A0A1M6NHT1 · A0A1M6NHT1_PARC5
- ProteinRibulose-phosphate 3-epimerase
- Generpe
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids219 (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 | 7 | substrate | ||||
Sequence: S | ||||||
Binding site | 32 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 34 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 34 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 65 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 65 | substrate | ||||
Sequence: H | ||||||
Binding site | 141-144 | substrate | ||||
Sequence: GFGG | ||||||
Active site | 174 | Proton donor | ||||
Sequence: D | ||||||
Binding site | 174 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 174-176 | substrate | ||||
Sequence: DGG | ||||||
Binding site | 176 | substrate | ||||
Sequence: G | ||||||
Binding site | 196-197 | 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 > Bacillota > Clostridia > Peptostreptococcales > Caminicellaceae > Paramaledivibacter
Accessions
- Primary accessionA0A1M6NHT1
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length219
- Mass (Da)23,727
- Last updated2017-03-15 v1
- Checksum385B5B78C9B308CB
Keywords
- Technical term