A2XEX2 · F16P1_ORYSI
- ProteinFructose-1,6-bisphosphatase, chloroplastic
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids406 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Catalyzes the irreversible reaction from fructose-1,6-bisphosphate to fructose-6-phosphate and inorganic phosphate, to regenerate the primary CO2 acceptor molecule, ribulose-1,5-bisphosphate (Probable). Involved in the regulation of photosynthetic performance and sucrose synthesis (Ref.2).
Miscellaneous
In plants there are two FBPase isozymes: one in the cytosol and the other in the chloroplast.
Catalytic activity
- beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Cofactor
Note: Binds 3 Mg2+ ions per subunit.
Activity regulation
Inhibited by sodium chloride.
Pathway
Carbohydrate biosynthesis; Calvin cycle.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 128 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 157 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 157 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 178 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 178 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 180 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 181 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 181-184 | substrate | ||||
Sequence: DGSS | ||||||
Binding site | 286 | substrate | ||||
Sequence: N | ||||||
Binding site | 318 | substrate | ||||
Sequence: Y | ||||||
Binding site | 336 | substrate | ||||
Sequence: Y | ||||||
Binding site | 338 | substrate | ||||
Sequence: Y | ||||||
Binding site | 348 | substrate | ||||
Sequence: K | ||||||
Binding site | 354 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast stroma | |
Cellular Component | cytosol | |
Molecular Function | fructose 1,6-bisphosphate 1-phosphatase activity | |
Molecular Function | metal ion binding | |
Biological Process | fructose 1,6-bisphosphate metabolic process | |
Biological Process | fructose 6-phosphate metabolic process | |
Biological Process | fructose metabolic process | |
Biological Process | gluconeogenesis | |
Biological Process | reductive pentose-phosphate cycle | |
Biological Process | sucrose biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFructose-1,6-bisphosphatase, chloroplastic
- EC number
- Short namesFBPase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa
Accessions
- Primary accessionA2XEX2
- Secondary accessions
Proteomes
Genome annotation databases
Subcellular Location
PTM/Processing
Features
Showing features for transit peptide, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-47 | Chloroplast | ||||
Sequence: MAAAATTSSHLLLLSRQQAAASLQCGLSFRRQPGRLAGGSSAPSVRC | ||||||
Chain | PRO_0000438734 | 48-406 | Fructose-1,6-bisphosphatase, chloroplastic | |||
Sequence: MAAVDTASAPAATEASKKSSYEITTLTTWLLKQEQAGTIDGEMTIVLASISTACKQIASLVQRAPISNLTGVQGAVNVQGEDQKKLDVVSNEVFSNCLKSSGRTGVIASEEEDVPVAVEESYSGNYIVVFDPLDGSSNIDAAVSTGSIFGIYSPNDECLADIADDQNLDQVEQRCIVSVCQPGSNLLAAGYCMYSSSVIFVLTIGTGVYVFTLDPMYGEFVLTQEKVQIPKAGKIYAFNEGNYALWDDKLKSYMDSLKEPGPSGKPYSARYIGSLVGDFHRTLLYGGIYGYPRDQKSKNGKLRLLYECAPMSFIVEQAGGKGSDGHQRILDIMPTEIHQRVPLYIGSVEEVEKVEKFLA | ||||||
Disulfide bond | 222↔227 | Redox-active (light-modulated) | ||||
Sequence: CIVSVC |
Keywords
- PTM
Expression
Induction
Light activation through pH changes, Mg2+ levels and also by light-modulated reduction of essential disulfide groups via the ferredoxin-thioredoxin f system.
Interaction
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length406
- Mass (Da)43,604
- Last updated2007-03-20 v1
- Checksum1665BB680EC06069
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 343 | in Ref. 2; ABY75186 | ||||
Sequence: K → R |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CM000128 EMBL· GenBank· DDBJ | EAY89382.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CM000128 EMBL· GenBank· DDBJ | EAY89383.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
EU370973 EMBL· GenBank· DDBJ | ABY75186.1 EMBL· GenBank· DDBJ | mRNA |