A0A2I9CSJ6 · A0A2I9CSJ6_9DEIO
- ProteinRibulose-phosphate 3-epimerase
- Generpe
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids225 (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 | 8 | substrate | ||||
Sequence: S | ||||||
Binding site | 33 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 35 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 35 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 66 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 66 | substrate | ||||
Sequence: H | ||||||
Binding site | 142-145 | substrate | ||||
Sequence: GFGG | ||||||
Active site | 175 | Proton donor | ||||
Sequence: D | ||||||
Binding site | 175 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 175-177 | substrate | ||||
Sequence: DGG | ||||||
Binding site | 177 | substrate | ||||
Sequence: G | ||||||
Binding site | 197-198 | 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
- Organism
- Strain
- Taxonomic lineageBacteria > Deinococcota > Deinococci > Deinococcales > Deinococcaceae > Deinococcus
Accessions
- Primary accessionA0A2I9CSJ6
Proteomes
Structure
Sequence
- Sequence statusComplete
- Length225
- Mass (Da)23,829
- Last updated2018-03-28 v1
- ChecksumAF128577E4821BE9
Keywords
- Technical term