P43525 · RIBA_AZOBR
- ProteinGTP cyclohydrolase-2
- GeneribA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids385 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.
Catalytic activity
- GTP + 4 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + formate + 2 phosphate + 3 H+
Cofactor
Note: Binds 1 zinc ion per subunit.
Pathway
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 | 240-244 | GTP (UniProtKB | ChEBI) | |||
Binding site | 245 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 256 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 258 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 261 | GTP (UniProtKB | ChEBI) | |||
Binding site | 283-285 | GTP (UniProtKB | ChEBI) | |||
Binding site | 305 | GTP (UniProtKB | ChEBI) | |||
Active site | 317 | Proton acceptor | |||
Active site | 319 | Nucleophile | |||
Binding site | 340 | GTP (UniProtKB | ChEBI) | |||
Binding site | 345 | 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
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Rhodospirillales > Azospirillaceae > Azospirillum
Accessions
- Primary accessionP43525
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000151784 | 1-385 | GTP cyclohydrolase-2 | ||
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-189 | DHBP synthase-like | |||
Region | 190-385 | GTP cyclohydrolase II | |||
Sequence similarities
In the N-terminal section; belongs to the DHBP synthase family.
In the C-terminal section; belongs to the GTP cyclohydrolase II family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length385
- Mass (Da)40,972
- Last updated1995-11-01 v1
- MD5 ChecksumA09CE1A4E2909F3BB90D982AFC36A144
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U09869 EMBL· GenBank· DDBJ | AAA82170.1 EMBL· GenBank· DDBJ | Genomic DNA |