Q7YJW4 · RBL_CALFG
- ProteinRibulose bisphosphate carboxylase large chain
- GenerbcL
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids475 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.
Miscellaneous
The basic functional RuBisCO is composed of a large chain homodimer in a 'head-to-tail' conformation. In form I RuBisCO this homodimer is arranged in a barrel-like tetramer with the small subunits forming a tetrameric 'cap' on each end of the 'barrel'.
Catalytic activity
- 2 (2R)-3-phosphoglycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O
- D-ribulose 1,5-bisphosphate + O2 = 2-phosphoglycolate + (2R)-3-phosphoglycerate + 2 H+
Cofactor
Note: Binds 1 Mg2+ ion per subunit.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 123 | substrate; in homodimeric partner | |||
Binding site | 173 | substrate | |||
Active site | 175 | Proton acceptor | |||
Binding site | 177 | substrate | |||
Binding site | 201 | Mg2+ (UniProtKB | ChEBI); via carbamate group | |||
Binding site | 203 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 204 | Mg2+ (UniProtKB | ChEBI) | |||
Active site | 294 | Proton acceptor | |||
Binding site | 295 | substrate | |||
Binding site | 327 | substrate | |||
Site | 334 | Transition state stabilizer | |||
Binding site | 379 | substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Molecular Function | magnesium ion binding | |
Molecular Function | monooxygenase activity | |
Molecular Function | ribulose-bisphosphate carboxylase activity | |
Biological Process | photorespiration | |
Biological Process | reductive pentose-phosphate cycle |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRibulose bisphosphate carboxylase large chain
- EC number
- Short namesRuBisCO large subunit
Gene names
Encoded on
- Chloroplast
Organism names
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Magnoliidae > Laurales > Calycanthaceae > Calycanthus
Accessions
- Primary accessionQ7YJW4
Subcellular Location
PTM/Processing
Features
Showing features for propeptide, modified residue, chain, disulfide bond.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Propeptide | PRO_0000042907 | 1-2 | |||
Modified residue | 3 | N-acetylproline | |||
Chain | PRO_0000042908 | 3-475 | Ribulose bisphosphate carboxylase large chain | ||
Modified residue | 14 | N6,N6,N6-trimethyllysine | |||
Modified residue | 201 | N6-carboxylysine | |||
Disulfide bond | 247 | Interchain; in linked form | |||
Post-translational modification
The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover.
Keywords
- PTM
Interaction
Subunit
Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers.
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length475
- Mass (Da)52,605
- Last updated2003-10-01 v1
- ChecksumDD242D6B895A7949
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ428413 EMBL· GenBank· DDBJ | CAD28729.1 EMBL· GenBank· DDBJ | Genomic DNA |