ID A0A1G9QLT5_9GAMM Unreviewed; 946 AA.
AC A0A1G9QLT5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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 ORFNames=SAMN05661010_03396 {ECO:0000313|EMBL:SDM11936.1};
OS Halomonas muralis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=119000 {ECO:0000313|EMBL:SDM11936.1, ECO:0000313|Proteomes:UP000198654};
RN [1] {ECO:0000313|EMBL:SDM11936.1, ECO:0000313|Proteomes:UP000198654}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14789 {ECO:0000313|EMBL:SDM11936.1,
RC ECO:0000313|Proteomes:UP000198654};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 -!- 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}.
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DR EMBL; FNGI01000012; SDM11936.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9QLT5; -.
DR STRING; 119000.SAMN05661010_03396; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000198654; Unassembled WGS sequence.
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: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; 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 InterPro; IPR010663; Znf_FPG/IleRS.
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 Pfam; PF06827; zf-FPG_IleRS; 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:UP000198654};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02002}.
FT DOMAIN 29..647
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 692..848
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 907..934
FT /note="Zinc finger FPG/IleRS-type"
FT /evidence="ECO:0000259|Pfam:PF06827"
FT MOTIF 58..68
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT MOTIF 609..613
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT BINDING 568
FT /ligand="L-isoleucyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:178002"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT BINDING 612
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT BINDING 908
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT BINDING 911
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT BINDING 928
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT BINDING 931
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
SQ SEQUENCE 946 AA; 105656 MW; FC40E3E6A273C91C CRC64;
MSDYKHTLNL PETDFPMRGN LPKREPARVQ HWQQIDLYQR LREAGQGRET FVLHDGPPYA
NGSIHIGHAV NKILKDIIVK SKGLAGFDAP YVPGWDCHGL PIEHKVETTH GKHLPASQAR
ALCREYAAEQ IDGQRTDFVR LGVVGDWARP YRTMDFVNEA GEIRALAEMV KHGYVFKGLK
PVNWCFDCGS ALAEAEVEYA DKQSDAIDVA FPCAEDDKLA AAFGLAELPK PAAAVIWTTT
PWTIPANQAL NVHPEFTYAL VDVGDRLLLL AEELVESCLE RFGREGHIIA TVGGERLSEI
EFAHPFYARR SPVYLADYVE SEVGSTGIVH SSPAYGVDDF NTCRAHGMSF DEIESPVMGN
GVYAEDLKFF GGQMIWKANL QIVAKLDEVD ALLAHKTITH SYMHCWRHKS PVIYRATAQW
FVGMDIEGAD GKTLRQRALD GVEATQFVPA WGKARLHSMI ANRPDWCISR QRNWGVPIPF
FLHKVSGELH PRTVELMEDV AKRVELEGID AWFRLAAEEL IGDDAAHYDK VSDTLDVWFD
SGTTHWHVLR GSHALGHSQG PRADLYLEGS DQHRGWFHSS LLTGCAIDGH PPYKGLLTHG
FTVDAQGRKM SKSVGNVVAP QEVMDKLGAD ILRLWVASTD YSGEMAVSDE ILKRTADVYR
RIRNTSRFLL ANLNGFDATR DAVAFEDMLA LDQWVVDRAA QLQARIEAAY AEYRFLDVYQ
QVHTFCAREL GGFYLDVIKD RQYTTQADSL ARRSCQTALY QVVEALARWV APILSFTAEE
IYEHIPGERK ASVLLETFYT GLSTLGDDAA FGRDFWEQVL EVKQAVNKCL EDARNAKVIK
NSLAAEVTLY ASDELRETLG RLGDELRFVL LTSEVHLASL DSAEASSGEA TELDALRVAV
IASPNTKCER CWHHREDVGS HAEHPDLCGR CISNLPDGPG EVRHYA
//
