A0A023X1H9 · A0A023X1H9_9ACTN

Function

function

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).

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per subunit.

Pathway

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 site98-1024-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI)
Binding site1304-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI)
Binding site131Mg2+ (UniProtKB | ChEBI)
Binding site1694-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI)
Binding site195-1972-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate (UniProtKB | ChEBI)
Binding site1984-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI)
Binding site2252-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate (UniProtKB | ChEBI)
Binding site245-2462-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionmagnesium ion binding
Molecular Functionthiamine-phosphate diphosphorylase activity
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
      RradSPS_0587

Organism names

  • Taxonomic identifier
  • Strain
    • RSPS-4
  • Taxonomic lineage
    Bacteria > Actinomycetota > Rubrobacteria > Rubrobacterales > Rubrobacteraceae > Rubrobacter

Accessions

  • Primary accession
    A0A023X1H9

Proteomes

Subcellular Location

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain, compositional bias.

TypeIDPosition(s)Description
Region1-24Disordered
Domain70-248Thiamine phosphate synthase/TenI
Region258-292Disordered
Compositional bias259-292Basic and acidic residues

Sequence similarities

Belongs to the thiamine-phosphate synthase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    292
  • Mass (Da)
    30,790
  • Last updated
    2014-07-09 v1
  • Checksum
    71B2FEB534D62AFD
MPEENSSAENIPLEPEPDSTGVGKRGYGHLDWSCRRVPRNGRGGSFLAGRCLREEASTLQKTRLSPHLIHVVTDRKQASGSPRAAALAALRGGVDAVQFREKGGPARSLYKDVLAVLPEARALGARVLVNDRLDVALAASADGVHLPTKGLPPAVARELLPERMLLGASVHDLREAKEAVACGADYVTFGHVYPTGSKPGLPPKGVRLLAEIVESVSVPVLAIGGIDPSNVDEVLATGAAGIAVISSVIAAGDPQAAARELRRAVDRSPYRPKHPFPQKEKRGAAHATDRQP

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias259-292Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP007514
EMBL· GenBank· DDBJ
AHY45870.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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