A0A2V8PLK2 · A0A2V8PLK2_UNCAI

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

Function

function

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

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
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 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)
Site164Essential 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
      DMF74_10100

Organism names

Accessions

  • Primary accession
    A0A2V8PLK2

Proteomes

Subcellular Location

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain, region.

Type
IDPosition(s)Description
Domain208-373GTP cyclohydrolase II
Region375-395Disordered

Sequence similarities

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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    395
  • Mass (Da)
    43,458
  • Last updated
    2018-09-12 v1
  • Checksum
    49840657337FC154
MAFASIADAAADIREGRMIIIVDDEDRENEGDLVCAAEKVTPEIINFMARHARGLICLPLTEERCDELHLPPQVTDNTSRLGTAFTVSIEARRGVTTGISAADRATTILTAVDQRTRPQDLARPGHVFPLRARKGGVLVRPGQTEAAVDMARIAGLYPAGVICEIMNEDGTMARLPQLRDFAVVHGLKIITVADLVHYRISKEVLVRRAVETDLPTVYGRFRAIAFENTINGDVHLAMVMGDVRNDDPVLVRVHTENVTCDMFGSTIDDTGYQLRRALEKISEVGQGVVLYLRQSEHSLDLIHQLRTYALMQERGIRKAEASAETGYGLNRDYGVGAQILHELGLRRILLLTNHPPKVTALEGFELEVVGNVPLGSPASERMSERSELAVTLNEP

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QHXG01000178
EMBL· GenBank· DDBJ
PYS63428.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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