G2GWD2 · G2GWD2_9ENTR

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 site30Mg2+ 4 (UniProtKB | ChEBI)
Binding site30Mg2+ 3 (UniProtKB | ChEBI)
Binding site45Mg2+ 4 (UniProtKB | ChEBI)
Binding site46Mg2+ 1 (UniProtKB | ChEBI)
Binding site47Mg2+ 1 (UniProtKB | ChEBI)
Binding site47Mg2+ 2 (UniProtKB | ChEBI)
Binding site54substrate
Binding site75Mg2+ 4 (UniProtKB | ChEBI)
Binding site75Mg2+ 3 (UniProtKB | ChEBI)
Binding site75Mg2+ 2 (UniProtKB | ChEBI)
Binding site121-122ATP (UniProtKB | ChEBI)
Binding site122Mg2+ 1 (UniProtKB | ChEBI)
Binding site146ATP (UniProtKB | ChEBI)
Binding site212Mg2+ 3 (UniProtKB | ChEBI)
Binding site214ATP (UniProtKB | ChEBI)
Binding site215Mg2+ 5 (UniProtKB | ChEBI)
Binding site263substrate
Binding site324substrate

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
      Rin_00000650

Organism names

  • Taxonomic identifier
  • Strain
    • R5.15
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > aphid secondary symbionts > Candidatus Regiella

Accessions

  • Primary accession
    G2GWD2

Proteomes

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain28-136PurM-like N-terminal
Domain152-301PurM-like C-terminal

Sequence similarities

Belongs to the thiamine-monophosphate kinase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    337
  • Mass (Da)
    37,143
  • Last updated
    2011-11-16 v1
  • Checksum
    BDC6C902D2A1FE08
MTCGEFDLITRYFNCSKNKRPDVQLGIGDDCALLAVTDEQWLAVSTDTLVSGIHFLPEIAPQDLAYKALAVNLSDLSAMGAEPCWLSLALTMPKVDERWLKAFSDSLFEQLDYHGMQLIGGDTTRGPLSLTLTVHGHLPANKALTRAGAKNDDWIYVSGTLGDSAAGLAILQKKLAIDNAEDRKRLIELHLRPKARVSLGLALRGLANAAIDISDGLIADLQHILTASQCGAKIELDKLPYSDELQRYLDVEKKQGWALNGGEDYELCFTVPECNRIALEKKLNHLEVKYSCIGSITSEVKKIHFLKKGQSVEIKAPYLNHYGFDHFAVTTVDDESK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AGCA01000017
EMBL· GenBank· DDBJ
EGY29943.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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