Q5SCV9 · RBL_HUPLU
- ProteinRibulose bisphosphate carboxylase large chain
- GenerbcL
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids475 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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 > Lycopodiopsida > Lycopodiales > Lycopodiaceae > Huperzioideae > Huperzia
Accessions
- Primary accessionQ5SCV9
Subcellular Location
PTM/Processing
Features
Showing features for propeptide, modified residue, chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Propeptide | PRO_0000042909 | 1-2 | |||
Modified residue | 3 | N-acetylproline | |||
Chain | PRO_0000042910 | 3-475 | Ribulose bisphosphate carboxylase large chain | ||
Modified residue | 14 | N6,N6,N6-trimethyllysine | |||
Modified residue | 201 | N6-carboxylysine | |||
Keywords
- PTM
Interaction
Subunit
Heterohexadecamer of 8 large chains and 8 small chains.
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length475
- Mass (Da)52,730
- Last updated2004-12-21 v1
- Checksum5827335C03B19382
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY660566 EMBL· GenBank· DDBJ | AAT80717.1 EMBL· GenBank· DDBJ | Genomic DNA |