ID   SYI_BARHE               Reviewed;         971 AA.
AC   Q6G4S5;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 115.
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=BH02580;
OS   Bartonella henselae (strain ATCC 49882 / DSM 28221 / CCUG 30454 / Houston
OS   1) (Rochalimaea henselae).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=283166;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49882 / DSM 28221 / CCUG 30454 / Houston 1;
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; BX897699; CAF27070.1; -; Genomic_DNA.
DR   RefSeq; WP_011180208.1; NZ_LRIJ02000001.1.
DR   AlphaFoldDB; Q6G4S5; -.
DR   SMR; Q6G4S5; -.
DR   PaxDb; 283166-BH02580; -.
DR   EnsemblBacteria; CAF27070; CAF27070; BH02580.
DR   GeneID; 64156557; -.
DR   KEGG; bhe:BH02580; -.
DR   eggNOG; COG0060; Bacteria.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000000421; 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_0000098353"
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;  110734 MW;  D404145683BF5EDA CRC64;
     MTVKNETVDY SKTLYLPQTN FPMRAGLPQK ELELMERWEK RGLYAQLRQQ AKDRPLYTLH
     DGPPYANGHI HIGHALNKVL KDVIIRSFQM RGFNANYVPG WDCHGLPIEW KIEEKYRAQG
     KNKDDVPLNE FRQECRQFAQ HWITVQSEEF KRLGVVGDFN RPYTTMAFHA EARIASELMK
     FALSDQIYRG SKPVMWSVVE RTALAEAEIE YHDHESDVIW VKFPVLQADS KDLYDAYVVI
     WTTTPWTIPA NRAVSYSSQI SYSIYEVKSA ENDFGPQVGE KLLFADALVM SCAEKAKLVL
     KRLRVISAKE FKTLVLSHPL KGLAGGYNNK IAMLDGSHVT ESAGTGFVHT APSHGREDFE
     IWNAYKPLLE QSGIDSSIPF PVDDAGFYTK DAPGFGPDRK GGAIRVIDDN GKMGDANKEV
     INALIKADRL FARGRLKHSY PHSWRSKKPI IFRNTPQWFI SMDKDLGDGS TLRSRALKAI
     SMTRFVPSSG QNRLASMIAD RPDWVLSRQR AWGVPICIFA NEDGVILKDE RVNERILRAF
     EAEGADAWFA EGARERFLGE RAHESWIQVV DILDVWFDSG ASHSFVLEDR DDLNWPADVY
     FEGSDQHRGW FQSSLLESCG TRACSPYKAV ITHGFTLDEN GKKMSKSLGN TVVPQEIIKT
     FGADIFRLWV MTTDYWEDQR LGKQILQTNV DSYRKLRNAI RWMLGTLAHD EGEEISYCAL
     PDLEKLILHR LSELDQLVNR AYDDFDFKKI MRALLDFSIT ELSAFYFDIR KDSLYCDPPS
     SKKRKASLQV VREIFERMVI WLAPMLPFTM EEAWLERYPE STSVHLEQFR PVPMEWQNES
     LAERWKKIRQ VRKVVTGALE LERADKRIGS SLEAAPIVFI SNPVLREALE NLDMAEICIT
     SALTITQGVP PSDAFILSDV EGVGVYPRKA LGTKCARSWR YTQDVGSDPT YPDVSARDAA
     ALRELQVLGK I
//