SYI_AGRFC
ID SYI_AGRFC Reviewed; 967 AA.
AC Q8UHJ6; Q7D0X7;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, 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}; OrderedLocusNames=Atu0686;
GN ORFNames=AGR_C_1230;
OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS (strain C58)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=176299;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743193; DOI=10.1126/science.1066804;
RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA Gordon M.P., Olson M.V., Nester E.W.;
RT "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT C58.";
RL Science 294:2317-2323(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743194; DOI=10.1126/science.1066803;
RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT "Genome sequence of the plant pathogen and biotechnology agent
RT Agrobacterium tumefaciens C58.";
RL Science 294:2323-2328(2001).
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; AE007869; AAK86495.1; -; Genomic_DNA.
DR PIR; AH2660; AH2660.
DR PIR; F97442; F97442.
DR RefSeq; NP_353710.1; NC_003062.2.
DR RefSeq; WP_010971068.1; NC_003062.2.
DR AlphaFoldDB; Q8UHJ6; -.
DR SMR; Q8UHJ6; -.
DR STRING; 176299.Atu0686; -.
DR PRIDE; Q8UHJ6; -.
DR EnsemblBacteria; AAK86495; AAK86495; Atu0686.
DR KEGG; atu:Atu0686; -.
DR PATRIC; fig|176299.10.peg.682; -.
DR eggNOG; COG0060; Bacteria.
DR HOGENOM; CLU_001493_7_1_5; -.
DR OMA; HLGTAWN; -.
DR PhylomeDB; Q8UHJ6; -.
DR BioCyc; AGRO:ATU0686-MON; -.
DR Proteomes; UP000000813; Chromosome circular.
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; Reference proteome.
FT CHAIN 1..967
FT /note="Isoleucine--tRNA ligase"
FT /id="PRO_0000098339"
FT MOTIF 64..74
FT /note="'HIGH' region"
FT MOTIF 641..645
FT /note="'KMSKS' region"
FT BINDING 600
FT /ligand="L-isoleucyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:178002"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 644
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
SQ SEQUENCE 967 AA; 108483 MW; 709A52EC5623ED0F CRC64;
MSDTAEKLDY STTLYLPQTD FPMRAGLPQK EPETVKRWQD MGLYKKLRAS AAGREKFVLH
DGPPYANGNI HIGHALNKIL KDVITRSFQM RGFDANYVPG WDCHGLPIEW KIEEAYRARG
KNKDEVPVNE FRKECRDFAA GWIKVQSEEF KRLGIEGDFE NPYTTMNFHA EARIAGELLK
IARSGQLYRG SKPIMWSVVE RTALAEAEVE YHDVESDMIW VKFPVKDAAP ALSGVSVVIW
TTTPWTIPGN RAIAFSSRVE YGLFEVESAQ NDFGPQTGEK LIFARKLADE AAAKAKLTFK
FVRDVKSEEL AAITCAHPLA SLGYDFPVPL LDGDHVTDDA GTGFVHTAPS HGREDFDAWT
NSVRTLEARG IDTKIPFPVD DAGFYTEDAP GFGPSAEGGA ARVMDDNGKK GDANERVIKA
LIAANNLFAR GRLKHSYPHS WRSKKPVIFR NTPQWFVYMD KELGDGTTLR SRSLDAIDQT
RFVPASGQNR LRAMIEGRPD WVLSRQRSWG VPIAVFADEQ GEVLVDEAVN ARILEAFEAE
GADAWFAEGA KERFLGNDHD HAKWQQVMDI LDVWFDSGCT HTFTLEDRPD MKWPADVYLE
GSDQHRGWFH SSLLESCATR GRAPYNAVVT HGFTMDEQGR KQSKSLGNVV APQDVMKESG
ADILRLWVMT TDYWEDQRLG KAIIQTNIDA YRKLRNTVRW MLGTLAHDNG EEIAYADLPE
LEKLVLHRLS ELDKVVRDGY DAFDFKKITR ALIDFANVEL SAFYFDIRKD TLYCDAPSSL
KRRASLSVIA KLFDCLVTWL APMLPFTTEE AWLSRYPDAE SVHLAQFPEI PAEWKNDALE
AKWEKIRKVR TVVTGALEVE RREKRIGSSL EAAPVVHIAD SDLLAALSGQ DFAEICITSA
ITVVGDEGPA DGFRLQEVAK VVVEQKLAEG VKCARSWRIT TDVGSDPQYP DVSARDAAAL
RELAALK
