Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

V4XTM9 · V4XTM9_9ARCH

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.

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 site20Mg2+ 4 (UniProtKB | ChEBI)
Binding site20Mg2+ 3 (UniProtKB | ChEBI)
Binding site30Mg2+ 4 (UniProtKB | ChEBI)
Binding site31Mg2+ 1 (UniProtKB | ChEBI)
Binding site32Mg2+ 1 (UniProtKB | ChEBI)
Binding site32Mg2+ 2 (UniProtKB | ChEBI)
Binding site39substrate
Binding site60Mg2+ 3 (UniProtKB | ChEBI)
Binding site60Mg2+ 4 (UniProtKB | ChEBI)
Binding site60Mg2+ 2 (UniProtKB | ChEBI)
Binding site106-107ATP (UniProtKB | ChEBI)
Binding site107Mg2+ 1 (UniProtKB | ChEBI)
Binding site130ATP (UniProtKB | ChEBI)
Binding site188Mg2+ 3 (UniProtKB | ChEBI)
Binding site190ATP (UniProtKB | ChEBI)
Binding site191Mg2+ 5 (UniProtKB | ChEBI)
Binding site240substrate
Binding site287substrate

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
      A07HR60_01272

Organism names

Accessions

  • Primary accession
    V4XTM9

Proteomes

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain18-124PurM-like N-terminal
Domain135-274PurM-like C-terminal

Sequence similarities

Belongs to the thiamine-monophosphate kinase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    291
  • Mass (Da)
    30,670
  • Last updated
    2014-01-22 v1
  • MD5 Checksum
    DAB65853C69EFE5C831E1758AD93E337
MDERAALRKLASDLPKAGDDAAIIGDTAITTDMLHTVTDFPDGTTRYTAGWRAVGASLSDLAAVGATVDAAVAVYADDSFVETELTAFVRGATDVCELVGGSYVGGDLDENTELTVATTAIGEVDDPVLRSGATPGDVVCVTGHFGRSAAALRLFHDGHVEKANELFRFRPRIETGRLLRQRATAAMDSSDGLARSLHQLAEASGVGFDIDSEAVPVHPELEALATDSADRWDRAVHFGEDFELVFTLPESRLPDIAQQAPDAISQIGTVVESGITVDGATLPDRGYTHDG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KI543230
EMBL· GenBank· DDBJ
ESS11934.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help