A0A1E9HN18 · A0A1E9HN18_9MICO
- Protein3,4-dihydroxy-2-butanone 4-phosphate synthase
- GeneribB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids432 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
Catalytic activity
- D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate + formate + H+
Cofactor
Protein has several cofactor binding sites:
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Note: Binds 2 divalent metal cations per subunit. Magnesium or manganese.
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 | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 29-30 | D-ribulose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 30 | Mg2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 30 | Mg2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 34 | D-ribulose 5-phosphate (UniProtKB | ChEBI) | |||
Site | 128 | Essential for catalytic activity | |||
Binding site | 142-146 | D-ribulose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 145 | Mg2+ 2 (UniProtKB | ChEBI) | |||
Site | 166 | Essential for catalytic activity | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | 3,4-dihydroxy-2-butanone-4-phosphate synthase activity | |
Molecular Function | GTP binding | |
Molecular Function | GTP cyclohydrolase II activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | manganese ion binding | |
Biological Process | riboflavin biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name3,4-dihydroxy-2-butanone 4-phosphate synthase
- EC number
- Short namesDHBP synthase
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Micrococcales > Brevibacteriaceae > Brevibacterium
Accessions
- Primary accessionA0A1E9HN18
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 208-240 | Disordered | |||
Compositional bias | 209-232 | Polar residues | |||
Domain | 246-402 | GTP 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 statusComplete
- Length432
- Mass (Da)45,569
- Last updated2017-01-18 v1
- ChecksumE23315592B1C7312
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 209-232 | Polar residues | |||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LTHM01000009 EMBL· GenBank· DDBJ | OFL68009.1 EMBL· GenBank· DDBJ | Genomic DNA |