ID B3PRC2_RHIE6 Unreviewed; 968 AA.
AC B3PRC2;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 106.
DE RecName: Full=Isoleucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02002};
DE EC=6.1.1.5 {ECO:0000256|HAMAP-Rule:MF_02002};
DE AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02002};
DE Short=IleRS {ECO:0000256|HAMAP-Rule:MF_02002};
GN Name=ileS {ECO:0000256|HAMAP-Rule:MF_02002,
GN ECO:0000313|EMBL:ACE89905.1};
GN OrderedLocusNames=RHECIAT_CH0000920 {ECO:0000313|EMBL:ACE89905.1};
OS Rhizobium etli (strain CIAT 652).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=491916 {ECO:0000313|EMBL:ACE89905.1, ECO:0000313|Proteomes:UP000008817};
RN [1] {ECO:0000313|EMBL:ACE89905.1, ECO:0000313|Proteomes:UP000008817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIAT 652 {ECO:0000313|EMBL:ACE89905.1,
RC ECO:0000313|Proteomes:UP000008817};
RA Gonzalez V., Acosta J.L., Santamaria R.I., Bustos P.,
RA Hernandez-Gonzalez I.L., Fernandez J.L., Diaz R., Flores M., Mora J.,
RA Palacios R., Davila G.;
RT "Genome diversity and DNA divergence of Rhizobium etli.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00025217, ECO:0000256|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;
CC Evidence={ECO:0000256|ARBA:ARBA00000114, ECO:0000256|HAMAP-
CC Rule:MF_02002};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02002}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_02002}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC IleS type 1 subfamily. {ECO:0000256|ARBA:ARBA00006887,
CC ECO:0000256|HAMAP-Rule:MF_02002}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02002}.
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DR EMBL; CP001074; ACE89905.1; -; Genomic_DNA.
DR AlphaFoldDB; B3PRC2; -.
DR KEGG; rec:RHECIAT_CH0000920; -.
DR eggNOG; COG0060; Bacteria.
DR HOGENOM; CLU_001493_7_1_5; -.
DR OMA; IHLGTAW; -.
DR Proteomes; UP000008817; Chromosome.
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 {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_02002};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02002};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02002};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02002};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02002};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_02002}.
FT DOMAIN 34..680
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 724..873
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 64..74
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT MOTIF 642..646
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT BINDING 601
FT /ligand="L-isoleucyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:178002"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT BINDING 645
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
SQ SEQUENCE 968 AA; 108688 MW; 1F43C8AB36769976 CRC64;
MTDTAEKIDY SKTLYLPETD FPMRAGLPQK EPELVKRWQE MDLYKKLRAS AAGREKFVLH
DGPPYANGNI HIGHALNKIL KDVINRSFQM RGYDANYVPG WDCHGLPIEW KIEEENYRAK
GKAKPDLKEP AAMIEFRREC RAYAEKWIKV QGDEFQRLGI VGDFDNPYLT MNFHAESRIA
GELLKIAASG QLYRGSKPIM WSVVERTALA EAEVEYHDYE SDTIWVKFPV AKGPDGVKDA
FVVIWTTTPW TIPGNRAIAY SSRVAYGLYE VTAAENDFGP RPGEKLIFAD KLAEESFAKA
KLQYKRLADV TAADLAGITC AHPLKGLGGG YEFAVPLLEG DHVTDDAGTG FVHTAPSHGR
EDFDVWMAHG REIEARGIET KIPFPVDDGG FYTADAPGLE GARVIDDNGK KGDANDRVIK
ALIERSALFA RGRLKHQYPH SWRSKKPVIF RNTPQWFVYM DKTLPDGTTL RTRALTAIDD
TRFVPAAGQN RLRAMIEQRP DWVLSRQRAW GVPICVFVDE HGAVLQDEAV NARILEAFDA
EGADAWFAEG AKERFLGNEH DPAKWSQVMD ILDVWFDSGS THTFTLEDRP DLKWPADLYL
EGSDQHRGWF HSSLLESAAT RGRAPYNAVL THGFTMDEKG EKMSKSKGNV TAPQEVMKDA
GADILRLWVM TSDYADDLRV GKTIIQTNVD AYRKLRNTIR WMLGTLAHDK GEEIALADLP
ELEQLMLHRL AELDQLVREN YDAFDFKKIA RALIDFANVE LSAFYFDVRK DALYCDAPSS
LRRRASLHVI RQIFDCMVTW LAPMLPFTTE EAWLSRNPSA VSVHLEQFAP VAKEWRNDAL
AEKWKKIRAV RSVVTGALEI ERKDKRIGSS LEAAPVVHIA DAELRKALEG QDFSEVCITS
GITIKADAGP AEAFRLAEVP DVAVVPTLAE GVKCARSWRI TTDVGSDPDY PDVSARDAAT
LRELGIRA
//