TILS_LISIN
ID TILS_LISIN Reviewed; 648 AA.
AC Q92F56;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=lin0251;
OS Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=272626;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-680 / CLIP 11262;
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).
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; AL596164; CAC95484.1; -; Genomic_DNA.
DR PIR; AD1464; AD1464.
DR RefSeq; WP_010990297.1; NC_003212.1.
DR AlphaFoldDB; Q92F56; -.
DR SMR; Q92F56; -.
DR STRING; 272626.lin0251; -.
DR EnsemblBacteria; CAC95484; CAC95484; CAC95484.
DR KEGG; lin:lin0251; -.
DR eggNOG; COG0037; Bacteria.
DR eggNOG; COG0634; Bacteria.
DR HOGENOM; CLU_018869_0_1_9; -.
DR OMA; QQYGMNA; -.
DR OrthoDB; 666797at2; -.
DR Proteomes; UP000002513; 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; Transferase; tRNA processing.
FT CHAIN 1..648
FT /note="Bifunctional protein TilS/HprT"
FT /id="PRO_0000181716"
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; 74527 MW; 796860D8E403E0CD CRC64;
MDDTKKRIHK YIEKHDLIRS DDKLLVAVSG GPDSFALLHF LWSANLVPKE AIAVAHLNHH
LRENAEKEQL AVQTFCEERD IPFFIEEVDV KKRAEKLQKG IEETARIVRY DFFEKVMAEN
NINKLVLAHH ADDQIETILM RLVRGSSSIG WSGIQPKREV RGGYAIRPFL PITKAEIIEY
ATKHALPYEI DESNTSQEYT RNRYRTQLLP FLSKENPAVY EHFKRFSEET SEDFQFLEEL
ASNLLKKNLI QNGKQSTLLL SDFKNEANPL QRRAIHLLLM YLYNDDGRVI TVNHIYQIIQ
MIQSENPSSS IDLPKKLTVI RSYNELHFQF GERHAPPEFY HQLELNDRIE LDNKASIRLK
LKSSVVQTNG LNGMLLDAED ITLPLIVRNR VNGDRMTMKG QAGSKKLKDI FIDAKIPRQE
RDNLPVITDY TGKILWVPGV KKSAYDREFS RSKKQYIIRY TRNIGGNESM HNDIQKVLIS
EDELQEKIRE LGRELTAEYE GRNPLVVGVL KGATPFMTDL LKRIDTYLEM DFMDVSSYGN
GTVSSGEVKI IKDLNASVEG RDVLIIEDII DSGRTLSYLV DLIKYRKAKS VKLVTLLDKP
AGRNVAIEAD YVGFVVPNEF VVGYGLDYAE RYRNLPYIGI LKPEIYSE
