SYI_PROM5
ID SYI_PROM5 Reviewed; 965 AA.
AC A2BUL8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=P9515_02701;
OS Prochlorococcus marinus (strain MIT 9515).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167542;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9515;
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; CP000552; ABM71479.1; -; Genomic_DNA.
DR RefSeq; WP_011819591.1; NC_008817.1.
DR AlphaFoldDB; A2BUL8; -.
DR SMR; A2BUL8; -.
DR STRING; 167542.P9515_02701; -.
DR EnsemblBacteria; ABM71479; ABM71479; P9515_02701.
DR KEGG; pmc:P9515_02701; -.
DR eggNOG; COG0060; Bacteria.
DR HOGENOM; CLU_001493_7_0_3; -.
DR OMA; HLGTAWN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000001589; 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 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; Zinc.
FT CHAIN 1..965
FT /note="Isoleucine--tRNA ligase"
FT /id="PRO_1000022099"
FT MOTIF 68..78
FT /note="'HIGH' region"
FT MOTIF 623..627
FT /note="'KMSKS' region"
FT BINDING 582
FT /ligand="L-isoleucyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:178002"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 626
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 936
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
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 956
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"
SQ SEQUENCE 965 AA; 111215 MW; 4280F03BCF3C776D CRC64;
MKPKNNKDKK SKFSYKETLN LLKTDFSMRA NSVSREPQIQ EFWLKNKIDL ELGSSNLGEK
FTLHDGPPYA NGSLHMGHAL NKVLKDIINK YKTLKGFKVH FVPGWDCHGL PIELKVLQSL
KSHERKDLDS LGLRKKATDY AKIQIKNQLE GFKRWGIWGD WDNPYLTLKN NYESAQIGVF
GKMFLNGYIY RGLKPVHWSP SSRTALAEAE LEYPEEHYSS SVYVSLNISN LSDEILLKLE
EKDLKNKLLS NLNKLFIAIW TTTPWTIPGN EAVAINPRIN YVFAEDQNGD IFLFAKDLIS
EISEKLEREF NTLIDVKGSM LTGIEYKHPT KNKFCNIVIG GDYITTESGT GIVHTAPGHG
MDDFNVGKKY HLPITCIVDE KGNLNNHAEK FCGLNVLKDA NDLIIEDLKK NNLLLLKEKY
KHRYPYDWRT KKPTIFRATE QWFASVEGFR SSALKAIEDV EWMPKTGKKR IYSMVVGRGD
WCISRQRSWG VPIPVFYEKK GKEILLNSET INHIQKLFNE HGADIWWDWD EKDLLPKQYK
EESDRWIKGL DTMDVWFDSG SSWAAVCEQR EELAYPADLY LEGSDQHRGW FQSSLLTSVA
VNNKPPYKKV LTHGFALDEN GRKMSKSLGN VVDPNIIING GSNQKIQPAY GADVLRLWVS
SVDYSVDVPI GSNILKQLSD VYRKVRNTAR YLLGNIHDYD PIDEEIDIDQ LPILDQWMLN
RLVDVSDQIT IAYENYEFSK FFQILQSFCV VDLSNFYLDI AKDRLYVSAK SSIRRRTCQF
VMSKIVENLA VLISPVLCHM AEDIWQNIPY STNEKSVFER GWPNLPKSWI NPELNERISN
LRKLRVEINK AIEGCRTQQI IGAALETEVN YLPENEIIKN SLSWLEKFGN KEVDLYSDWL
IVSKFNVVNN LFEDYLIIDD NELGKIQILK AKGQKCDRCW HYQSNTVMGI EDTKLCKRCA
NIITS
