A0A384L6B3 · A0A384L6B3_PLAKH
- ProteinRibulose-phosphate 3-epimerase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids227 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
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.
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 | 70 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 70 | substrate | ||||
Sequence: H | ||||||
Binding site | 150-153 | substrate | ||||
Sequence: GFGG | ||||||
Active site | 179 | Proton donor | ||||
Sequence: D | ||||||
Binding site | 179 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 181 | substrate | ||||
Sequence: G | ||||||
Binding site | 201-202 | substrate | ||||
Sequence: GT |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | D-ribulose-phosphate 3-epimerase activity | |
Molecular Function | metal ion binding | |
Biological Process | carbohydrate metabolic 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
- Organism
- Strain
- Taxonomic lineageEukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Haemosporida > Plasmodiidae > Plasmodium > Plasmodium (Plasmodium)
Accessions
- Primary accessionA0A384L6B3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length227
- Mass (Da)25,566
- Last updated2018-11-07 v1
- Checksum6CFE0AD317630927
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AM910996 EMBL· GenBank· DDBJ | CAA9990987.1 EMBL· GenBank· DDBJ | Genomic DNA |