ID   SYI_BACTN               Reviewed;        1162 AA.
AC   Q8A9K9;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 124.
DE   RecName: Full=Isoleucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02003};
DE            EC=6.1.1.5 {ECO:0000255|HAMAP-Rule:MF_02003};
DE   AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02003};
DE            Short=IleRS {ECO:0000255|HAMAP-Rule:MF_02003};
GN   Name=ileS {ECO:0000255|HAMAP-Rule:MF_02003};
GN   OrderedLocusNames=BT_0806;
OS   Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS   CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=226186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50;
RX   PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA   Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(2003).
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_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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_02003};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_02003};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02003}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_02003}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       IleS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02003}.
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DR   EMBL; AE015928; AAO75913.1; -; Genomic_DNA.
DR   RefSeq; NP_809719.1; NC_004663.1.
DR   RefSeq; WP_011107458.1; NC_004663.1.
DR   AlphaFoldDB; Q8A9K9; -.
DR   SMR; Q8A9K9; -.
DR   STRING; 226186.BT_0806; -.
DR   PaxDb; 226186-BT_0806; -.
DR   EnsemblBacteria; AAO75913; AAO75913; BT_0806.
DR   GeneID; 60926775; -.
DR   KEGG; bth:BT_0806; -.
DR   PATRIC; fig|226186.12.peg.824; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_1_1_10; -.
DR   InParanoid; Q8A9K9; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000001414; 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; 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; cd07961; Anticodon_Ia_Ile_ABEc; 1.
DR   CDD; cd00818; IleRS_core; 1.
DR   Gene3D; 3.30.720.200; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
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; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc.
FT   CHAIN           1..1162
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098522"
FT   MOTIF           50..60
FT                   /note="'HIGH' region"
FT   MOTIF           710..714
FT                   /note="'KMSKS' region"
FT   BINDING         713
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ   SEQUENCE   1162 AA;  132494 MW;  B6CEFE096695451B CRC64;
     MGKRFTEYSQ FDLSQVNKDV LKKWDENQVF AKSMTERDGC PSFVFFEGPP SANGMPGIHH
     VMARTIKDIF CRYKTMKGYQ VKRKAGWDTH GLPVELSVEK ALGITKEDIG KKISVADYNA
     ACRKDVMKYT KEWEDLTHQM GYWVDMKHPY ITYDNRYIET LWWLLKQLHK KGLLYKGYTI
     QPYSPAAGTG LSSHELNQPG CYRDVKDTTA VAQFKMKNPK PEMAEWGTPY FLAWTTTPWT
     LPSNTALCVG PKIDYVAVQT YNAYTGEPIT VVLAKALLNT HFNSKAADLK LEDYKAGDKL
     VPFKVVAEYK GADLIGMEYE QLIPWVKPVE VSEDGTWKVS GKGFRVIPGD YVTTEDGTGI
     VHIAPTFGAD DANVARAAGI PSLFMINKKG ETRPMVDLTG KFYMLDELDE NFVKECVDVD
     KYKEYQGAWV KNAYNPVFMV DGKYDEKAAQ AAESLDVALC MMMKANNQAF KIEKHIHNYP
     HCWRTDKPVL YYPLDSWFIR STACKERMME LNKTINWKPE STGTGRFGKW LENLNDWNLS
     RSRYWGTPLP IWRTEDGTSE ICIESVEELY NEIEKSVAAG FMKSNPYKDK GFVPGEYTEG
     NYDKIDLHRP YVDDIILVSE DGQPMKRESD LIDVWFDSGA MPYAQIHYPF ENKNILDNRE
     VYPADFIAEG VDQTRGWFFT LHAIATMVFD SVSYKAVISN GLVLDKNGNK MSKRLNNAVD
     PFTTIEKYGS DPLRWYMITN SSPWDNLKFD IDGIEEVRRK FFGTLYNTYS FFALYANVDG
     FEYKEADVPM AERPEIDRWI LSVLNTLIKE VDTCYNEYEP TKAGRLISDF VNDNLSNWYV
     RLNRKRFWGG EFTQDKLSAY QTLYTCLETV AKLMAPISPF YADRLYTDLT TATGRDNVVS
     IHLAEFPKYQ EEMIDKELEA RMQMAQDVTS MVLALRRKVN IKVRQPLQCI MIPVADEEQK
     AHIEAVKALI MNEVNVKDIK FVDGAAGVLV KKVKCDFKKL GPKFGKQMKA VAAAVAEMSQ
     EAIAELEKNG KYALNLDGAE AVIEAADVEI FSEDIPGWLV ANEGKLTVAL EVTVTEELRR
     EGIARELVNR IQNIRKSSGF EITDKIKITI SKNTQTDDAV NEYNTYICNQ VLGTSLDLAD
     EVKDGTELNF DDFSLFVNVI KD
//