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A0A2D3D3I1 · A0A2D3D3I1_9BIFI

Function

function

Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.
Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per subunit.

Pathway

Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-ribosyl)imidazole: step 3/3.
Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site48-524-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI)
Binding site844-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI)
Binding site85Mg2+ (UniProtKB | ChEBI)
Binding site109Mg2+ (UniProtKB | ChEBI)
Binding site1284-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI)
Binding site157-1592-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate (UniProtKB | ChEBI)
Binding site1604-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI)
Binding site1932-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate (UniProtKB | ChEBI)
Binding site213-2142-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionhydroxymethylpyrimidine kinase activity
Molecular Functionmagnesium ion binding
Molecular Functionphosphomethylpyrimidine kinase activity
Molecular Functionthiamine-phosphate diphosphorylase activity
Biological Processphosphorylation
Biological Processthiamine biosynthetic process
Biological Processthiamine diphosphate biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Thiamine-phosphate synthase
  • EC number
  • Short names
    TP synthase
    ; TPS
  • Alternative names
    • Thiamine-phosphate pyrophosphorylase
      (TMP pyrophosphorylase
      ; TMP-PPase
      )

Gene names

    • Name
      thiE
    • ORF names
      BcFMB_00315

Organism names

  • Taxonomic identifier
  • Strain
    • FMB-1
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Bifidobacteriales > Bifidobacteriaceae > Bifidobacterium

Accessions

  • Primary accession
    A0A2D3D3I1

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain18-216Thiamine phosphate synthase/TenI
Domain264-508Pyridoxamine kinase/Phosphomethylpyrimidine kinase

Sequence similarities

Belongs to the thiamine-phosphate synthase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    514
  • Mass (Da)
    53,432
  • Last updated
    2018-01-31 v1
  • MD5 Checksum
    FD6154BFF40441E4255C4406D397A5A6
MTAAFPYPSMRRSFDLRFYFVIGPDDCKGRTLLDVVSKALDGGASFVQLRAKHADVADIVSMAADIAEEIRGHHLDDRVAFVIDDRVDAAIEARHRGIKVDGVHIGQDDLSPEEARRLLGNDAIVGLSANTPEQVEAANALPAGTIDYIGAGPLHATATKPEAGVAGKAKTLDAEQINALCDKSLYPLVVGGGVHVDDVPMLADTYADGWFVVSAIAAADDPEVATQRLVDAWTAVRGDARHGYEETVGTPVKLPAVLSIATTDSSGGAGIAADLKTMLANDVYGECVIAGITAQNTTGVQAIASVDAALIGAQIDSVFDDIRPTAVKIGVVVGREAIETVAAKLRAHGAKHVVVDPVMVATSGSSLADDESVVTMTRELFPLAEVITPNIPETSTLVGEAIDGRDAMERAARTLAERYGCAALVKGGHGTNDASDVLVWPGGDVRWFEGERIANTNTHGTGCTLSSAIASRLALGDTLGDAVANAKAYLGGALRAQLDLGAGAGPMDHGWARH

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP018044
EMBL· GenBank· DDBJ
ATU19638.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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