacteria; 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 STRING; 224914.BMEII1043; -.
DR PRIDE; Q8YB57; -.
DR EnsemblBacteria; AAL54285; AAL54285; BMEII1043.
DR GeneID; 29595769; -.
DR KEGG; bme:BMEII1043; -.
DR PATRIC; fig|224914.52.peg.2319; -.
DR eggNOG; COG0060; Bacteria.
DR OMA; HLGTAWN; -.
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; 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_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
