A0A6M8U6B4 · A0A6M8U6B4_9GAMM

  • Protein
    1-deoxy-D-xylulose-5-phosphate synthase
  • Gene
    dxs
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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 site80thiamine diphosphate (UniProtKB | ChEBI)
Binding site121-123thiamine diphosphate (UniProtKB | ChEBI)
Binding site152Mg2+ (UniProtKB | ChEBI)
Binding site153-154thiamine diphosphate (UniProtKB | ChEBI)
Binding site181Mg2+ (UniProtKB | ChEBI)
Binding site181thiamine diphosphate (UniProtKB | ChEBI)
Binding site288thiamine diphosphate (UniProtKB | ChEBI)
Binding site370thiamine diphosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
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 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
      PMPD1_1190

Organism names

Accessions

  • Primary accession
    A0A6M8U6B4

Proteomes

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain319-484Transketolase-like pyrimidine-binding

Sequence similarities

Belongs to the transketolase family. DXPS subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    621
  • Mass (Da)
    67,584
  • Last updated
    2020-10-07 v1
  • Checksum
    C2D99CD5E063A1AA
MSFDIAKYPTLAQASSVTELRSLPKEKLPKLCDELRQYLLDSVSRSSGHFASGLGVVELTVALHYVYNTPFDHLVWDVGHQAYPHKILTGRRDRIGTIRQKNGLHPFPWREESEYDVLCVGHSSTSISAGLGMAVAAEKEAKGRRTACVIGDGAITAGMAFEAMNHAGDIKADLLVVLNDNEMSISENVGALNNRLAQILSGKTYARLREGGKKVLTGLPPIKELVKRTEEHLKGMVVPGTLFEELGFNYIGPVDGHDVLALVHTLKNMRDLKGPQFLHIMTKKGKGYAPAEKDPITWHAVPKFDPASGLLPKSVEGLPSYSKIFGNWLCEMAADDNKLMAVTPAMREGSGMVGFSREYPAQYFDVAIAEQHAVTFAAGLAIGGYKPIVAIYSTFLQRAYDQVIHDVAIQKLPVLFAIDRGGIVGADGQTHQGAFDLAYLRCIPNMVIMTPSDENECRLMLYTGYHRNDGPSAVRYPRGNGTGATLAPLAALPLGKGVTKRQGEKLAILNFGTLLPEAQTVADALNATLVDMRFVKPLDEKLILELAATHESLITLEEGAIKGGAGSGVNELLMAKRTPVPVLNLGLPDEFIPQGTQDEIRHDYRLDASGIQQQIDDWLAQ

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP054212
EMBL· GenBank· DDBJ
QKJ86155.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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