TILS_AQUAE
ID TILS_AQUAE Reviewed; 317 AA.
AC O67728;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
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=aq_1887;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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; AE000657; AAC07685.1; -; Genomic_DNA.
DR PIR; F70462; F70462.
DR RefSeq; NP_214296.1; NC_000918.1.
DR RefSeq; WP_010881232.1; NC_000918.1.
DR PDB; 1WY5; X-ray; 2.42 A; A/B=1-317.
DR PDB; 2E21; X-ray; 2.70 A; A/B/C/D=1-317.
DR PDB; 2E89; X-ray; 2.50 A; A/B/C/D=1-317.
DR PDBsum; 1WY5; -.
DR PDBsum; 2E21; -.
DR PDBsum; 2E89; -.
DR AlphaFoldDB; O67728; -.
DR SMR; O67728; -.
DR DIP; DIP-29530N; -.
DR STRING; 224324.aq_1887; -.
DR EnsemblBacteria; AAC07685; AAC07685; aq_1887.
DR KEGG; aae:aq_1887; -.
DR PATRIC; fig|224324.8.peg.1462; -.
DR eggNOG; COG0037; Bacteria.
DR HOGENOM; CLU_018869_0_0_0; -.
DR InParanoid; O67728; -.
DR OMA; CDPARRI; -.
DR OrthoDB; 666797at2; -.
DR BRENDA; 6.3.4.19; 396.
DR EvolutionaryTrace; O67728; -.
DR Proteomes; UP000000798; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Ligase; Nucleotide-binding;
KW Reference proteome; tRNA processing.
FT CHAIN 1..317
FT /note="tRNA(Ile)-lysidine synthase"
FT /id="PRO_0000181639"
FT BINDING 32..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01161"
FT HELIX 3..18
FT /evidence="ECO:0007829|PDB:1WY5"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:1WY5"
FT HELIX 35..46
FT /evidence="ECO:0007829|PDB:1WY5"
FT TURN 48..52
FT /evidence="ECO:0007829|PDB:1WY5"
FT STRAND 54..62
FT /evidence="ECO:0007829|PDB:1WY5"
FT HELIX 68..83
FT /evidence="ECO:0007829|PDB:1WY5"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:1WY5"
FT HELIX 94..100
FT /evidence="ECO:0007829|PDB:1WY5"
FT HELIX 105..123
FT /evidence="ECO:0007829|PDB:1WY5"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:1WY5"
FT HELIX 135..148
FT /evidence="ECO:0007829|PDB:1WY5"
FT HELIX 152..156
FT /evidence="ECO:0007829|PDB:1WY5"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:1WY5"
FT TURN 168..171
FT /evidence="ECO:0007829|PDB:1WY5"
FT HELIX 174..183
FT /evidence="ECO:0007829|PDB:1WY5"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:1WY5"
FT HELIX 199..206
FT /evidence="ECO:0007829|PDB:1WY5"
FT HELIX 208..215
FT /evidence="ECO:0007829|PDB:1WY5"
FT HELIX 219..248
FT /evidence="ECO:0007829|PDB:1WY5"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:2E89"
FT HELIX 256..259
FT /evidence="ECO:0007829|PDB:1WY5"
FT HELIX 264..275
FT /evidence="ECO:0007829|PDB:1WY5"
FT HELIX 280..287
FT /evidence="ECO:0007829|PDB:1WY5"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:1WY5"
FT STRAND 295..305
FT /evidence="ECO:0007829|PDB:1WY5"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:1WY5"
SQ SEQUENCE 317 AA; 37320 MW; 78D8C6229152A296 CRC64;
MNPESRVIRK VLALQNDEKI FSGERRVLIA FSGGVDSVVL TDVLLKLKNY FSLKEVALAH
FNHMLRESAE RDEEFCKEFA KERNMKIFVG KEDVRAFAKE NRMSLEEAGR FLRYKFLKEI
LESEGFDCIA TAHHLNDLLE TSLLFFTRGT GLDGLIGFLP KEEVIRRPLY YVKRSEIEEY
AKFKGLRWVE DETNYEVSIP RNRIRHRVIP ELKRINENLE DTFLKMVKVL RAEREFLEEE
AQKLYKEVKK GNCLDVKKLK EKPLALQRRV IRKFIGEKDY EKVELVRSLL EKGGEVNLGK
GKVLKRKERW LCFSPEV
