A0A6G6WE23 · A0A6G6WE23_9ACTN
- ProteinRiboflavin biosynthesis protein RibBA
- GeneribBA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids423 (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 | 41-42 | D-ribulose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 42 | Mg2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 42 | Mg2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 46 | D-ribulose 5-phosphate (UniProtKB | ChEBI) | |||
Site | 140 | Essential for DHBP synthase activity | |||
Binding site | 154-158 | D-ribulose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 157 | Mg2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 178 | D-ribulose 5-phosphate (UniProtKB | ChEBI) | |||
Site | 178 | Essential for DHBP synthase activity | |||
Binding site | 266-270 | GTP (UniProtKB | ChEBI) | |||
Binding site | 271 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 282 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 284 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 287 | GTP (UniProtKB | ChEBI) | |||
Binding site | 310-312 | GTP (UniProtKB | ChEBI) | |||
Binding site | 332 | GTP (UniProtKB | ChEBI) | |||
Active site | 344 | Proton acceptor; for GTP cyclohydrolase activity | |||
Active site | 346 | Nucleophile; for GTP cyclohydrolase activity | |||
Binding site | 367 | GTP (UniProtKB | ChEBI) | |||
Binding site | 372 | 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 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 > Actinomycetota > Actinomycetes > Propionibacteriales > Nocardioidaceae > Nocardioides
Accessions
- Primary accessionA0A6G6WE23
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-215 | DHBP synthase | |||
Region | 216-423 | GTP cyclohydrolase II | |||
Domain | 222-388 | GTP cyclohydrolase II | |||
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.
Family and domain databases
Sequence
- Sequence statusComplete
- Length423
- Mass (Da)45,952
- Last updated2020-08-12 v1
- ChecksumCEB5D7A2475C2250
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP049257 EMBL· GenBank· DDBJ | QIG43456.1 EMBL· GenBank· DDBJ | Genomic DNA |