A0A2N5JAG3 · A0A2N5JAG3_9BIFI
- ProteinMultifunctional fusion protein
- GeneribA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids441 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.
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.
Note: Binds 1 zinc ion per subunit.
Pathway
Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4.
Features
Showing features for binding site, site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 51-52 | D-ribulose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 52 | Mg2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 52 | Mg2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 56 | D-ribulose 5-phosphate (UniProtKB | ChEBI) | |||
Site | 149 | Essential for catalytic activity | |||
Binding site | 163-167 | D-ribulose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 166 | Mg2+ 2 (UniProtKB | ChEBI) | |||
Site | 187 | Essential for catalytic activity | |||
Binding site | 287-291 | GTP (UniProtKB | ChEBI) | |||
Binding site | 292 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 303 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 305 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 308 | GTP (UniProtKB | ChEBI) | |||
Binding site | 330-332 | GTP (UniProtKB | ChEBI) | |||
Binding site | 352 | GTP (UniProtKB | ChEBI) | |||
Active site | 364 | Proton acceptor | |||
Active site | 366 | Nucleophile | |||
Binding site | 387 | GTP (UniProtKB | ChEBI) | |||
Binding site | 392 | GTP (UniProtKB | ChEBI) | |||
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 | |
Molecular Function | zinc ion binding | |
Biological Process | riboflavin biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMultifunctional fusion protein
Including 2 domains:
- Recommended nameGTP cyclohydrolase-2
- EC number
- Alternative 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 > Bifidobacteriales > Bifidobacteriaceae > Bifidobacterium
Accessions
- Primary accessionA0A2N5JAG3
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-29 | Disordered | |||
Compositional bias | 15-29 | Basic and acidic residues | |||
Domain | 233-408 | GTP cyclohydrolase II | |||
Sequence similarities
Belongs to the DHBP synthase family.
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
- Length441
- Mass (Da)48,662
- Last updated2018-04-25 v1
- Checksum235CEE4EC8765522
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 15-29 | Basic and acidic residues | |||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
NMWU01000015 EMBL· GenBank· DDBJ | PLS31189.1 EMBL· GenBank· DDBJ | Genomic DNA |