A0AAF0GYM6 · A0AAF0GYM6_RHIRD
- Protein3,4-dihydroxy-2-butanone 4-phosphate synthase
- GeneribB
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids366 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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) | ||||
Sequence: RE | ||||||
Binding site | 30 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 30 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 34 | D-ribulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Site | 128 | Essential for catalytic activity | ||||
Sequence: H | ||||||
Binding site | 142-146 | D-ribulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: RSGHT | ||||||
Binding site | 145 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Site | 166 | Essential for catalytic activity | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | 3,4-dihydroxy-2-butanone-4-phosphate synthase activity | |
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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Rhizobiaceae > Rhizobium/Agrobacterium group > Agrobacterium > Agrobacterium tumefaciens complex
Accessions
- Primary accessionA0AAF0GYM6
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 213-361 | GTP cyclohydrolase II | ||||
Sequence: SFTIDTPFGPAKAQTYSLPWDPMQHMAVIFGDIRDGVDIPVRLHPENVADDVFGDRQPVRHYMQKIAEEGRGVIVYLREGSVGVGQVAGRRKARDPEEAHAQARSRENEWLEIGLGAQILKDLGISSIKLLTTRERHYVGLEGFGIKIS |
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.
Family and domain databases
Sequence
- Sequence statusComplete
- Length366
- Mass (Da)40,183
- Last updated2024-05-29 v1
- ChecksumC8E0033CCB2F07AF