A0A5C6BAP7 · A0A5C6BAP7_9PLAN
- ProteinGTP cyclohydrolase-2
- GeneribBA_1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids422 (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 | 257-261 | GTP (UniProtKB | ChEBI) | |||
Binding site | 262 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 273 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 275 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 278 | GTP (UniProtKB | ChEBI) | |||
Binding site | 300-302 | GTP (UniProtKB | ChEBI) | |||
Binding site | 322 | GTP (UniProtKB | ChEBI) | |||
Active site | 334 | Proton acceptor | |||
Active site | 336 | Nucleophile | |||
Binding site | 357 | GTP (UniProtKB | ChEBI) | |||
Binding site | 362 | 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 > Planctomycetota > Planctomycetia > Planctomycetales > Planctomycetaceae > Symmachiella
Accessions
- Primary accessionA0A5C6BAP7
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 77-91 | Polar residues | |||
Region | 77-97 | Disordered | |||
Domain | 213-379 | 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
- Length422
- Mass (Da)46,878
- Last updated2019-11-13 v1
- ChecksumF11ED2B5EE8F41CE
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 77-91 | Polar residues | |||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
SJPP01000002 EMBL· GenBank· DDBJ | TWU09070.1 EMBL· GenBank· DDBJ | Genomic DNA |