ID Q1CZ22_MYXXD Unreviewed; 1247 AA.
AC Q1CZ22;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 18-JUN-2025, entry version 136.
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 OrderedLocusNames=MXAN_6220 {ECO:0000313|EMBL:ABF90022.1};
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
OC Cystobacterineae; Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF90022.1, ECO:0000313|Proteomes:UP000002402};
RN [1] {ECO:0000313|EMBL:ABF90022.1, ECO:0000313|Proteomes:UP000002402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402};
RX PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA Kaplan H.B.;
RT "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
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=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_02003};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|HAMAP-Rule:MF_02003};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245, ECO:0000256|HAMAP-
CC Rule:MF_02003}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC 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|ARBA:ARBA00007078,
CC ECO:0000256|HAMAP-Rule:MF_02003}.
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DR EMBL; CP000113; ABF90022.1; -; Genomic_DNA.
DR RefSeq; WP_011556164.1; NC_008095.1.
DR AlphaFoldDB; Q1CZ22; -.
DR STRING; 246197.MXAN_6220; -.
DR EnsemblBacteria; ABF90022; ABF90022; MXAN_6220.
DR GeneID; 41363447; -.
DR KEGG; mxa:MXAN_6220; -.
DR eggNOG; COG0060; Bacteria.
DR HOGENOM; CLU_001493_1_1_7; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000002402; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; cd07961; Anticodon_Ia_Ile_ABEc; 1.
DR FunFam; 3.40.50.620:FF:000063; Isoleucine--tRNA ligase; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 1.
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};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02003};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02003};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW 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:UP000002402};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_02003}.
FT DOMAIN 25..686
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 876..1027
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 55..65
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT MOTIF 661..665
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 664
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1247 AA; 140232 MW; 6E98F668283DD36D CRC64;
MPETPPSLFD AVPAEMDFPS DERRIQAFWK DRRIFERSLE TREDAPSFVF YEGPPTANGL
PHNGHVLTRV IKDLFPRYKT MTGHYVPRKA GWDTHGLPVE VEVEKELRIH GKAEIERYGV
EPFTERCIES VFRYTSEWER LTERIGFWVD LNQAYVTYHR PFVESVWWAL AELHRKGLLY
QGHKVVWWWP QGGTALSAAE VGLGYKTVDD PSVYVAFPLR DTPDTALVVW TTTPWTLPSN
MYAAVNPGVD YVTVDAGERK LIVAAALREA LAKKLKQDLP VLATQKGSDL VGQRYQPPFD
LYHQRAGDTR LPLKDGGEDA QAWRVLGADF VTLDSGTGIV HIAPAFGEDD YEAFRKDKAR
FAQPEALELF CAVKPDGTFS DDVPLVAGRF VKEADKDIQR HLKERGLVLF TEQYKHEYPF
CWRADDDPLI QFARPAWYIR TTSVKDEAIA NNRAVNWVPE HIKEGRFGDF LANNVDWALS
RERYWGTPLP LWVHSETGEV EAIPSLQALR EKPGNNVAAV EAELNAFLAG KPHEANARHL
IVHKPWIDKV TFEKPGMPGR FQRVPEVVDV WFDSGCMPFA QWGFPHAPGS REIFNRAFPA
DFISEAIDQT RGWFYSLLMV STLLFDEETQ ARMGLSPQRG WPQPYKSCIV LGHVSDKEGR
KESKSKGNYT PPEIILDEVR MDFAVLTATE AGVPGEPGVA LIAREDLEGL DIQEGAKVQL
FRPDRPDVVI TATVKAHKKL KRRVLLLAPA DLQTLDVAPS ARGASVMPVE VPRLAPSERV
VLKDPAAKAP GADAFRWFFY AASPTWSNTR HSLSNVRLLQ KDFQVKLRNV YSFFTIYANI
DGFNPAAGNT DATDSPWEAI RRSQGWREVK ARPVLDRWIL SEVHLTLRDV TSALDTYQVY
DAAQRMVALV DALSNWYLRR SRSRFWAPGF EQDKQDAYFT LYEALTTIAS LSAPFIPFFA
DEMWGNLVRK PWPTTQPESV HLARFPTVDA SLIDEGLAAE MGAVRDLVSL GLKVRTDNRL
KVRQPLSRAD VILARKELTD RVAVYRDLIA DELNVHEVRF VEPGSPEADV VRFRVRPNLR
AVGGRLGPKL APVRKAFDTG DGAALHRELL QTGRVAMTVA GEDLVFTAEE LETLVEANPG
YAAAGMGVGV VVLHTELTES LVDEGLVREL LARVQGARKD MELGYTDRIQ LWVDGDARVK
RVTDEARELI ARETLASSIL VGPEGLTGKE EEASINGLPA RIRVERA
//
