TILS_GLUOX
ID TILS_GLUOX Reviewed; 398 AA.
AC Q5FQB6;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=GOX1690;
OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=290633;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=621H;
RX PubMed=15665824; DOI=10.1038/nbt1062;
RA Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT oxydans.";
RL Nat. Biotechnol. 23:195-200(2005).
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; CP000009; AAW61430.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5FQB6; -.
DR SMR; Q5FQB6; -.
DR STRING; 290633.GOX1690; -.
DR EnsemblBacteria; AAW61430; AAW61430; GOX1690.
DR KEGG; gox:GOX1690; -.
DR eggNOG; COG0037; Bacteria.
DR HOGENOM; CLU_018869_3_2_5; -.
DR OMA; TFLMRLA; -.
DR Proteomes; UP000006375; 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..398
FT /note="tRNA(Ile)-lysidine synthase"
FT /id="PRO_0000181699"
FT BINDING 21..26
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01161"
SQ SEQUENCE 398 AA; 43874 MW; 3F2DC7AA741D30B4 CRC64;
MARFGPWPPD IDDAPVGLAV SGGADSMALA FLARRWRRNV VAFVVDHALR PESAAEAQLT
VHRLAGMNVK ARLLTLAPFP KGRMQERARH ARFEALEAAC VSEGCLDLLV AHHAGDQDET
VWMRHLHASG PLGLSGIQPV SVRGRIRLVR PLLTFPTARL RLTLQAENLP WIEDPSNANR
RFERVRLRQD LTPEQRQEAR VLQQDALQER LRLEAELAEE LGRHAVWYSQ GWVFLGQEGV
DEEALSVLIR LVSGSAYRPA REAVRTLMTQ GYGTLSGVQV RPAGRFGNGI ILVREERALG
PFVPAKAGAV WDGRWRLLAC DVPQGSLIGS LGDAIHVMDL RRLGVPYAAA RCLPGVWHEG
RLVLGPRLGE RAWGEFAGEA DFVWSSGVPA TGENHFGT