ID A0A0D0QPG6_9FIRM Unreviewed; 978 AA.
AC A0A0D0QPG6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Isoleucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02003};
DE EC=6.1.1.5 {ECO:0000256|HAMAP-Rule:MF_02003};
DE AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02003};
DE Short=IleRS {ECO:0000256|HAMAP-Rule:MF_02003};
GN Name=ileS {ECO:0000256|HAMAP-Rule:MF_02003};
GN ORFNames=P261_01763 {ECO:0000313|EMBL:KIR02948.1};
OS Lachnospiraceae bacterium TWA4.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1392836 {ECO:0000313|EMBL:KIR02948.1, ECO:0000313|Proteomes:UP000032079};
RN [1] {ECO:0000313|EMBL:KIR02948.1, ECO:0000313|Proteomes:UP000032079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TWA4 {ECO:0000313|EMBL:KIR02948.1,
RC ECO:0000313|Proteomes:UP000032079};
RX PubMed=25495654;
RA Gagen E.J., Wang J., Padmanabha J., Liu J., de Carvalho I., Liu J.,
RA Webb R.I., Al Jassim R., Morrison M., Denman S.E., McSweeney C.S.;
RT "Investigation of a new acetogen isolated from an enrichment of the tammar
RT wallaby forestomach.";
RL BMC Microbiol. 14:314-314(2014).
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_02003}.
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_02003};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02003};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02003}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02003}.
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_02003}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC IleS type 2 subfamily. {ECO:0000256|HAMAP-Rule:MF_02003}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02003}.
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:KIR02948.1}.
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DR EMBL; JPZU01000001; KIR02948.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0QPG6; -.
DR STRING; 1392836.P261_01763; -.
DR PATRIC; fig|1392836.3.peg.2008; -.
DR Proteomes; UP000032079; 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; cd07961; Anticodon_Ia_Ile_ABEc; 1.
DR CDD; cd00818; IleRS_core; 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_02003; Ile_tRNA_synth_type2; 1.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033709; Anticodon_Ile_ABEc.
DR InterPro; IPR002301; Ile-tRNA-ligase.
DR InterPro; IPR023586; Ile-tRNA-ligase_type2.
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; PTHR42780:SF1; ISOLEUCINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR42780; SOLEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF19302; DUF5915; 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.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_02003};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02003}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02003};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02003};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02003};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02003};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_02003}; Reference proteome {ECO:0000313|Proteomes:UP000032079};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT DOMAIN 2..560
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 616..765
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 529..533
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 532
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 978 AA; 112043 MW; FB52C902F1521B3D CRC64;
MIPRYHAMKG AMVPRKAGWD THGLPVELEV EKKLGLDGKE QIEEYGLEPF INHCKESVWK
YKGMWEDFSD TVGFWADMEN PYVTYDNNFI ESEWWSLKKI WEKGLLYKGF KIVPYCPRCG
TPLSSHEVAQ GYKAVKERSA IVRFKVAGED AYFLAWTTTP WTLPSNTGLC VNPDETYNKV
KTNDGYTYYM ANALLDKVLG EVGYEIVETY VGKDLEYKEY EPLFACAGEV AAKQKKKAHF
VTCDSYVTMS DGTGIVHIAP AFGEDDAKVG RKYDFPFIQF VDGKGNMTEE TPYAGLFVKD
ADPKILVDLD KDGKLFSAPK FEHDYPFCWR CDTPLIYYAR ESWFIKMTEV KDQLIRNNNT
INWIPESIGK GRFGDWLENV QDWGLSRNRY WGTPLPIWEC ECGKRHAIGS IAELKEMSPN
CPEDIELHRP YIDAVTIECP DCHKQMKRVS EVIDCWYDSG SMPFAQHHYP FENEDLFKAQ
FPADFISEAV DQTRGWFYSL LAISTLIFDK APFKNVIVMG HVQDKDGQKM SKSKGNAVDP
FNALEKHGAD AIRWYFYTSS APWLPKRFHD DAVTEGQRKF MGTLWNTYAF YVLYAEIDQF
DPTKYSLDYN KLSVMDKWLL SKMNSVVGEV DNFLANYKIP EAARALQEFV DDMSNWYVRR
SRERFWAKGM EQDKINAYMT LYTALVTISK AAAPMIPFMT EQIYQNLVRN LDSNAPESIH
LCDYPEANAA HIDKELEKHM ETVLKVVVMG RACRNTANIK NRQPIGHMYV KTEDTLPEYY
QSIITEELNV KEIEFTEDMR SFTSYTFKPQ MRTVGPKYGK LLNAIKGKLA ELDGNKAMDE
LNANGQLVFE LDGNEVVLTA DDLLIDTAQM PGFVSEQDNT LTVVLDTNLT DKLLEEGFVR
EIASKIQTMR KEAGFEVTDH IFVYVDNNEK IVTLMGAYAA EIKGAVMADQ IHANAMAGYS
KEWNINGEKV TLGVEKIQ
//
