F1VYJ2 · F1VYJ2_9BURK
- ProteinRibulose-phosphate 3-epimerase
- Generpe
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids223 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.
Catalytic activity
- D-ribulose 5-phosphate = D-xylulose 5-phosphate
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 divalent metal cation per subunit.
Pathway
Carbohydrate degradation.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 11 | substrate | ||||
Sequence: S | ||||||
Binding site | 36 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 38 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 38 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 69 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 69 | substrate | ||||
Sequence: H | ||||||
Binding site | 145-148 | substrate | ||||
Sequence: GFGG | ||||||
Active site | 178 | Proton donor | ||||
Sequence: D | ||||||
Binding site | 178 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 178-180 | substrate | ||||
Sequence: DGG | ||||||
Binding site | 180 | substrate | ||||
Sequence: G | ||||||
Binding site | 200-201 | substrate | ||||
Sequence: GS |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | D-ribulose-phosphate 3-epimerase activity | |
Molecular Function | metal ion binding | |
Biological Process | pentose catabolic process | |
Biological Process | pentose-phosphate shunt |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRibulose-phosphate 3-epimerase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Oxalobacteraceae
Accessions
- Primary accessionF1VYJ2
Proteomes
Structure
Sequence
- Sequence statusComplete
- Length223
- Mass (Da)23,865
- Last updated2011-05-31 v1
- Checksum18B84BDC88554BFD
Keywords
- Technical term