A0A2V8PLK2 · A0A2V8PLK2_UNCAI
- Protein3,4-dihydroxy-2-butanone 4-phosphate synthase
- GeneribB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids395 (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 | 27-28 | D-ribulose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 28 | Mg2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 28 | Mg2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 32 | D-ribulose 5-phosphate (UniProtKB | ChEBI) | |||
Site | 126 | Essential for catalytic activity | |||
Binding site | 140-144 | D-ribulose 5-phosphate (UniProtKB | ChEBI) | |||
Site | 164 | 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 > Acidobacteriota
Accessions
- Primary accessionA0A2V8PLK2
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 208-373 | GTP cyclohydrolase II | |||
Region | 375-395 | Disordered | |||
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 statusComplete
- Length395
- Mass (Da)43,458
- Last updated2018-09-12 v1
- Checksum49840657337FC154
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
QHXG01000178 EMBL· GenBank· DDBJ | PYS63428.1 EMBL· GenBank· DDBJ | Genomic DNA |