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Q8YAC7

- TILS_LISMO

UniProt

Q8YAC7 - TILS_LISMO

Protein

Bifunctional protein TilS/HprT

Gene

tilS/hprT

Organism
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      Previous versions | rss
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    Functioni

    Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine By similarity.By similarity

    Catalytic activityi

    IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate.
    GMP + diphosphate = guanine + 5-phospho-alpha-D-ribose 1-diphosphate.
    (tRNA(Ile2))-cytidine(34) + L-lysine + ATP = (tRNA(Ile2))-lysidine(34) + AMP + diphosphate + H2O.

    Cofactori

    Binds 2 magnesium ions per subunit. One of the ions does not make direct protein contacts By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi627 – 6271Magnesium 1By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi29 – 346ATPSequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-HAMAP
    2. guanine phosphoribosyltransferase activity Source: UniProtKB-EC
    3. hypoxanthine phosphoribosyltransferase activity Source: UniProtKB-EC
    4. ligase activity, forming carbon-nitrogen bonds Source: UniProtKB-HAMAP
    5. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. purine ribonucleoside salvage Source: InterPro
    2. tRNA modification Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Glycosyltransferase, Ligase, Transferase

    Keywords - Biological processi

    tRNA processing

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciLMON169963:LMO0219-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional protein TilS/HprT
    Including the following 2 domains:
    tRNA(Ile)-lysidine synthase (EC:6.3.4.19)
    Alternative name(s):
    tRNA(Ile)-2-lysyl-cytidine synthase
    tRNA(Ile)-lysidine synthetase
    Hypoxanthine-guanine phosphoribosyltransferase (EC:2.4.2.8)
    Short name:
    HGPRT
    Short name:
    HGPRTase
    Gene namesi
    Name:tilS/hprT
    Ordered Locus Names:lmo0219
    OrganismiListeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
    Taxonomic identifieri169963 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria
    ProteomesiUP000000817: Chromosome

    Organism-specific databases

    GenoListiLMO0219.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 648648Bifunctional protein TilS/HprTPRO_0000181718Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi169963.lmo0219.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8YAC7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domaini

    The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.

    Sequence similaritiesi

    In the N-terminal section; belongs to the tRNA(Ile)-lysidine synthase family.Curated
    In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.Curated

    Phylogenomic databases

    eggNOGiCOG0634.
    HOGENOMiHOG000217053.
    KOiK15780.
    OMAiNDISYPL.
    OrthoDBiEOG693GNP.
    PhylomeDBiQ8YAC7.

    Family and domain databases

    Gene3Di3.40.50.2020. 1 hit.
    3.40.50.620. 1 hit.
    HAMAPiMF_01161. tRNA_Ile_lys_synt.
    InterProiIPR005904. Hxn_phspho_trans.
    IPR012094. Lysidine-tRNA-synth.
    IPR012796. Lysidine-tRNA-synth_C.
    IPR012795. Lysidine-tRNA-synth_N.
    IPR020825. Phe-tRNA_synthase_B3/B4.
    IPR000836. PRibTrfase_dom.
    IPR029057. PRTase-like.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR011063. tRNA-lysidine/thiocyt_synth.
    [Graphical view]
    PANTHERiPTHR11807:SF2. PTHR11807:SF2. 1 hit.
    PfamiPF01171. ATP_bind_3. 1 hit.
    PF00156. Pribosyltran. 1 hit.
    PF11734. TilS_C. 1 hit.
    [Graphical view]
    SMARTiSM00977. TilS_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF53271. SSF53271. 1 hit.
    SSF56037. SSF56037. 1 hit.
    TIGRFAMsiTIGR01203. HGPRTase. 1 hit.
    TIGR02433. lysidine_TilS_C. 1 hit.
    TIGR02432. lysidine_TilS_N. 1 hit.
    PROSITEiPS00103. PUR_PYR_PR_TRANSFER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8YAC7-1 [UniParc]FASTAAdd to Basket

