K7RV09 · K7RV09_ACIA4
- ProteinGTP cyclohydrolase-2
- GeneribB
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids435 (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:
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, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 263-267 | GTP (UniProtKB | ChEBI) | |||
Binding site | 268 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 279 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 281 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 284 | GTP (UniProtKB | ChEBI) | |||
Binding site | 306-308 | GTP (UniProtKB | ChEBI) | |||
Binding site | 328 | GTP (UniProtKB | ChEBI) | |||
Active site | 340 | Proton acceptor | |||
Active site | 342 | Nucleophile | |||
Binding site | 363 | GTP (UniProtKB | ChEBI) | |||
Binding site | 368 | 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 | zinc ion binding | |
Biological Process | riboflavin biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGTP cyclohydrolase-2
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Propionibacteriales > Propionibacteriaceae > Acidipropionibacterium
Accessions
- Primary accessionK7RV09
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 219-380 | GTP cyclohydrolase II | |||
Sequence similarities
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
- Length435
- Mass (Da)45,856
- Last updated2013-02-06 v1
- Checksum2F793D4135BEC403
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP003493 EMBL· GenBank· DDBJ | AFV90241.1 EMBL· GenBank· DDBJ | Genomic DNA |