SYI_LACLA
ID SYI_LACLA Reviewed; 932 AA.
AC Q9CEH8;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Isoleucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02002};
DE EC=6.1.1.5 {ECO:0000255|HAMAP-Rule:MF_02002};
DE AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02002};
DE Short=IleRS {ECO:0000255|HAMAP-Rule:MF_02002};
GN Name=ileS {ECO:0000255|HAMAP-Rule:MF_02002}; OrderedLocusNames=LL1863;
GN ORFNames=L0350;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
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:0000255|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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_02002};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02002};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_02002};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02002}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_02002}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC IleS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02002}.
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DR EMBL; AE005176; AAK05961.1; -; Genomic_DNA.
DR PIR; G86857; G86857.
DR RefSeq; NP_268020.1; NC_002662.1.
DR RefSeq; WP_010906172.1; NC_002662.1.
DR AlphaFoldDB; Q9CEH8; -.
DR SMR; Q9CEH8; -.
DR STRING; 272623.L0350; -.
DR PaxDb; Q9CEH8; -.
DR EnsemblBacteria; AAK05961; AAK05961; L0350.
DR KEGG; lla:L0350; -.
DR PATRIC; fig|272623.7.peg.1996; -.
DR eggNOG; COG0060; Bacteria.
DR HOGENOM; CLU_001493_7_1_9; -.
DR OMA; HLGTAWN; -.
DR Proteomes; UP000002196; 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: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 Gene3D; 3.40.50.620; -; 2.
DR Gene3D; 3.90.740.10; -; 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 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; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00392; ileS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc.
FT CHAIN 1..932
FT /note="Isoleucine--tRNA ligase"
FT /id="PRO_0000098404"
FT MOTIF 57..67
FT /note="'HIGH' region"
FT MOTIF 593..597
FT /note="'KMSKS' region"
FT BINDING 552
FT /ligand="L-isoleucyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:178002"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 596
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 889
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 892
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 911
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 914
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
SQ SEQUENCE 932 AA; 106509 MW; 85EF03E46A85D751 CRC64;
MKIKDTLNLG KTAFPMRAGL PNKEPNWQKD WADATLYEKR QELNEGKPSF MLHDGPPYAN
GNIHLGHSLN KISKDIIVRY KSMAGFRAPY VPGWDTHGLP IEQQLAKAGM KRKEMDLLDY
LEECRKYAMK QVDMQRSDFK SLGVLADWDR PYLTLLPEYE AAQIRVFGKM AEKGYIYKGQ
KPIYWSPSSE SSLAEAEIEY QDVRSASIFV AFKAKDTKGK LPEDVEFVIW TTTPWTIPSN
LGIFAHPDYD YSVVAVNGRK FVIASEMLEA VAEKLEWENP EVLQTIKGSE LEYMVAKHPF
YDRETLIMNA DYVTLDSGTG LVHVAPGHGE DDYFASRKYK LPVLSPIDNR GYYTDEAPGL
EGLLYDEGNK VVSKWLEEKD ALLKLEFFTH SYPHDWRTKK PVIFRATPQW FASIDDFRQN
ILDEVERVDW VIPWGKTRLF NMVRDRGDWV ISRQRAWGVP LPIFYGENGE PIITPETTEH
VAKLFAEFGS KVWFEREAKD LLPEGFTHPA SPNGEFTKEK DIMDVWFDSG SSWNGVLNER
DYLSFPADLY LEGSDQYRGW FNSSITTSVA VNGVAPYKAV LSQGFVLDGK GRKMSKSIGN
TIVPKDVTKK FGADILRLWV ASIDTESDVR VSMDILSQVS EVYRKIRNTL RFLIANTSDF
NPKEDAIDFA ELRPVDKYML VKFNELVKQI RTAYDNYSFM TVYKSIINFI TNDLSSFYLD
FAKDVVYIEA ANSPERRSMQ TVMYVILKDL VKILVPILPH TAEETWTYLE HEPENFAYLA
EMPEAAEIPG SEELLGNWQE FLDFRDKILK ALESAREAKL IGKSLEATVT IYPNEVVRTL
LTAIDENVAQ LLIVSNFVVA NEPVNNAPES AMKFDDLAVL VEHAAGEVCD RCRRTDETVG
HNANEHLKML CEHCAHIVET EFPEILEEGF ED