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    MDDTEKRVHK YIEKHDLIRS DDKLLVAVSG GPDSLALLHF LWNSNLVPKE    50
    AISVAHLNHQ LRENAAKEQR VVETFCERQG IPFYIEEVDI KSRAQSLQKG 100
    LEETARIVRY DFFEKVMAEK NINKLVLAHH ADDQIETILM RLVRGSASIG 150
    WSGIQPKREL KGGQAIRPFL PITKAEIIDY AQKHELAYEI DESNTSQEYT 200
    RNRYRAQLLP FLKQENPAVY SHFERFSEET SEDFQFLEAL ASDLLKKNLI 250
    KNGKQTTLLL SSFKNEANPL QRRAIHLLLR YLYNEDASFI TVNHIYQIIQ 300
    MIQSDNPSSS IDLPNKLIAN RAYDKLHFQF GEREAPSEFY HQLELNDRIE 350
    LDNKASIRLK LKSSVVQTNG LNGMLLDAEE ITLPLIVRNR VNGDRMTMKG 400
    QAGSKKLKDI FIDAKIPRQE RDKLPVITDY TGKILWVPGV KKSAYDREFS 450
    RSKKQYIIRY TRNIGGNESM HNDIQKVLIS EDELQEKIRE LGRELTTEYE 500
    GRNPLVVGVL KGATPFMTDL LKRVDTYLEM DFMDVSSYGN GTVSSGEVKI 550
    IKDLNASVEG RDVLVIEDII DSGRTLSYLV DLIKYRKAKS VKLVTLLDKP 600
    AGRNVEIEAD YVGFVVPNEF VVGYGLDYAE RYRNLPYIGI LKPEIYSE 648
    Length:648
    Mass (Da):74,368
    Last modified:March 1, 2002 - v1
    Checksum:iDACEA788D7AD5F77
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti5 – 51E → D in AAM74001. 1 PublicationCurated
    Sequence conflicti57 – 571L → I in AAM74001. 1 PublicationCurated
    Sequence conflicti60 – 601Q → H in AAM74001. 1 PublicationCurated
    Sequence conflicti67 – 671K → N in AAM74001. 1 PublicationCurated
    Sequence conflicti70 – 701R → N in AAM74001. 1 PublicationCurated
    Sequence conflicti74 – 741T → A in AAM74001. 1 PublicationCurated
    Sequence conflicti78 – 781R → S in AAM74001. 1 PublicationCurated
    Sequence conflicti90 – 901I → V in AAM74001. 1 PublicationCurated
    Sequence conflicti95 – 951Q → E in AAM74001. 1 PublicationCurated
    Sequence conflicti101 – 1011L → I in AAM74001. 1 PublicationCurated
    Sequence conflicti121 – 1211N → K in AAM74001. 1 PublicationCurated
    Sequence conflicti126 – 1261V → A in AAM74001. 1 PublicationCurated
    Sequence conflicti255 – 2551Q → R in AAM74001. 1 PublicationCurated
    Sequence conflicti261 – 2622SS → TN in AAM74001. 1 PublicationCurated
    Sequence conflicti318 – 3181I → V in AAM74001. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL591974 Genomic DNA. Translation: CAD00746.1.
    AF467001 Genomic DNA. Translation: AAM74001.1.
    PIRiAD1102.
    RefSeqiNP_463750.1. NC_003210.1.

    Genome annotation databases

    EnsemblBacteriaiCAD00746; CAD00746; CAD00746.
    GeneIDi987055.
    KEGGilmo:lmo0219.
    PATRICi20309445. VBILisMon69206_0224.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL591974 Genomic DNA. Translation: CAD00746.1 .
    AF467001 Genomic DNA. Translation: AAM74001.1 .
    PIRi AD1102.
    RefSeqi NP_463750.1. NC_003210.1.

    3D structure databases

    ProteinModelPortali Q8YAC7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 169963.lmo0219.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAD00746 ; CAD00746 ; CAD00746 .
    GeneIDi 987055.
    KEGGi lmo:lmo0219.
    PATRICi 20309445. VBILisMon69206_0224.

    Organism-specific databases

    GenoListi LMO0219.

    Phylogenomic databases

    eggNOGi COG0634.
    HOGENOMi HOG000217053.
    KOi K15780.
    OMAi NDISYPL.
    OrthoDBi EOG693GNP.
    PhylomeDBi Q8YAC7.

    Enzyme and pathway databases

    BioCyci LMON169963:LMO0219-MONOMER.

    Family and domain databases

    Gene3Di 3.40.50.2020. 1 hit.
    3.40.50.620. 1 hit.
    HAMAPi MF_01161. tRNA_Ile_lys_synt.
    InterProi IPR005904. Hxn_phspho_trans.
    IPR012094. Lysidine-tRNA-synth.
    IPR012796. Lysidine-tRNA-synth_C.
    IPR012795. Lysidine-tRNA-synth_N.
    IPR020825. Phe-tRNA_synthase_B3/B4.
    IPR000836. PRibTrfase_dom.
    IPR029057. PRTase-like.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR011063. tRNA-lysidine/thiocyt_synth.
    [Graphical view ]
    PANTHERi PTHR11807:SF2. PTHR11807:SF2. 1 hit.
    Pfami PF01171. ATP_bind_3. 1 hit.
    PF00156. Pribosyltran. 1 hit.
    PF11734. TilS_C. 1 hit.
    [Graphical view ]
    SMARTi SM00977. TilS_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53271. SSF53271. 1 hit.
    SSF56037. SSF56037. 1 hit.
    TIGRFAMsi TIGR01203. HGPRTase. 1 hit.
    TIGR02433. lysidine_TilS_C. 1 hit.
    TIGR02432. lysidine_TilS_N. 1 hit.
    PROSITEi PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-679 / EGD-e.
    2. Li G., Kathariou S.
      Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 4b1.

    Entry informationi

    Entry nameiTILS_LISMO
    AccessioniPrimary (citable) accession number: Q8YAC7
    Secondary accession number(s): Q8KU03
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2005
    Last sequence update: March 1, 2002
    Last modified: October 1, 2014
    This is version 85 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3