SYI_PROM4
ID SYI_PROM4 Reviewed; 969 AA.
AC A9BDK6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=P9211_02611;
OS Prochlorococcus marinus (strain MIT 9211).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=93059;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9211;
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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 -!- 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; CP000878; ABX08192.1; -; Genomic_DNA.
DR RefSeq; WP_012194817.1; NC_009976.1.
DR AlphaFoldDB; A9BDK6; -.
DR SMR; A9BDK6; -.
DR STRING; 93059.P9211_02611; -.
DR EnsemblBacteria; ABX08192; ABX08192; P9211_02611.
DR KEGG; pmj:P9211_02611; -.
DR eggNOG; COG0060; Bacteria.
DR HOGENOM; CLU_001493_7_0_3; -.
DR OMA; HLGTAWN; -.
DR Proteomes; UP000000788; 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:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
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 InterPro; IPR010663; Znf_FPG/IleRS.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR Pfam; PF06827; zf-FPG_IleRS; 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..969
FT /note="Isoleucine--tRNA ligase"
FT /id="PRO_1000189186"
FT MOTIF 68..78
FT /note="'HIGH' region"
FT MOTIF 626..630
FT /note="'KMSKS' region"
FT BINDING 585
FT /ligand="L-isoleucyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:178002"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 629
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 939
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 942
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 959
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 962
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
SQ SEQUENCE 969 AA; 109816 MW; 9C4CAAB0CD942EAF CRC64;
MTKETRQGEQ NRPSYKESLN LLKTSFGMRA NATLREPELQ NFWADKGIDL ELGLANKGPS
FTLHDGPPYA NGALHMGHAL NKVLKDIINK FHIMRGHKVH FVPGWDCHGL PIELKVLQTL
SNKERQALTP IQLRKKAAAY ASKQVKGQME GFKRWGIWGN WNKPYLTLQK EYESAQVKLF
GQMVLKGYIY RGLKPVHWSP SSRTALAEAE LEYPEAHTSP SVYVAFSVIH LPQSLSENLI
KQGLELPGDE VELSKRLKVC IWTTTPWTLP ANAAVSVNSN LDYSFVRHEE KGQILIFATE
LLEEVSEILG ISFKQVANAK GESLKGILYK HPLYERTAPI VLGGSYITTQ SGTGLVHTAP
GHGIDDFKTG LQNNLEVFCP VDEKGIFTSE AGKFEGLNVL KDANKEIISS LEISGSLLKE
LPYVHKYPYD WRTKKPTIFR ATEQWFASVE GFREDALKAI DDVEWLPESG RNRIQSMVRE
RGDWCISRQR TWGIPIPVFY KKNTNEILLN KETIDHIENL FAQYGADIWW EFDESKLLPP
SLASESHHWQ KGVDTMDVWF DSGSSWASVS CQRDELGYPA DLYLEGTDQH RGWFQSSLLT
SVAVNGHAPY KKVLTHGFAL DENGRKMSKS LGNIIDPTVI INGGTNKKTD PAYGADVLRL
WVSSVDYSVD VPIGSNILKQ LSDVYRKVRN TSRYLLGNLH DFDPKKNSVD IDNLPILDKW
MLNRTAEVID EITLAFEKYE FSRFFQLLQS FCTVDLSNFY LDIAKDRLYV SAPDDPRRRA
CQTVMALIIE KLAGLISPVL CHMAEDIWQN IPYQLSEESV FKRGWPVSPS NWKRASLTEP
ISLIRELRTS VNRVLEGCRN RQELGSSLEA GLRLEITNQG LLDAIDFLAK NGDHDVDCIR
DWFLVSQLQI GGEPWAEVLI SQQFELGVIE ISNARGYKCE RCWHYEQDIG SCSEHPTLCG
RCVTVMNRL
