Q1QUD0 · Q1QUD0_CHRSD

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 site31Mg2+ 3 (UniProtKB | ChEBI)
Binding site31Mg2+ 4 (UniProtKB | ChEBI)
Binding site46Mg2+ 4 (UniProtKB | ChEBI)
Binding site48Mg2+ 1 (UniProtKB | ChEBI)
Binding site48Mg2+ 2 (UniProtKB | ChEBI)
Binding site55substrate
Binding site76Mg2+ 4 (UniProtKB | ChEBI)
Binding site76Mg2+ 2 (UniProtKB | ChEBI)
Binding site76Mg2+ 3 (UniProtKB | ChEBI)
Binding site122-123ATP (UniProtKB | ChEBI)
Binding site123Mg2+ 1 (UniProtKB | ChEBI)
Binding site147ATP (UniProtKB | ChEBI)
Binding site209Mg2+ 3 (UniProtKB | ChEBI)
Binding site211ATP (UniProtKB | ChEBI)
Binding site212Mg2+ 5 (UniProtKB | ChEBI)
Binding site260substrate
Binding site311substrate

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
    • Ordered locus names
      Csal_2581

Organism names

Accessions

  • Primary accession
    Q1QUD0

Proteomes

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain29-139PurM-like N-terminal
Domain152-300PurM-like C-terminal

Sequence similarities

Belongs to the thiamine-monophosphate kinase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    319
  • Mass (Da)
    32,609
  • Last updated
    2006-05-16 v1
  • Checksum
    6A2FDB0887FF2FAB
MLGEFDIIARYFTTPDSEPPMPGVALGVGDDCALLSPEAGHELALSVDTSVVDVHFPGDAPPEAIGHRALAVALSDLAAMGARPRGCLMALTLSHAEPDWLERFAHGFRELGRRTATPLIGGDVTRGSLSIGVTVIGDVPAGQALRRTGAAPGERLAVTGSLGGGHAGLRMWQAGGHDLADPLLAAYLTPTPQLAAGQALRDLASAGLDISDGLLADLGHLCRASGVGAVLSPDDLPLAPSLDMTLGREAALHAALNGGDDYQLLVSVPDAAWADAQQRCAACDVALTEIGRVTAEPGIRGIPETLQGVGWQHFTGGAS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000285
EMBL· GenBank· DDBJ
ABE59928.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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