A0AA37NQ17 · A0AA37NQ17_9BACT

  • 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).

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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 site78thiamine diphosphate (UniProtKB | ChEBI)
Binding site119-121thiamine diphosphate (UniProtKB | ChEBI)
Binding site150Mg2+ (UniProtKB | ChEBI)
Binding site151-152thiamine diphosphate (UniProtKB | ChEBI)
Binding site180Mg2+ (UniProtKB | ChEBI)
Binding site180thiamine 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 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
      CE91St16_34820

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • CE91-St16
  • Taxonomic lineage
    Bacteria > Bacteroidota > Bacteroidia > Bacteroidales > Rikenellaceae > Alistipes

Accessions

  • Primary accession
    A0AA37NQ17

Proteomes

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain319-483Transketolase-like pyrimidine-binding

Sequence similarities

Belongs to the transketolase family. DXPS subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    632
  • Mass (Da)
    68,662
  • Last updated
    2024-01-24 v1
  • Checksum
    25DE8C1ED479762B
MTSEEYRLLLHIDSPEDLKRLSAEELRAYCDELRRYIVDECSVNPGHLASSLGAVELAAALHYVFDTPADKIVWDVGHQTYAHKIITGRREAFKTKRRLGGISGFPRMSESEYDAFGGGHASVSISAAFGMAKAAELRGEKYRVVAVIGDGSMTGGLAFEGLNNAGASKRTNLLVILNDNNMAIDQATGALKNYLLKISTSVHYNRFKQRLWGILSHTPRLLRLCQKAGNAVKQGLLNKSNLFESLNFRYFGPVDGHNLKELVRTLRALRDIEGPKLLHVMTVKGKGYLPAEHNQPVWHAPGRFNPDTGERISSPGSASRYQDVFGETLVELAERDSRVVGVTPAMPSGCSMNLLMQAMPSRCFDVGIAEGHAVTFSAGLAAAGMVPFCNIYSTFMQRAYDNVIHDVAIQDLPVVMCLDRGGLVGEDGVTHHGVFDMAAFGCVPTLAIAAPMDELELRGMMYTGLQYGHPFMIRYPRGCGEGRMWRGARFETLPVGRGRKLRDGADVALVTVGTVGNAAARAAARAAEEGVSAAHYDLRFAKPLDEELLLEVGAKFRRVVTVEDGALRGGVGEAVAAFFNARGLDVSVRSLGIGDEWVEHGTPAQLYALCGYDEEGILKALLETKQAPVCAK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BQOL01000004
EMBL· GenBank· DDBJ
GKI20574.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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