TILS_CHLVU
ID TILS_CHLVU Reviewed; 504 AA.
AC O20163;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=tRNA(Ile)-lysidine synthase, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01161};
DE EC=6.3.4.19 {ECO:0000255|HAMAP-Rule:MF_01161};
DE AltName: Full=tRNA(Ile)-2-lysyl-cytidine synthase {ECO:0000255|HAMAP-Rule:MF_01161};
DE AltName: Full=tRNA(Ile)-lysidine synthetase {ECO:0000255|HAMAP-Rule:MF_01161};
GN Name=tilS {ECO:0000255|HAMAP-Rule:MF_01161}; Synonyms=ycf62;
OS Chlorella vulgaris (Green alga).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX NCBI_TaxID=3077;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAM C-27 / Tamiya;
RX PubMed=9159184; DOI=10.1073/pnas.94.11.5967;
RA Wakasugi T., Nagai T., Kapoor M., Sugita M., Ito M., Ito S., Tsudzuki J.,
RA Nakashima K., Tsudzuki T., Suzuki Y., Hamada A., Ohta T., Inamura A.,
RA Yoshinaga K., Sugiura M.;
RT "Complete nucleotide sequence of the chloroplast genome from the green alga
RT Chlorella vulgaris: the existence of genes possibly involved in chloroplast
RT division.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:5967-5972(1997).
CC -!- FUNCTION: Ligates lysine onto the cytidine present at position 34 of
CC the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an
CC ATP-dependent manner. Cytidine is converted to lysidine, thus changing
CC the amino acid specificity of the tRNA from methionine to isoleucine.
CC {ECO:0000255|HAMAP-Rule:MF_01161}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP +
CC diphosphate + H(+) + lysidine(34) in tRNA(Ile2);
CC Xref=Rhea:RHEA:43744, Rhea:RHEA-COMP:10625, Rhea:RHEA-COMP:10670,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:82748, ChEBI:CHEBI:83665,
CC ChEBI:CHEBI:456215; EC=6.3.4.19; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01161};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- DOMAIN: The N-terminal region contains the highly conserved SGGXDS
CC motif, predicted to be a P-loop motif involved in ATP binding.
CC -!- SIMILARITY: Belongs to the tRNA(Ile)-lysidine synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_01161}.
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DR EMBL; AB001684; BAA57935.1; -; Genomic_DNA.
DR PIR; T07287; T07287.
DR RefSeq; NP_045859.1; NC_001865.1.
DR AlphaFoldDB; O20163; -.
DR PRIDE; O20163; -.
DR GeneID; 1457443; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProtKB-UniRule.
DR GO; GO:0002097; P:tRNA wobble base modification; IEA:UniProt.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_01161; tRNA_Ile_lys_synt; 1.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR011063; TilS/TtcA_N.
DR InterPro; IPR012094; tRNA_Ile_lys_synt.
DR Pfam; PF01171; ATP_bind_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chloroplast; Ligase; Nucleotide-binding; Plastid;
KW tRNA processing.
FT CHAIN 1..504
FT /note="tRNA(Ile)-lysidine synthase, chloroplastic"
FT /id="PRO_0000181815"
FT BINDING 35..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01161"
SQ SEQUENCE 504 AA; 59973 MW; E2A4FD28192C6AF0 CRC64;
MKKDSTIIST CNEFSLSSVK TKRVYKNNHL LCSVSGGQDS IVSFFFLVNF LYLSKNFKLI
KSKLSSFSVA SKSAEKKRCF DCFFSLKKNK KINALINKEK KLSRLDLVFC QHFWQTQNFF
CVEFLFQLTF FFDIPYTFVL SKNILVSENR ARGWRKKTFS RLLKIQKLST IVTGQTKTDT
AEKSITNLLR GTSPKSFSLI TKANSKTTSS FFCFRLFRPK TFYLTLTGNK RERKVNRRIS
FSFYRTQKKD SKKLRETRAP FFIEMASFSA FFGNTFQKKK SSNSFLLYKT RLSFSFCFSG
ETREHSINSL KPLQNRNRYH ISKLVKFYKF PLTIDATNFS LNFSRNKIRH LFIPFIRFLF
KLKFETLLLN FLYLVNLEHE QIENENLELK RVLNFLRINY LKKNFFSSNR RSFFVIQTGH
KNNNVFPTKK KEKRWFYCNE IGISKIRKQC KIHEDPILET SLVIYFTSVL TTSRKYSLLQ
NLLYNYREIE INFRQISKLE NSFW