A0A0A0EJ29 · A0A0A0EJ29_9GAMM

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 site80thiamine diphosphate (UniProtKB | ChEBI)
Binding site121-123thiamine diphosphate (UniProtKB | ChEBI)
Binding site152Mg2+ (UniProtKB | ChEBI)
Binding site153-154thiamine diphosphate (UniProtKB | ChEBI)
Binding site188Mg2+ (UniProtKB | ChEBI)
Binding site188thiamine diphosphate (UniProtKB | ChEBI)
Binding site296thiamine diphosphate (UniProtKB | ChEBI)
Binding site378thiamine 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
      N792_12915

Organism names

Accessions

  • Primary accession
    A0A0A0EJ29

Proteomes

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain327-491Transketolase-like pyrimidine-binding

Sequence similarities

Belongs to the transketolase family. DXPS subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    640
  • Mass (Da)
    68,913
  • Last updated
    2015-01-07 v1
  • Checksum
    199F1825A71931EE
MMIDPQRYPRLSRIDVPADLRQFPAEELPAIAAELRAYLIEQVAQSGGHFGAGLGVIELTVALHWLYDTPTDRLVWDVGHQTYPHKILTGRRDRIHTVKQKDGVAPFPKRDESEYDTFGVGHSSTSISAALGMAIALQRTGDERKVIAVIGDGAITAGMAFEALAHGGGMGEQPGGIEPNLLVILNDNQMSISENVGGVTRMLGRLTGSRTLNALREGGKKLLGDKHRPAAKFVKRWEEQWKGMFVPSTMFEELGFHYTGPIDGHDMDALVGTLKTLQGMKGPQLLHIITTKGKGYERAEGDQIGYHAVGPFNPDLGMVSKTGAKKPTYTDVFGDWICDMAAADEQLMGITPAMREGSGLVRFSKQYPQRYFDVAIAEQHAVTLAAGMACEGAKPVVAIYSTFLQRGYDQLVHDVAVQELDVLFAIDRGGVVGPDGATHAGNLDLSYLRCVPNMVVMAPADENECRQMLSTGFRFQGPAAVRYPRGTGPGVEVQGSLDLLPIGKAQLRRHGANVALLAFGALVPAAEQVGEALDLTVVNMRFVKPLDRTLLLELTKTHEGFVTLEDNVVAGGAGSGVAELLAAEGLTMPMLHLGLPDAFQHHASREELLAEAGLDADGIRAAVLRRWPQLGASPTRSAAV

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AVPS01000009
EMBL· GenBank· DDBJ
KGM50971.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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