A0A0U5B4I9 · A0A0U5B4I9_9BACT

Function

function

Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per subunit.
thiamine diphosphate (UniProtKB | Rhea| CHEBI:58937 )

Note: Binds 1 thiamine pyrophosphate per subunit.

Pathway

Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose 5-phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D-glyceraldehyde 3-phosphate and pyruvate: step 1/1.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site73thiamine diphosphate (UniProtKB | ChEBI)
Binding site114-116thiamine diphosphate (UniProtKB | ChEBI)
Binding site145Mg2+ (UniProtKB | ChEBI)
Binding site146-147thiamine diphosphate (UniProtKB | ChEBI)
Binding site174Mg2+ (UniProtKB | ChEBI)
Binding site174thiamine diphosphate (UniProtKB | ChEBI)
Binding site284thiamine diphosphate (UniProtKB | ChEBI)
Binding site366thiamine diphosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Function1-deoxy-D-xylulose-5-phosphate synthase activity
Molecular Functionmagnesium ion binding
Molecular Functionthiamine pyrophosphate binding
Biological Process1-deoxy-D-xylulose 5-phosphate biosynthetic process
Biological Processisopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway
Biological Processterpenoid biosynthetic process
Biological Processthiamine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    1-deoxy-D-xylulose-5-phosphate synthase
  • EC number
  • Alternative names
    • 1-deoxyxylulose-5-phosphate synthase
      (DXP synthase
      ; DXPS
      )

Gene names

    • Name
      dxs
    • ORF names
      THC_0582

Organism names

  • Taxonomic identifier
  • Strain
    • TF1
  • Taxonomic lineage
    Bacteria > Thermodesulfobacteriota > Thermodesulfobacteria > Thermodesulfobacteriales > Thermodesulfobacteriaceae > Caldimicrobium

Accessions

  • Primary accession
    A0A0U5B4I9

Proteomes

Subcellular Location

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain315-479Transketolase-like pyrimidine-binding

Sequence similarities

Belongs to the transketolase family. DXPS subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    623
  • Mass (Da)
    68,281
  • Last updated
    2016-03-16 v1
  • MD5 Checksum
    CEACB73A641891B081326CEAAE967D8D
MSLLSKIEGPEDLKKLKPSQLKLLAEEIRKLILDVVSKNGGHLAPNLGVVELTLALHYVFDTPKDKIIWDVGHQCYTHKILTGRRDAFKTLRTFQGLAGFPKRAESPYDVLDTGHSSTSISAGLGMAVARRIKGETGKIIVVIGDGSITAGMAFEALNNTGYLREDLLIILNDNEMSISPNVGALSSFVSKRMTGNLARFIKKEIEKIVPRLPGGDNLLHIFKKGEDLLKMAVTPGALFTALNFEYVGPVDGHDLDTLIEILKNLKELKGPIIFHVVTKKGKGYPPAEADPETFHGIGPFNLETGRPLKSEGAPPSYTEVFGDTLVKLAELEPRLIAITAAMKSGTGLKKFAQKYPDRFFDVGICEQHAVTFAAGLALEGFIPVCAIYSTFLQRAYDQIIHDVALNKAKVIFAIDRAGLVGEDGPTHHGAFDLSYLRPIPDLIICAPKDEKELRNLLFSALKYEGPCAIRYPRGEAIGVKIDENFSFIPSGKAEVLKEGKDGAIFAIGSMCYPALKAGEELEKKGFSVAVINVRFLKPLDRELLLEYAKKTGKVLVVEENSILGGLRSSVSELLLEEGIYVKFGYLGLPDHFVEQGDLKTLRKKYGLSTEKIIEKFVNLVGNY

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP014945
EMBL· GenBank· DDBJ
BAU22976.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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