Q8G9H7 · Q8G9H7_PHOPO

  • Protein
    3,4-dihydroxy-2-butanone 4-phosphate synthase
  • Gene
    ribBA
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.

Catalytic activity

Cofactor

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

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Note: Binds 2 divalent metal cations per subunit. Magnesium or manganese.
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Pathway

Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.

Features

Showing features for binding site, site.

Type
IDPosition(s)Description
Binding site27-28D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site28Mg2+ 1 (UniProtKB | ChEBI)
Binding site28Mg2+ 2 (UniProtKB | ChEBI)
Binding site32D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site126Essential for catalytic activity
Binding site140-144D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site143Mg2+ 2 (UniProtKB | ChEBI)
Site164Essential for catalytic activity

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Function3,4-dihydroxy-2-butanone-4-phosphate synthase activity
Molecular FunctionGTP cyclohydrolase II activity
Molecular Functionmagnesium ion binding
Molecular Functionmanganese ion binding
Biological Processriboflavin biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    3,4-dihydroxy-2-butanone 4-phosphate synthase
  • EC number
  • Short names
    DHBP synthase

Gene names

    • Name
      ribBA
    • Synonyms
      ribB

Organism names

  • Taxonomic identifier
  • Strain
    • IFO 13896
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Vibrionales > Vibrionaceae > Photobacterium

Accessions

  • Primary accession
    Q8G9H7

Subcellular Location

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain208-365GTP cyclohydrolase II

Sequence similarities

Belongs to the DHBP synthase family.
In the C-terminal section; belongs to the GTP cyclohydrolase II family.
In the N-terminal section; belongs to the DHBP synthase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    367
  • Mass (Da)
    40,054
  • Last updated
    2003-03-01 v1
  • MD5 Checksum
    F028620724AF14AF55A9B65AB59AD7E8
MALSSAKEIIDDIRQGKMVILMDDEDRENEGDLIIASEKITPETINFMAMYGRGLICLTLSKARCQKLGLPLMVQDNTEQFGTPFTISIEAATGVTTGISAADRARTVQAAVAADATAANIVMPGHIFPLMAQEGGVLTRAGHTEAGCDIARLAGLEPSSVIVEILNEDGTMARRPQLEIFAEKHGLKLGTIADLIEYRNHHETTIERVGECKLNTEFGEFDMITYRDKIDDQIHYALCKGDIEADAATLVRVHLQDTFKDILQSGATQWTLPAAMQRISAENGVLVILSKQESTDSIINKVKNIAAEKEGRPQVKMSPYNPSRQVGVGSQILSDLGIGKMRLLSSSTQRYHSLSGFGLEVVEYICE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB065118
EMBL· GenBank· DDBJ
BAC44851.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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