A0A2I0PLG9 · A0A2I0PLG9_9EURY

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 site45Mg2+ 4 (UniProtKB | ChEBI)
Binding site45Mg2+ 3 (UniProtKB | ChEBI)
Binding site59Mg2+ 4 (UniProtKB | ChEBI)
Binding site60Mg2+ 1 (UniProtKB | ChEBI)
Binding site61Mg2+ 1 (UniProtKB | ChEBI)
Binding site61Mg2+ 2 (UniProtKB | ChEBI)
Binding site68substrate
Binding site89Mg2+ 4 (UniProtKB | ChEBI)
Binding site89Mg2+ 3 (UniProtKB | ChEBI)
Binding site89Mg2+ 2 (UniProtKB | ChEBI)
Binding site136-137ATP (UniProtKB | ChEBI)
Binding site137Mg2+ 1 (UniProtKB | ChEBI)
Binding site162ATP (UniProtKB | ChEBI)
Binding site237Mg2+ 3 (UniProtKB | ChEBI)
Binding site239ATP (UniProtKB | ChEBI)
Binding site240Mg2+ 5 (UniProtKB | ChEBI)
Binding site291substrate
Binding site342substrate

GO annotations

AspectTerm
Molecular FunctionATP binding
Molecular Functionmagnesium ion binding
Molecular Functionthiamine-phosphate kinase activity
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
      CVV28_06630

Organism names

Accessions

  • Primary accession
    A0A2I0PLG9

Proteomes

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain43-154PurM-like N-terminal
Domain166-329PurM-like C-terminal

Sequence similarities

Belongs to the thiamine-monophosphate kinase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    347
  • Mass (Da)
    38,372
  • Last updated
    2018-02-28 v1
  • Checksum
    01CB71634D1F70E7
MMSKKPLISDFGEKKLIENIINKTNIYQKEYFSSHPQIRDSLGDDAALTDIGSGYLVSTSDMLLQETHFPPQMNHRQMGWKIVTVNVSDLAAMGAYPRGILISMGLPRDMTMEQFNELVEGILDACTYYETPLIGGDTNESPQIVLNGTALGEVTKEKVLMKKNLQKGNLIVVTGSLGLAAAGFEILLADDNDSLQKIESLKGEFVKKAVKHALDPRAKIKEGIIAAESKLVTSCTDITDGLTSELYDMLKAENNIGIRIYEHKIPSHPLVEEVSKITGKNLHQMTLYYGEDFELLLTVKKEEIDVLKKLMDVYVVGEVTDSAYVEIVDKYGKTNILPPGGYQHLGG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
PGYO01000005
EMBL· GenBank· DDBJ
PKL67079.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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