A0A1E9HN18 · A0A1E9HN18_9MICO

Function

function

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

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 )

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 site29-30D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site30Mg2+ 2 (UniProtKB | ChEBI)
Binding site30Mg2+ 1 (UniProtKB | ChEBI)
Binding site34D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site128Essential for catalytic activity
Binding site142-146D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site145Mg2+ 2 (UniProtKB | ChEBI)
Site166Essential for catalytic activity

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Function3,4-dihydroxy-2-butanone-4-phosphate synthase activity
Molecular FunctionGTP binding
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
      ribB
    • ORF names
      HMPREF2757_08920

Organism names

  • Taxonomic identifier
  • Strain
    • HMSC063G07
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Micrococcales > Brevibacteriaceae > Brevibacterium

Accessions

  • Primary accession
    A0A1E9HN18

Proteomes

Subcellular Location

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region208-240Disordered
Compositional bias209-232Polar residues
Domain246-402GTP cyclohydrolase II

Sequence similarities

Belongs to the DHBP synthase family.
In the N-terminal section; belongs to the DHBP synthase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    432
  • Mass (Da)
    45,569
  • Last updated
    2017-01-18 v1
  • Checksum
    E23315592B1C7312
MTTTLASIEDAIQQIAAGRPIVVVDDEDRENEGDLIMAADAVTAEWMGFIIRYSSGVVCAPIPAQTAQRLALPPMTADNEDPKGTAYTVSVDAKAGVTTGISAADRSLTARLLADPDTRTEDLTRPGHLFPLIAQDDGVLARDGHTEAGLDFARLAGRSPAAVIAEIVHDDGSMMRFAALAEFAREHGLAMVTIADLIAYRKANPDAPMTPVPTTSGKNQSTGPTAAQSAAAGGNTAGRRLVRGETVPLPTDFGTLTATAYTFDGTDHLVLSGPPNADSTPLVRIHSECLTGDVFGSHRCDCGEQLAQALRTVATVGGHVIYVRGHEGRGIGLAGKIAAYSLQDTGVDTVDANTRLGFAADARKYDAVAAILADMGLHSVRLMTNNPTKITALQHMDIDVTRVDAEVAPRPENIAYLATKRDRMSHLLERTL

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias209-232Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LTHM01000009
EMBL· GenBank· DDBJ
OFL68009.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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