SYI_MYCGE
ID SYI_MYCGE Reviewed; 895 AA.
AC P47587;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2018, sequence version 2.
DT 03-AUG-2022, entry version 145.
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=MG345;
OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS (Mycoplasmoides genitalium).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=243273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT "The minimal gene complement of Mycoplasma genitalium.";
RL Science 270:397-403(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 262-371 AND 605-711.
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993;
RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT "A survey of the Mycoplasma genitalium genome by using random sequencing.";
RL J. Bacteriol. 175:7918-7930(1993).
RN [3]
RP SEQUENCE REVISION TO 791, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=16407165; DOI=10.1073/pnas.0510013103;
RA Glass J.I., Assad-Garcia N., Alperovich N., Yooseph S., Lewis M.R.,
RA Maruf M., Hutchison C.A. III, Smith H.O., Venter J.C.;
RT "Essential genes of a minimal bacterium.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:425-430(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: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 -!- DISRUPTION PHENOTYPE: Probably essential, it was not disrupted in a
CC global transposon mutagenesis study. {ECO:0000269|PubMed:16407165}.
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; L43967; AAC71570.2; -; Genomic_DNA.
DR EMBL; U02196; AAD12482.1; -; Genomic_DNA.
DR EMBL; U02254; AAD12519.1; -; Genomic_DNA.
DR PIR; B64238; B64238.
DR RefSeq; WP_010869443.1; NC_000908.2.
DR AlphaFoldDB; P47587; -.
DR SMR; P47587; -.
DR STRING; 243273.MG_345; -.
DR EnsemblBacteria; AAC71570; AAC71570; MG_345.
DR KEGG; mge:MG_345; -.
DR eggNOG; COG0060; Bacteria.
DR HOGENOM; CLU_001493_7_1_14; -.
DR OMA; HLGTAWN; -.
DR OrthoDB; 32262at2; -.
DR BioCyc; MGEN243273:G1GJ2-432-MON; -.
DR Proteomes; UP000000807; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
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; IBA:GO_Central.
DR CDD; cd07960; Anticodon_Ia_Ile_BEm; 1.
DR Gene3D; 3.40.50.620; -; 2.
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; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc.
FT CHAIN 1..895
FT /note="Isoleucine--tRNA ligase"
FT /id="PRO_0000098417"
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"
FT BINDING 869
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 872
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 888
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 891
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
SQ SEQUENCE 895 AA; 104468 MW; 8ED8F6C88F19BB08 CRC64;
MDLKKTLLMP KTSFAMQANL STSEKNFHDF WKDKKVFQKL KKQNKGKQIK ILHDGPPYAN
GSIHVGHALN KILKDFILRS WLYEGYDVVF IPGWDCHGLP IEHAVSKKNP SSYSNLSTVE
KRKLCHQFAL SQIAVQKEQF QRLGLLNDFQ NCYYTIDESF QFKELELFLQ AIKKGLIFQD
LKPTYWSPIS RTSLAEAEIE YKEVNSIALY LTFKVSKSDF LDENANLLVW TTTPWTLPTN
QAIAIHPDFD YLLFEYNQQK FVILEKLFEV FTNKLNWTNA IKLKKFKGSN LKNSSYSHCF
YNKVLPVLMG IHVVDNEGTG IVHSSPAFGI DDFYLCQKNK IKEVLISIDE KGVFNNLLND
KELENCFYLK ANDLIINRLK QNNSFIFSEV ISHREPHDWR SKTPVIYRAS KQLFIKTKSI
KKQLKKQINQ VNFLNSKNQL RLKEMLLQRD EWCISRQRVW GLPIPIVYAN NKPLLDFSTI
QYTIKQLKKH GIDSWFEKDV TCFLKPDKTK KWVKYHKEID TLDVWFDSGS SYNVLEINKY
GSIADLYIEG SDQYRGWFNS SSNCGIIQND LIPFKSLVSH GFTLDENGNK MSKSLGNIVD
PLKICDQYGA DILRLWVANT DWQIDNKIGV NILKQVAEQY RRIRNSLLRF ILGNINGFNF
TSMDDYKFSL EDKIVIHKTN SLVEQIEKFL EKYNFLGCLK VINKFVLWLS SWYFEIIKDT
LYCDAKNNPN RLAKQAVLNY IFTQLISFLN IFIPHTAEDA WKNYSFNKKP ISVNLFTKPT
VFKVANSKNL ENIYKTFTSI KNAAFKEIEK LRKEGLISKN NQIELTVGIN KKIPKKLKDN
LALWLNVNSV NLTNNENEIK VKKTKKTMCE RCWNFQTIIK QKLDHNLCSR CFKVC
