TILS_GEOKA
ID TILS_GEOKA Reviewed; 464 AA.
AC Q5L3T3;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=GK0060;
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426;
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(2004).
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; BA000043; BAD74345.1; -; Genomic_DNA.
DR RefSeq; WP_011229575.1; NC_006510.1.
DR PDB; 3A2K; X-ray; 3.65 A; A/B=1-464.
DR PDB; 3HJ7; X-ray; 2.20 A; A=332-464.
DR PDBsum; 3A2K; -.
DR PDBsum; 3HJ7; -.
DR AlphaFoldDB; Q5L3T3; -.
DR SMR; Q5L3T3; -.
DR DIP; DIP-59287N; -.
DR STRING; 235909.GK0060; -.
DR EnsemblBacteria; BAD74345; BAD74345; GK0060.
DR KEGG; gka:GK0060; -.
DR eggNOG; COG0037; Bacteria.
DR HOGENOM; CLU_018869_0_1_9; -.
DR OMA; QQYGMNA; -.
DR BRENDA; 6.3.4.19; 8138.
DR EvolutionaryTrace; Q5L3T3; -.
DR Proteomes; UP000001172; 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; IPR012796; Lysidine-tRNA-synth_C.
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 InterPro; IPR015262; tRNA_Ile_lys_synt_subst-bd.
DR PANTHER; PTHR43033; PTHR43033; 2.
DR Pfam; PF01171; ATP_bind_3; 1.
DR Pfam; PF09179; TilS; 1.
DR Pfam; PF11734; TilS_C; 1.
DR SMART; SM00977; TilS_C; 1.
DR TIGRFAMs; TIGR02433; lysidine_TilS_C; 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..464
FT /note="tRNA(Ile)-lysidine synthase"
FT /id="PRO_0000181696"
FT BINDING 26..31
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01161"
FT STRAND 338..341
FT /evidence="ECO:0007829|PDB:3HJ7"
FT STRAND 343..348
FT /evidence="ECO:0007829|PDB:3HJ7"
FT STRAND 352..362
FT /evidence="ECO:0007829|PDB:3HJ7"
FT STRAND 372..375
FT /evidence="ECO:0007829|PDB:3HJ7"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:3HJ7"
FT STRAND 382..387
FT /evidence="ECO:0007829|PDB:3HJ7"
FT STRAND 394..398
FT /evidence="ECO:0007829|PDB:3HJ7"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:3HJ7"
FT HELIX 406..412
FT /evidence="ECO:0007829|PDB:3HJ7"
FT HELIX 417..420
FT /evidence="ECO:0007829|PDB:3HJ7"
FT STRAND 425..427
FT /evidence="ECO:0007829|PDB:3HJ7"
FT STRAND 433..436
FT /evidence="ECO:0007829|PDB:3HJ7"
FT TURN 437..439
FT /evidence="ECO:0007829|PDB:3HJ7"
FT STRAND 440..442
FT /evidence="ECO:0007829|PDB:3HJ7"
FT STRAND 454..462
FT /evidence="ECO:0007829|PDB:3HJ7"
SQ SEQUENCE 464 AA; 53105 MW; 6C81D0B26D2FFCFD CRC64;
MIDKVRAFIH RHQLLSEGAA VIVGVSGGPD SLALLHVFLS LRDEWKLQVI AAHVDHMFRG
RESEEEMEFV KRFCVERRIL CETAQIDVPA FQRSAGLGAQ EAARICRYRF FAELMEKHQA
GYVAVGHHGD DQVETILMRL VRGSTSKGYA GIPVKRPFHG GYLIRPFLAV SRAEIEAYCR
QMGLSPRCDP SNEKDDYTRN RFRHHIVPLL RQENPRLHER FQQYSEMMAE DEQFLEELAA
DALNKVMEKQ HRDAALSIGP FLELPRPLQR RVLQLLLLRL YGGVPPTLTS VHIGHILMLC
ERGRPSGMID LPKGLKVIRS YDRCLFTFDA ESGEKGYWFE LPVPALLPLP NGYAIISEFG
EHYPRKQAGN DWFVVDPASV SLPLRVRTRR RGDRMVLKGT GGTKKLKEIF IEAKIPRMER
DRWPIVEDAD GRILWVPGLK KSAFEAQNRG QARYILLQYQ AMNS
