TILS_LISMO
ID TILS_LISMO Reviewed; 648 AA.
AC Q8YAC7; Q8KU03;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=lmo0219;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=4b1;
RA Li G., Kathariou S.;
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; AL591974; CAD00746.1; -; Genomic_DNA.
DR EMBL; AF467001; AAM74001.1; -; Genomic_DNA.
DR PIR; AD1102; AD1102.
DR RefSeq; NP_463750.1; NC_003210.1.
DR RefSeq; WP_003723741.1; NZ_CP023861.1.
DR AlphaFoldDB; Q8YAC7; -.
DR SMR; Q8YAC7; -.
DR STRING; 169963.lmo0219; -.
DR PaxDb; Q8YAC7; -.
DR EnsemblBacteria; CAD00746; CAD00746; CAD00746.
DR GeneID; 987055; -.
DR KEGG; lmo:lmo0219; -.
DR PATRIC; fig|169963.11.peg.224; -.
DR eggNOG; COG0037; Bacteria.
DR eggNOG; COG0634; Bacteria.
DR HOGENOM; CLU_018869_0_1_9; -.
DR OMA; QQYGMNA; -.
DR PhylomeDB; Q8YAC7; -.
DR BioCyc; LMON169963:LMO0219-MON; -.
DR Proteomes; UP000000817; Chromosome.
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; Reference proteome; Transferase;
KW tRNA processing.
FT CHAIN 1..648
FT /note="Bifunctional protein TilS/HprT"
FT /id="PRO_0000181718"
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"
FT CONFLICT 5
FT /note="E -> D (in Ref. 2; AAM74001)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="L -> I (in Ref. 2; AAM74001)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="Q -> H (in Ref. 2; AAM74001)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="K -> N (in Ref. 2; AAM74001)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="R -> N (in Ref. 2; AAM74001)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="T -> A (in Ref. 2; AAM74001)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="R -> S (in Ref. 2; AAM74001)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="I -> V (in Ref. 2; AAM74001)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="Q -> E (in Ref. 2; AAM74001)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="L -> I (in Ref. 2; AAM74001)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="N -> K (in Ref. 2; AAM74001)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="V -> A (in Ref. 2; AAM74001)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="Q -> R (in Ref. 2; AAM74001)"
FT /evidence="ECO:0000305"
FT CONFLICT 261..262
FT /note="SS -> TN (in Ref. 2; AAM74001)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="I -> V (in Ref. 2; AAM74001)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 648 AA; 74368 MW; DACEA788D7AD5F77 CRC64;
MDDTEKRVHK YIEKHDLIRS DDKLLVAVSG GPDSLALLHF LWNSNLVPKE AISVAHLNHQ
LRENAAKEQR VVETFCERQG IPFYIEEVDI KSRAQSLQKG LEETARIVRY DFFEKVMAEK
NINKLVLAHH ADDQIETILM RLVRGSASIG WSGIQPKREL KGGQAIRPFL PITKAEIIDY
AQKHELAYEI DESNTSQEYT RNRYRAQLLP FLKQENPAVY SHFERFSEET SEDFQFLEAL
ASDLLKKNLI KNGKQTTLLL SSFKNEANPL QRRAIHLLLR YLYNEDASFI TVNHIYQIIQ
MIQSDNPSSS IDLPNKLIAN 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
