Q43157 · RPE_SPIOL
- ProteinRibulose-phosphate 3-epimerase, chloroplastic
- GeneRPE
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids285 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
Fe2+ (UniProtKB | Rhea| CHEBI:29033 )
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )
Note: Binds 1 divalent metal cation per subunit. Active with Co2+, Fe2+, Mn2+ and Zn2+.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
250 μM | ribulose 5-phosphate |
pH Dependence
Optimum pH is 8.5.
Pathway
Carbohydrate biosynthesis; Calvin cycle.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 67 | substrate | ||||
Sequence: S | ||||||
Binding site | 92 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 94 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 94 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 125 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 125 | substrate | ||||
Sequence: H | ||||||
Binding site | 203-206 | substrate | ||||
Sequence: GFGG | ||||||
Active site | 236 | Proton donor | ||||
Sequence: D | ||||||
Binding site | 236 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 236-238 | substrate | ||||
Sequence: DGG | ||||||
Binding site | 258-259 | substrate | ||||
Sequence: GS |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast thylakoid membrane | |
Molecular Function | D-ribulose-phosphate 3-epimerase activity | |
Molecular Function | metal ion binding | |
Biological Process | pentose-phosphate shunt | |
Biological Process | reductive pentose-phosphate cycle |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRibulose-phosphate 3-epimerase, chloroplastic
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > Caryophyllales > Chenopodiaceae > Chenopodioideae > Anserineae > Spinacia
Accessions
- Primary accessionQ43157
Proteomes
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 236 | Almost abolished enzyme activity. | ||||
Sequence: D → A, E, or N |
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-50 | Chloroplast | ||||
Sequence: MSAASLCQSTLQSQINGFCGGLNIRKLQPSTSSPNSLTFTRRKVQTLVKA | ||||||
Chain | PRO_0000025416 | 51-285 | Ribulose-phosphate 3-epimerase, chloroplastic | |||
Sequence: TSRVDKFSKSDIIVSPSILSANFAKLGEQVKAVELAGCDWIHVDVMDGRFVPNITIGPLVVDALRPVTDLPLDVHLMIVEPEQRVPDFIKAGADIVSVHCELASTIHLHRTVNQIKSLGAKAGVVLNPGTPLSTIEYVLDVVDLVLIMSVNPGFGGQSFIESQVKKISDLRKMCVEKGVNPWIEVDGGVTPANAYKVIEAGANALVAGSAVFGAKDYAEAIKGIKASKRPEPVAV |
Interaction
Subunit
Homooctamer.
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length285
- Mass (Da)30,366
- Last updated1996-11-01 v1
- ChecksumED0236FB7B629512
Keywords
- Technical term