B2SYZ9 · B2SYZ9_PARPJ
- ProteinRibulose-phosphate 3-epimerase
- Generpe
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids238 (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 | 20 | substrate | ||||
Sequence: S | ||||||
Binding site | 45 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 47 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 47 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 78 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 78 | substrate | ||||
Sequence: H | ||||||
Binding site | 154-157 | substrate | ||||
Sequence: GFGG | ||||||
Active site | 191 | Proton donor | ||||
Sequence: D | ||||||
Binding site | 191 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 191-193 | substrate | ||||
Sequence: DGG | ||||||
Binding site | 193 | substrate | ||||
Sequence: G | ||||||
Binding site | 213-214 | substrate | ||||
Sequence: GS |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | D-ribulose-phosphate 3-epimerase activity | |
Molecular Function | metal ion binding | |
Biological Process | pentose catabolic process | |
Biological Process | pentose-phosphate shunt, non-oxidative branch |
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 > Burkholderiaceae > Paraburkholderia
Accessions
- Primary accessionB2SYZ9
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length238
- Mass (Da)25,893
- Last updated2008-07-01 v1
- ChecksumF89449C3F8D3E398
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP001052 EMBL· GenBank· DDBJ | ACD17884.1 EMBL· GenBank· DDBJ | Genomic DNA |