A0A292DDN0 · A0A292DDN0_STALU
- ProteinRiboflavin biosynthesis protein RibBA
- GeneribBA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids393 (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.
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 | 27-28 | D-ribulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: RE | ||||||
Binding site | 28 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 28 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 32 | D-ribulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Site | 125 | Essential for DHBP synthase activity | ||||
Sequence: H | ||||||
Binding site | 139-143 | D-ribulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: REGHT | ||||||
Binding site | 142 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 163 | D-ribulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Site | 163 | Essential for DHBP synthase activity | ||||
Sequence: E | ||||||
Binding site | 249-253 | GTP (UniProtKB | ChEBI) | ||||
Sequence: RIHSA | ||||||
Binding site | 254 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 265 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 267 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 270 | GTP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 291-293 | GTP (UniProtKB | ChEBI) | ||||
Sequence: EGR | ||||||
Binding site | 313 | GTP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Active site | 325 | Proton acceptor; for GTP cyclohydrolase activity | ||||
Sequence: D | ||||||
Active site | 327 | Nucleophile; for GTP cyclohydrolase activity | ||||
Sequence: R | ||||||
Binding site | 348 | GTP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 353 | GTP (UniProtKB | ChEBI) | ||||
Sequence: K |
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 nameRiboflavin biosynthesis protein RibBA
Including 2 domains:
- Recommended name3,4-dihydroxy-2-butanone 4-phosphate synthase
- EC number
- Short namesDHBP synthase
- Recommended nameGTP cyclohydrolase-2
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Staphylococcaceae > Staphylococcus
Accessions
- Primary accessionA0A292DDN0
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-200 | DHBP synthase | ||||
Sequence: MQFDTIEEALQALKKGETIIVVDDEDRENEGDLVAVTQWMQDQTINFMAKHGRGLICTPISTDIAERLELKPMVMQNSDDYGTNFTVSIDHYTTTTGISAIERMTTARSLIATDTMAEDFHKPGHLFPLIAKDNGVLEREGHTEATVDLAKMTGAAPAGVICEIMNDDGSMAKGEQLEKFKETHQLKLISIKQIIEYRHQ | ||||||
Region | 201-393 | GTP cyclohydrolase II | ||||
Sequence: HDIQVNLRAKVNMPTDFGNFEMYGFDSTLTQDEIVVITKGEPRTTENVRIHSACLTGDIFHSQRCDCGAQLESSLKYINEHGGMVIYLPQEGRGIGLINKLRAYELIEQGYDTVTANLALGFDEDLRDYKVASQILKYFNVKQVNLLSNNPKKFEGLSEYDIEIAKRIEVIVPETTHNHDYMETKKIKMGHLI | ||||||
Domain | 209-368 | GTP cyclohydrolase II | ||||
Sequence: AKVNMPTDFGNFEMYGFDSTLTQDEIVVITKGEPRTTENVRIHSACLTGDIFHSQRCDCGAQLESSLKYINEHGGMVIYLPQEGRGIGLINKLRAYELIEQGYDTVTANLALGFDEDLRDYKVASQILKYFNVKQVNLLSNNPKKFEGLSEYDIEIAKRI |
Sequence similarities
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 statusComplete
- Length393
- Mass (Da)44,308
- Last updated2018-02-28 v1
- ChecksumADDA817CFEDA4288
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
SCHB01000006 EMBL· GenBank· DDBJ | TBW71722.1 EMBL· GenBank· DDBJ | Genomic DNA |