ID A0A918XU49_9PROT Unreviewed; 936 AA.
AC A0A918XU49;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 28-JAN-2026, entry version 14.
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:GHD56448.1};
GN ORFNames=GCM10017083_36410 {ECO:0000313|EMBL:GHD56448.1};
OS Thalassobaculum fulvum.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Rhodospirillales; Thalassobaculaceae; Thalassobaculum.
OX NCBI_TaxID=1633335 {ECO:0000313|EMBL:GHD56448.1, ECO:0000313|Proteomes:UP000630353};
RN [1] {ECO:0000313|EMBL:GHD56448.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KCTC 42651 {ECO:0000313|EMBL:GHD56448.1};
RX PubMed=25193709;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Walter F., Albersmeier A., Kalinowski J., Ruckert C.;
RT "Complete genome sequence of Corynebacterium casei LMG S-19264T (=DSM
RT 44701T), isolated from a smear-ripened cheese.";
RL Int. J. Syst. Evol. Microbiol. 189:76-77(2014).
RN [2] {ECO:0000313|EMBL:GHD56448.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KCTC 42651 {ECO:0000313|EMBL:GHD56448.1};
RA Sun Q., Kim S.;
RL Submitted (SEP-2020) 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=tRNA(Ile) + L-isoleucine + ATP = L-isoleucyl-tRNA(Ile) + AMP +
CC diphosphate; Xref=Rhea:RHEA:11060, Rhea:RHEA-COMP:9666, Rhea:RHEA-
CC COMP:9695, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58045,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78528, ChEBI:CHEBI:456215; EC=6.1.1.5;
CC Evidence={ECO:0000256|ARBA:ARBA00048359, ECO:0000256|HAMAP-
CC Rule:MF_02002};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02002};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GHD56448.1}.
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DR EMBL; BMZS01000009; GHD56448.1; -; Genomic_DNA.
DR RefSeq; WP_189992285.1; NZ_BMZS01000009.1.
DR AlphaFoldDB; A0A918XU49; -.
DR Proteomes; UP000630353; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0002161; F:aminoacyl-tRNA deacylase 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:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd07960; Anticodon_Ia_Ile_BEm; 1.
DR CDD; cd00818; IleRS_core; 1.
DR Gene3D; 1.10.730.20; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 1.10.10.830; Ile-tRNA synthetase CP2 domain-like; 1.
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; IPR050081; Ile-tRNA_ligase.
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 Metal-binding {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}; Reference proteome {ECO:0000313|Proteomes:UP000630353};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02002}.
FT DOMAIN 29..649
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 693..844
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 59..69
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT MOTIF 611..615
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT BINDING 570
FT /ligand="L-isoleucyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:178002"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT BINDING 614
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT BINDING 904
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT BINDING 907
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT BINDING 921
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT BINDING 924
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
SQ SEQUENCE 936 AA; 104534 MW; 1FF007E1B3D0C81E CRC64;
MTTDYKNTVF LPKTDFPMRA GLPQREPEIL AWWQEIGLDR RIVDVRKGRE KFILHDGPPY
ANGHLHIGHA LNKILKDVIN RSQHMAGKQT AYVPGWDCHG LPIEWKIEED YRARGQNKDD
VPIVEFRQEC RAFADKWIDV QRAEFKRLGV TGLWDRPYLT MTYPAEAQIA RELGKFLMNG
GLYKGARPVM WSVVEKTALA DAEIEYHDHV STTIHARFPV VRTAAPALEG ATVVIWTTTP
WTMPGNRAVA YGDEIDYAVV EVTAVAENSL AKVGEKLVCA AALLDDFKAQ AKIEAVSELA
RLKGAGLAGT VCAHPLRGHG YDYDVPMLAA DFATDETGTG FVHIAPGHGA DDFELGREHG
LEIPQTVADD GSFYDHVPLF AGMNVLEDNM KIAAILRDHG GIVARGKLKH SYPHSWRSKA
PLIFRNTAQW FISMDTNDLR KTALQAIDDT RFVPASGQTR LRGMIEGRPD WCISRQRAWG
VPIPVFVSKK TGEPLRDQAV LDRIADAFEE EGADAWFASP PSRFLGNDHN PDDFEQVQDI
CDVWFDSGST HAFVLENDPE LQWPASLYLE GSDQHRGWFH SSLLESCGTR GRAPYDAVLT
HGFVLDQDGR KMSKSLGNVT APQEVMDQYG ADILRLWVVS SDYSEDLRIG PDIIKHQVDH
YRRLRNTLRY LLGALDGYTD AETLPVERMP ELERWVLHRI AELDEIVRRC TDDFDFHTLF
TQIHQFCAVD LSAFYFDVRK DSLYCDRPDS ERRRAARTVM AQLFDCLTAW LAPILCFTAE
EAWRTRNTGP ADSVHLREYP AVPAGWRDEA LAAKWAKIRQ LRRVVTGALE LERAEKRIGA
SLQAHPAVYA GADLLAGMQG VDPAEVFITS GATLVEGDGP ADAYRLAEVP GVAVVSALAD
GAKCERCWRV LPEVAVGEPV CDRCDDAVAA GRDAAE
//
