A0A2T0YHQ4 · A0A2T0YHQ4_9MICC
- ProteinGTP cyclohydrolase-2
- GeneribA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids664 (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
- GTP + 4 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + formate + 3 H+ + 2 phosphate
Cofactor
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 | 512-516 | GTP (UniProtKB | ChEBI) | ||||
Sequence: RMHSE | ||||||
Binding site | 517 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 528 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 530 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 533 | GTP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 555-557 | GTP (UniProtKB | ChEBI) | ||||
Sequence: EGR | ||||||
Binding site | 577 | GTP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Active site | 591 | Nucleophile | ||||
Sequence: R | ||||||
Binding site | 612 | GTP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 617 | GTP (UniProtKB | ChEBI) | ||||
Sequence: K |
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 | riboflavin synthase 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 > Micrococcales > Micrococcaceae > Nesterenkonia
Accessions
- Primary accessionA0A2T0YHQ4
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for domain, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-98 | Lumazine-binding | ||||
Sequence: MFTGIVTGLGEVLARRFDPAKGVERLSFSAPGHTAGLGLGGSIAVNGVCVSAVAIEDDQISVELIQETLSRTTLGQLQVGDPLNLERCLPSGARLDGH | ||||||
Repeat | 1-98 | Lumazine-binding | ||||
Sequence: MFTGIVTGLGEVLARRFDPAKGVERLSFSAPGHTAGLGLGGSIAVNGVCVSAVAIEDDQISVELIQETLSRTTLGQLQVGDPLNLERCLPSGARLDGH | ||||||
Repeat | 99-198 | Lumazine-binding | ||||
Sequence: VVQGHVDGLAQLILADPQDGRHRFLISQDLAPYIAEKGSIAINGVSLTVSAVSAPGSSDPFFEVGLIPTTLADTTLGSTGIGAQVNVEVDVLAKYARRML | ||||||
Domain | 99-198 | Lumazine-binding | ||||
Sequence: VVQGHVDGLAQLILADPQDGRHRFLISQDLAPYIAEKGSIAINGVSLTVSAVSAPGSSDPFFEVGLIPTTLADTTLGSTGIGAQVNVEVDVLAKYARRML |
Sequence similarities
Belongs to the GTP cyclohydrolase II family.
In the N-terminal section; belongs to the DHBP synthase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length664
- Mass (Da)70,407
- Last updated2018-07-18 v1
- Checksum153CD73E74B81ABE