A0A0H5CC70 · A0A0H5CC70_9PSEU
- ProteinGTP cyclohydrolase-2
- GeneribA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids214 (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 | 53-57 | GTP (UniProtKB | ChEBI) | ||||
Sequence: RVHSE | ||||||
Binding site | 58 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 69 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 71 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 74 | GTP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 97-99 | GTP (UniProtKB | ChEBI) | ||||
Sequence: EGR | ||||||
Binding site | 120 | GTP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Active site | 132 | Proton acceptor | ||||
Sequence: D | ||||||
Active site | 134 | Nucleophile | ||||
Sequence: R | ||||||
Binding site | 155 | GTP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 160 | GTP (UniProtKB | ChEBI) | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | GTP binding | |
Molecular Function | GTP cyclohydrolase II activity | |
Molecular Function | lyase 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 > Actinomycetota > Actinomycetes > Pseudonocardiales > Pseudonocardiaceae
Accessions
- Primary accessionA0A0H5CC70
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 | 12-176 | GTP cyclohydrolase II | ||||
Sequence: VAESNLVTRRGTFRAVAFRLAGHEHMAMVYGKVRLRERVLVRVHSECMTGDIFGAMRCECGEQLNAALDAIVSEGSGVLIYLRGHEGRGIGLVAKVRTHVLQDEQGLDTLDSATSLGLPVDVRDYTPAATVLRHLGVRSVRLMSNNPDKVDALESQGVPVVDRVP |
Sequence similarities
Belongs to the GTP cyclohydrolase II family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length214
- Mass (Da)23,504
- Last updated2015-10-14 v1
- Checksum953696DEB2ACE5A1
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LN850107 EMBL· GenBank· DDBJ | CRK55064.1 EMBL· GenBank· DDBJ | Genomic DNA |