A0A087NGH6 · A0A087NGH6_9SPHN

  • Protein
    3,4-dihydroxy-2-butanone 4-phosphate synthase
  • Gene
    ribB
  • 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.

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 site89-90D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site90Mg2+ 2 (UniProtKB | ChEBI)
Binding site90Mg2+ 1 (UniProtKB | ChEBI)
Binding site94D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site188Essential for catalytic activity
Binding site202-206D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site205Mg2+ 2 (UniProtKB | ChEBI)
Site226Essential for catalytic activity

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Function3,4-dihydroxy-2-butanone-4-phosphate synthase activity
Molecular FunctionDNA 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
      IL54_3658

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • ba1
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Sphingomonadales > Sphingomonadaceae > Sphingobium

Accessions

  • Primary accession
    A0A087NGH6

Proteomes

Subcellular Location

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain270-423GTP 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.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    426
  • Mass (Da)
    46,089
  • Last updated
    2014-10-29 v1
  • Checksum
    1A8AF69335DF06C2
MSSALLDTVRRLVTDGGMSRSGLARAAGLHANSLRKLGEGDWNPTADTLGKLEAYLLKREGGTALASPEEIINEARNGRMFILVDDEDRENEGDLVIPAQMATPDAINFMATHGRGLICLALTKARVEELGLGLMSRNNGTRHETAFTVSIEAREGVTTGISAADRARTVSVAIDGSKGKADIVTPGHVFPLVAKDGGVLVRTGHTEAAVDVARLAGLNPSGVICEVMKDDGTMARLDDLIPFAQKHKMKIGTIRDLIAYRRRHDHIVERRAETTFESQWGGDWKAISFYNKATQTEQLALQKGHVTPDQPTLVRMHQFSPLTDTFGQQGPRAGMLARSMKIIGEEGAGIIVVLRGDEPDMLTRMLQHHSGIAQGDMDELRNYGAGAQILAELGVHDMILLTNSNHSLIALDGYDLAVVGQRPIEL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JPPQ01000069
EMBL· GenBank· DDBJ
KFL48229.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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