TILS_LISMF
ID TILS_LISMF Reviewed; 648 AA.
AC Q724J4;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Bifunctional protein TilS/HprT;
DE Includes:
DE RecName: Full=tRNA(Ile)-lysidine synthase;
DE EC=6.3.4.19;
DE AltName: Full=tRNA(Ile)-2-lysyl-cytidine synthase;
DE AltName: Full=tRNA(Ile)-lysidine synthetase;
DE Includes:
DE RecName: Full=Hypoxanthine-guanine phosphoribosyltransferase;
DE Short=HGPRT;
DE Short=HGPRTase;
DE EC=2.4.2.8;
GN Name=tilS/hprT; OrderedLocusNames=LMOf2365_0230;
OS Listeria monocytogenes serotype 4b (strain F2365).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=265669;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F2365;
RX PubMed=15115801; DOI=10.1093/nar/gkh562;
RA Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F.,
RA Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D.,
RA White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M.,
RA Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Haft D.H.,
RA Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A.,
RA Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O.,
RA Luchansky J.B., Fraser C.M.;
RT "Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne
RT pathogen Listeria monocytogenes reveal new insights into the core genome
RT components of this species.";
RL Nucleic Acids Res. 32:2386-2395(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 (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + IMP = 5-phospho-alpha-D-ribose 1-diphosphate +
CC hypoxanthine; Xref=Rhea:RHEA:17973, ChEBI:CHEBI:17368,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58053; EC=2.4.2.8;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + GMP = 5-phospho-alpha-D-ribose 1-diphosphate +
CC guanine; Xref=Rhea:RHEA:25424, ChEBI:CHEBI:16235, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58017, ChEBI:CHEBI:58115; EC=2.4.2.8;
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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. One of the ions does not make
CC direct protein contacts. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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: In the N-terminal section; belongs to the tRNA(Ile)-
CC lysidine synthase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine
CC phosphoribosyltransferase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE017262; AAT03017.1; -; Genomic_DNA.
DR RefSeq; WP_010958692.1; NC_002973.6.
DR AlphaFoldDB; Q724J4; -.
DR SMR; Q724J4; -.
DR KEGG; lmf:LMOf2365_0230; -.
DR HOGENOM; CLU_018869_0_1_9; -.
DR OMA; QQYGMNA; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0052657; F:guanine phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004422; F:hypoxanthine phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:InterPro.
DR GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
DR CDD; cd01992; PP-ATPase; 1.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_01161; tRNA_Ile_lys_synt; 1.
DR InterPro; IPR005904; Hxn_phspho_trans.
DR InterPro; IPR012796; Lysidine-tRNA-synth_C.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
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 Pfam; PF00156; Pribosyltran; 1.
DR Pfam; PF11734; TilS_C; 1.
DR SMART; SM00977; TilS_C; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR01203; HGPRTase; 1.
DR TIGRFAMs; TIGR02433; lysidine_TilS_C; 1.
DR TIGRFAMs; TIGR02432; lysidine_TilS_N; 1.
DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Glycosyltransferase; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Transferase; tRNA processing.
FT CHAIN 1..648
FT /note="Bifunctional protein TilS/HprT"
FT /id="PRO_0000181717"
FT BINDING 29..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 627
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 648 AA; 74266 MW; E181EE42A0D39129 CRC64;
MDDTDKRVHK YIEKHDLIRS DDKLLVAVSG GPDSLALLHF LWNSNLVPKE AISVAHLNHH
LRENAANEQN VVETFCESQG IPFYIEEVDV KSRAESLQKG IEETARIVRY DFFEKVMAEK
KINKLALAHH ADDQIETILM RLVRGSASIG WSGIQPKREL KGGQAIRPFL PITKAEIIDY
AQKHELAYEI DESNTSQEYT RNRYRAQLLP FLKQENPAVY SHFERFSEET SEDFQFLEAL
ASDLLKKNLI KNGKRTTLLL TNFKNEANPL QRRAIHLLLR YLYNEDASFI TVNHIYQIIQ
MIQSDNPSSS IDLPNKLVAN RAYDKLHFQF GEREAPSEFY HQLELNDRIE LDNKASIRLK
LKSSVVQTNG LNGMLLDAEE ITLPLIVRNR VNGDRMTMKG QAGSKKLKDI FIDAKIPRQE
RDKLPVITDY TGKILWVPGV KKSAYDREFS RSKKQYIIRY TRNIGGNESM HNDIQKVLIS
EDELQEKIRE LGRELTTEYE GRNPLVVGVL KGATPFMTDL LKRVDTYLEM DFMDVSSYGN
GTVSSGEVKI IKDLNASVEG RDVLVIEDII DSGRTLSYLV DLIKYRKAKS VKLVTLLDKP
AGRNVEIEAD YVGFVVPNEF VVGYGLDYAE RYRNLPYIGI LKPEIYSE
