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A0A1F9WFM0 · A0A1F9WFM0_9BACT

Function

function

Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.

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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Pathway

Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine phosphate: step 1/1.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site34Mg2+ 4 (UniProtKB | ChEBI)
Binding site34Mg2+ 3 (UniProtKB | ChEBI)
Binding site49Mg2+ 4 (UniProtKB | ChEBI)
Binding site50Mg2+ 1 (UniProtKB | ChEBI)
Binding site51Mg2+ 2 (UniProtKB | ChEBI)
Binding site51Mg2+ 1 (UniProtKB | ChEBI)
Binding site58substrate
Binding site80Mg2+ 4 (UniProtKB | ChEBI)
Binding site80Mg2+ 2 (UniProtKB | ChEBI)
Binding site80Mg2+ 3 (UniProtKB | ChEBI)
Binding site128-129ATP (UniProtKB | ChEBI)
Binding site129Mg2+ 1 (UniProtKB | ChEBI)
Binding site154ATP (UniProtKB | ChEBI)
Binding site221Mg2+ 3 (UniProtKB | ChEBI)
Binding site223ATP (UniProtKB | ChEBI)
Binding site224Mg2+ 5 (UniProtKB | ChEBI)
Binding site274substrate
Binding site321substrate

GO annotations

AspectTerm
Molecular FunctionATP binding
Molecular Functionmagnesium ion binding
Molecular Functionthiamine-phosphate kinase activity
Biological Processphosphorylation
Biological Processthiamine biosynthetic process
Biological Processthiamine diphosphate biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Thiamine-monophosphate kinase
  • EC number
  • Short names
    TMP kinase
    ; Thiamine-phosphate kinase

Gene names

    • Name
      thiL
    • ORF names
      A2285_02750

Organism names

Accessions

  • Primary accession
    A0A1F9WFM0

Proteomes

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain32-143PurM-like N-terminal

Sequence similarities

Belongs to the thiamine-monophosphate kinase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    324
  • Mass (Da)
    35,063
  • Last updated
    2017-02-15 v1
  • MD5 Checksum
    29262D60BE0F7C69C2EBEA1A648E003E
MKKRMAGEAGVLKVIESVLRFPADRRLILGPGDDCAVVRHAPGRELVITTDELVEGTHYLGRFASPENLAGKLMRVNLSDLAAMGAVRPVACLAGAGLCRDTPPVFFSRFIRELKREALRFGISVAGGNLARARENHFYMTVWGEASRCGLVKRRGAAAGDLLLSVGPLGEAAAGLEILKRGSRAEAGKFPGLVRAFWRPRPMLEEGRRISRGRLATGMLDNSDGLFSSARQLAALARCRVILSPGEGACSPALRAYCAGKKKDWRSYAISGGEDYGLVFSARPEDLSKIKNALPRVLVVGRFERGRGAEAENLDGKVKSFEHF

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MGVB01000020
EMBL· GenBank· DDBJ
OGS13965.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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