ID   SYI_BARQU               Reviewed;         971 AA.
AC   Q6G0K6;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 113.
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};
GN   OrderedLocusNames=BQ02440;
OS   Bartonella quintana (strain Toulouse) (Rochalimaea quintana).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=283165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Toulouse;
RX   PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA   Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA   Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA   La Scola B., Holmberg M., Andersson S.G.E.;
RT   "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT   of the zoonotic agent Bartonella henselae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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; BX897700; CAF25747.1; -; Genomic_DNA.
DR   RefSeq; WP_011179057.1; NC_005955.1.
DR   AlphaFoldDB; Q6G0K6; -.
DR   SMR; Q6G0K6; -.
DR   KEGG; bqu:BQ02440; -.
DR   eggNOG; COG0060; Bacteria.
DR   HOGENOM; CLU_001493_7_1_5; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000000597; 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; 1.10.730.20; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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   NCBIfam; TIGR00392; ileS; 1.
DR   PANTHER; PTHR42765:SF1; ISOLEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42765; SOLEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 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.
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.
FT   CHAIN           1..971
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_0000098354"
FT   MOTIF           64..74
FT                   /note="'HIGH' region"
FT   MOTIF           643..647
FT                   /note="'KMSKS' region"
FT   BINDING         602
FT                   /ligand="L-isoleucyl-5'-AMP"
FT                   /ligand_id="ChEBI:CHEBI:178002"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT   BINDING         646
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
SQ   SEQUENCE   971 AA;  110443 MW;  C7478D6326045340 CRC64;
     MTVKNETIDY SKTLYLPQTN FPMRGRLPQK ELELIARWDN MGLYAQLRQQ AKDRPLYILH
     DGPPYANGHI HIGHALNKVL KDVIIRSFQM RGFNANYVPG WDCHGLPIEW KIEEKYRAQG
     KNKDDVPLNE FRQECREFAK YWITVQSEEF KRLGVVGDFN SPYTTMAFHA EARIASELMK
     FAMSGQIYRG SKPVMWSVVE RTALAEAEIE YHDYESEVIW VKFPVLQADS SDLCGAYVVI
     WTTTPWTIPG NRAVSYSSQI SYGVYEVAST QNDFGPQVGE RLLFADALAM SCAEKAKLVL
     KRLRIISADE LKTLFLFHPL KGFAGSYNDK IAMLDGAHVT ENAGTGFVHT APSHGREDFE
     IWNAYKPLLE QFGIDSSIPF PVDDAGFYTK DAPGFGPNRE GGAVRVIDDN GKMGDANKEV
     INALIKADRL FARGRLKHSY PHSWRSKKPV IFRNTPQWFI SMDKDLGDGS TLRSRALEAV
     SMTRFVPSSG QSRLASMIAD RPDWVLSRQR AWGVPICIFA NEDGVILKDE RVNERILRAF
     EAEGADAWFA EGARERFLGE RAHESWVQVL DILDVWFDSG ASHSFVLEDR DDLKWPADVY
     FEGSDQHRGW FQSSLLESCG TRACSPYKAV ITHGFTLDEN GKKMSKSLGN TVVPQEIIKT
     SGADIFRLWV MTTDYWEDQR LGKQILQTNM DLYRKLRNAI RWMLGILAHD EGEKISYCAL
     PDLEKFILHQ LFELDQLINR AYDEFDFKKI MRALLDFSIT ELSAFYFDIR KDSLYCDAPS
     SKKRKASLQV IREIFERMVI WLAPMLPFTM EEAWLEHSPK SHSVHLEQFR SVPGEWQNGF
     LAERWRKVRQ VRKVVTGALE FERAAKRIGS SLEAAPIVFI SNPVLLEALE NLDMAEICIT
     SALTITQDVP PSDAFILSDV EGVGVYPGKA LGTKCARSWR YTQDVGSDPA YPDVSARDAA
     ALRELQMLGK I
//