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Protein

Thiamine-monophosphate kinase

Gene

thiL

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1. Cannot use thiamine as substrate. Is highly specific for ATP as phosphate donor.2 Publications

Miscellaneous

Reaction mechanism of ThiL seems to utilize a direct, inline transfer of the gamma-phosphate of ATP to TMP rather than a phosphorylated enzyme intermediate.By similarity

Catalytic activityi

ATP + thiamine phosphate = ADP + thiamine diphosphate.1 Publication

Enzyme regulationi

Is markedly activated by the monovalent cations K+, NH4+, and Rb+. Is significantly inhibited by ADP, AMP, p-chloromercuribenzoate, N-ethylmaleimide, pyrophosphate, and EDTA.1 Publication

Kineticsi

  1. KM=1.1 µM for thiamine-monophosphate1 Publication
  2. KM=270 µM for ATP1 Publication

    pH dependencei

    Optimum pH is about 8.0.1 Publication

    Pathwayi: thiamine diphosphate biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes thiamine diphosphate from thiamine phosphate.
    Proteins known to be involved in this subpathway in this organism are:
    1. Thiamine-monophosphate kinase (thiL)
    This subpathway is part of the pathway thiamine diphosphate biosynthesis, which is itself part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes thiamine diphosphate from thiamine phosphate, the pathway thiamine diphosphate biosynthesis and in Cofactor biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi30Magnesium 3By similarity1
    Metal bindingi30Magnesium 4; via carbonyl oxygenBy similarity1
    Metal bindingi45Magnesium 4By similarity1
    Metal bindingi46Magnesium 1; via carbonyl oxygenBy similarity1
    Metal bindingi47Magnesium 1By similarity1
    Metal bindingi47Magnesium 2By similarity1
    Binding sitei54SubstrateBy similarity1
    Metal bindingi75Magnesium 2By similarity1
    Metal bindingi75Magnesium 3By similarity1
    Metal bindingi75Magnesium 4By similarity1
    Metal bindingi122Magnesium 1By similarity1
    Binding sitei146ATPBy similarity1
    Metal bindingi212Magnesium 3By similarity1
    Binding sitei214ATPBy similarity1
    Metal bindingi215Magnesium 5By similarity1
    Binding sitei263SubstrateBy similarity1
    Binding sitei319SubstrateBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi121 – 122ATPBy similarity2

    GO - Molecular functioni

    • ATP binding Source: EcoCyc
    • magnesium ion binding Source: EcoCyc
    • metal ion binding Source: EcoCyc
    • thiamine-phosphate kinase activity Source: UniProtKB

    GO - Biological processi

    • thiamine biosynthetic process Source: EcoCyc
    • thiamine diphosphate biosynthetic process Source: UniProtKB

    Keywordsi

    Molecular functionKinase, Transferase
    Biological processThiamine biosynthesis
    LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:THI-P-KIN-MONOMER
    MetaCyc:THI-P-KIN-MONOMER
    UniPathwayiUPA00060; UER00142

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thiamine-monophosphate kinase (EC:2.7.4.16)
    Short name:
    TMP kinase
    Short name:
    Thiamine-phosphate kinase
    Gene namesi
    Name:thiL
    Ordered Locus Names:b0417, JW0407
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG20227 thiL

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000961941 – 325Thiamine-monophosphate kinaseAdd BLAST325

    Proteomic databases

    PaxDbiP0AGG0
    PRIDEiP0AGG0

    Interactioni

    Protein-protein interaction databases

    BioGridi4259339, 26 interactors
    IntActiP0AGG0, 15 interactors
    STRINGi316385.ECDH10B_0373

    Structurei

    3D structure databases

    ProteinModelPortaliP0AGG0
    SMRiP0AGG0
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105CG2 Bacteria
    COG0611 LUCA
    HOGENOMiHOG000228429
    InParanoidiP0AGG0
    KOiK00946
    OMAiHFRRDWS
    PhylomeDBiP0AGG0

    Family and domain databases

    CDDicd02194 ThiL, 1 hit
    Gene3Di3.30.1330.10, 1 hit
    3.90.650.10, 1 hit
    HAMAPiMF_02128 TMP_kinase, 1 hit
    InterProiView protein in InterPro
    IPR010918 PurM-like_C_dom
    IPR036676 PurM-like_C_sf
    IPR016188 PurM-like_N
    IPR036921 PurM-like_N_sf
    IPR006283 ThiL
    PANTHERiPTHR30270 PTHR30270, 1 hit
    PfamiView protein in Pfam
    PF00586 AIRS, 1 hit
    PF02769 AIRS_C, 1 hit
    PIRSFiPIRSF005303 Thiam_monoph_kin, 1 hit
    SUPFAMiSSF55326 SSF55326, 1 hit
    SSF56042 SSF56042, 1 hit
    TIGRFAMsiTIGR01379 thiL, 1 hit

    Sequencei

    Sequence statusi: Complete.

    P0AGG0-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MACGEFSLIA RYFDRVRSSR LDVELGIGDD CALLNIPEKQ TLAISTDTLV
    60 70 80 90 100
    AGNHFLPDID PADLAYKALA VNLSDLAAMG ADPAWLTLAL TLPDVDEAWL
    110 120 130 140 150
    ESFSDSLFDL LNYYDMQLIG GDTTRGPLSM TLGIHGFVPM GRALTRSGAK
    160 170 180 190 200
    PGDWIYVTGT PGDSAAGLAI LQNRLQVADA KDADYLIKRH LRPSPRILQG
    210 220 230 240 250
    QALRDLANSA IDLSDGLISD LGHIVKASDC GARIDLALLP FSDALSRHVE
    260 270 280 290 300
    PEQALRWALS GGEDYELCFT VPELNRGALD VALGHLGVPF TCIGQMTADI
    310 320
    EGLCFIRDGE PVTLDWKGYD HFATP
    Length:325
    Mass (Da):35,071
    Last modified:December 20, 2005 - v1
    Checksum:i9955DCE2D8CFFB8F
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti254A → E in BAA21778 (Ref. 1) Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D17333 Genomic DNA Translation: BAA21778.1
    U82664 Genomic DNA Translation: AAB40173.1
    U00096 Genomic DNA Translation: AAC73520.1
    AP009048 Genomic DNA Translation: BAE76197.1
    PIRiA64771
    RefSeqiNP_414951.1, NC_000913.3
    WP_000742109.1, NZ_LN832404.1

    Genome annotation databases

    EnsemblBacteriaiAAC73520; AAC73520; b0417
    BAE76197; BAE76197; BAE76197
    GeneIDi947387
    KEGGiecj:JW0407
    eco:b0417
    PATRICifig|1411691.4.peg.1860

    Similar proteinsi

    Entry informationi

    Entry nameiTHIL_ECOLI
    AccessioniPrimary (citable) accession number: P0AGG0
    Secondary accession number(s): O32380, P77785, Q2MC09
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: December 20, 2005
    Last modified: March 28, 2018
    This is version 98 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health