SYI_MYCPN
ID SYI_MYCPN Reviewed; 861 AA.
AC P75258;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 127.
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=MPN_520;
GN ORFNames=MP322;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
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 -!- 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; U00089; AAB95970.1; -; Genomic_DNA.
DR PIR; S73648; S73648.
DR RefSeq; NP_110208.1; NC_000912.1.
DR RefSeq; WP_010874876.1; NC_000912.1.
DR AlphaFoldDB; P75258; -.
DR SMR; P75258; -.
DR STRING; 272634.MPN_520; -.
DR EnsemblBacteria; AAB95970; AAB95970; MPN_520.
DR KEGG; mpn:MPN_520; -.
DR PATRIC; fig|272634.6.peg.577; -.
DR HOGENOM; CLU_001493_7_1_14; -.
DR OMA; HLGTAWN; -.
DR BioCyc; MPNE272634:G1GJ3-853-MON; -.
DR Proteomes; UP000000808; 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: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 Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 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;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..861
FT /note="Isoleucine--tRNA ligase"
FT /id="PRO_0000098424"
FT MOTIF 57..67
FT /note="'HIGH' region"
FT MOTIF 590..594
FT /note="'KMSKS' region"
FT BINDING 549
FT /ligand="L-isoleucyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:178002"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 593
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
SQ SEQUENCE 861 AA; 99527 MW; 6A521066C0EE235D CRC64;
MNLKKTLLMP QTAFEMQGKL TTKEQQFQAF WQSKRIYQKL HRQNKDKPQK ILHDGPPYAN
GNIHVGHALN KILKDFVLRS WNLQGFGTVF IPGWDCHGLP IEHAVSKKDP QHYASLSLSE
KRDLCKQFAL SQIAIQKAQF QRLGLLNDFS KYYKTIDESF QQNELDLFLQ AVKKDLIFQA
LKPTYWSPVS RTSLAEAEIE YKEVKTIGLY LTFTVVQSAV LNSGTKLLVW TTTPWTLPTN
QAIAVHPQFE YLLFTYNNEQ YVVLASLFES LKTKFGWTDA IQVQTISGSQ LQNTTYKHCL
YDKVNPVLLG NHVLCNEGTG LVHTSPAYGL DDFYLCKQNK LNEALVSLDE KGVFNDTLND
PVLTGLFYLK ANDVIIERLK QHHNFVFSES FLHREPHDWR SKTPVIYRAS KQLFIKTKSI
QSKLKRQIKR VKFVNNKNKE RLQEMLLQRA EWCISRQRVW GLPIPLIYAD NQPLLDVTTI
KYTIQQLKKY GIDSWFEKDI NFFLNPKKIQ PGVEYKKETD TLEVWFDSGS TYNVLISNKL
NFPADLYLEG SDQYRGWFNS SASCGIIQTD QLPFKSLISH GFTLDEHGNK MSKSLGNVVD
PLKLCDQYGA DILRLWVTNV DWQVDNRIGD NIIKQIVEQY RRIRNSLLRF ILGNLNHFNF
GEMKDYRFAL EDKIVIHKTN ALVQELHQWL KQYNFLNCLK AINKFVLWLS GWYFEIIKDT
LYCDAKTNPN RVAKQAVLNY IFTQLIGFLN IFIPHTAEDA WQNYLLPKKP VSVNLFAGPA
MFKVANVKGL DRLHESFSAI KDRAYAAIEQ ARQNGVITKN NQVVLTLGVD STSAIDPTSC
KTFSSLAKRK PGKYNEWPQR N
