TILS_CHLTE
ID TILS_CHLTE Reviewed; 331 AA.
AC Q8KC15; Q93SU5;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=tRNA(Ile)-lysidine synthase {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}; OrderedLocusNames=CT1614;
OS Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS (Chlorobium tepidum).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX NCBI_TaxID=194439;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10976061; DOI=10.1126/science.289.5485.1724;
RA Xiong J., Fischer W.M., Inoue K., Nakahara M., Bauer C.E.;
RT "Molecular evidence for the early evolution of photosynthesis.";
RL Science 289:1724-1730(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX PubMed=12093901; DOI=10.1073/pnas.132181499;
RA Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.,
RA Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V.,
RA Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M.,
RA White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA Fraser C.M.;
RT "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT anaerobic, green-sulfur bacterium.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
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: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01161}.
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; AY005137; AAG12421.1; -; Genomic_DNA.
DR EMBL; AE006470; AAM72839.1; -; Genomic_DNA.
DR RefSeq; NP_662497.1; NC_002932.3.
DR RefSeq; WP_010933278.1; NC_002932.3.
DR AlphaFoldDB; Q8KC15; -.
DR SMR; Q8KC15; -.
DR STRING; 194439.CT1614; -.
DR EnsemblBacteria; AAM72839; AAM72839; CT1614.
DR KEGG; cte:CT1614; -.
DR PATRIC; fig|194439.7.peg.1459; -.
DR eggNOG; COG0037; Bacteria.
DR HOGENOM; CLU_018869_0_0_10; -.
DR OMA; LEWFLMQ; -.
DR OrthoDB; 666797at2; -.
DR Proteomes; UP000001007; Chromosome.
DR GO; GO:0005737; C:cytoplasm; 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:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
DR CDD; cd01992; PP-ATPase; 1.
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 InterPro; IPR012795; tRNA_Ile_lys_synt_N.
DR PANTHER; PTHR43033; PTHR43033; 1.
DR Pfam; PF01171; ATP_bind_3; 1.
DR TIGRFAMs; TIGR02432; lysidine_TilS_N; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Reference proteome;
KW tRNA processing.
FT CHAIN 1..331
FT /note="tRNA(Ile)-lysidine synthase"
FT /id="PRO_0000181676"
FT BINDING 29..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01161"
SQ SEQUENCE 331 AA; 37135 MW; 47FD34AF980E972D CRC64;
MNKTEKKFLE NMHRQKLVAN GDAVLLAVSG GPDSMALLHL FASVASVLHC RLGVAHCNFM
LRGDASDADE SFVRDACAEL GIDFHVRRFD TASVSSAWKK SIEETARLLR YDFFGELCRE
ASYTRIATGH HSDDNAETVL FNLFRGAGIS GLRGIRVRHG AIIRPLLPFT RREIVAYLEE
KRVVWRDDHT NEGIEYDRNF IRNRVIPVIE ERFAHKLMPS LQRISEHAGE LEEFIDLHIS
RLLEAHPGLD LAGGKLHVGT MRQLSMFERK EILKRALKLQ GLSVGSNVLN RIAGLLDNQA
GRSVPAGAGV EVVLHDGFLR FRQTGNPSDH R
