A0A7W7GN15 · A0A7W7GN15_9MICC
- ProteinGTP cyclohydrolase-2
- GeneribA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids617 (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 | 468-472 | GTP (UniProtKB | ChEBI) | ||||
Sequence: RVHSE | ||||||
Binding site | 473 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 484 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 486 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 489 | GTP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 511-513 | GTP (UniProtKB | ChEBI) | ||||
Sequence: EGR | ||||||
Binding site | 533 | GTP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Active site | 545 | Proton acceptor | ||||
Sequence: D | ||||||
Active site | 547 | Nucleophile | ||||
Sequence: R | ||||||
Binding site | 568 | GTP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 573 | 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 | 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 > Micrococcus
Accessions
- Primary accessionA0A7W7GN15
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for domain, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-109 | Lumazine-binding | ||||
Sequence: MFTGIITHIGTVVALQQDEQSDTAVLVLDTAGAAAGLPEGGSLAVNGVCLTSVPQDADPSAPDSAPDDGLFRADLMGQTLRMTALGELSPGDRVNLERCLRPTDHIDGH | ||||||
Repeat | 1-109 | Lumazine-binding | ||||
Sequence: MFTGIITHIGTVVALQQDEQSDTAVLVLDTAGAAAGLPEGGSLAVNGVCLTSVPQDADPSAPDSAPDDGLFRADLMGQTLRMTALGELSPGDRVNLERCLRPTDHIDGH | ||||||
Domain | 110-211 | Lumazine-binding | ||||
Sequence: IVQGHVDGVGTVAQVADEGAWRRVRVAVPDELARVIPAQGAITVQGVSLTVTAVSAPSQRRHWFEVGLIPATLEATVLGALAPGDRVNLETDVMARYAERMT | ||||||
Repeat | 110-211 | Lumazine-binding | ||||
Sequence: IVQGHVDGVGTVAQVADEGAWRRVRVAVPDELARVIPAQGAITVQGVSLTVTAVSAPSQRRHWFEVGLIPATLEATVLGALAPGDRVNLETDVMARYAERMT |
Sequence similarities
Belongs to the GTP cyclohydrolase II family.
In the N-terminal section; belongs to the DHBP synthase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length617
- Mass (Da)64,562
- Last updated2021-06-02 v1
- ChecksumB364191667E1A242
Keywords
- Technical term