P00875 · RBL_SPIOL
- ProteinRibulose bisphosphate carboxylase large chain
- GenerbcL
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids475 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 (Probable) (PubMed:2928307).
Both reactions occur simultaneously and in competition at the same active site (Probable). Binds to abscisic acid (ABA) which has weakly inhibits carboxylation and more strongly inhibits enzyme activation (PubMed:26197050).
Both reactions occur simultaneously and in competition at the same active site (Probable). Binds to abscisic acid (ABA) which has weakly inhibits carboxylation and more strongly inhibits enzyme activation (PubMed:26197050).
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+ = CO2 + D-ribulose 1,5-bisphosphate + H2O
- D-ribulose 1,5-bisphosphate + O2 = (2R)-3-phosphoglycerate + 2-phosphoglycolate + 2 H+
Cofactor
Activity regulation
Abscisic acid (ABA) causes weak inhibition of RuBisCO catalytic activity, but more potent inhibition of RuBisCO activation.
Features
Showing features for site, binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 14 | Not N6-methylated | ||||
Sequence: K | ||||||
Binding site | 65 | substrate | ||||
Sequence: T | ||||||
Binding site | 123 | substrate; in homodimeric partner | ||||
Sequence: N | ||||||
Binding site | 173 | substrate | ||||
Sequence: T | ||||||
Active site | 175 | Proton acceptor | ||||
Sequence: K | ||||||
Binding site | 177 | substrate | ||||
Sequence: K | ||||||
Binding site | 201 | Mg2+ (UniProtKB | ChEBI); via carbamate group | ||||
Sequence: K | ||||||
Binding site | 203 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 204 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 204 | substrate | ||||
Sequence: E | ||||||
Active site | 294 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 294 | substrate | ||||
Sequence: H | ||||||
Binding site | 295 | substrate | ||||
Sequence: R | ||||||
Binding site | 327 | substrate | ||||
Sequence: H | ||||||
Binding site | 334 | substrate | ||||
Sequence: K | ||||||
Site | 334 | Transition state stabilizer | ||||
Sequence: K | ||||||
Binding site | 379 | substrate | ||||
Sequence: S | ||||||
Binding site | 381 | substrate | ||||
Sequence: G | ||||||
Binding site | 403 | substrate | ||||
Sequence: G | ||||||
Binding site | 404 | substrate | ||||
Sequence: G |
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
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameRibulose bisphosphate carboxylase large chain
- EC number
- Short namesRuBisCO large subunit
Gene names
Encoded on
- Chloroplast
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > Caryophyllales > Chenopodiaceae > Chenopodioideae > Anserineae > Spinacia
Accessions
- Primary accessionP00875
- Secondary accessions
Proteomes
Subcellular Location
Phenotypes & Variants
Protein family/group databases
PTM/Processing
Features
Showing features for propeptide, modified residue, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Propeptide | PRO_0000031415 | 1-2 | ||||
Sequence: MS | ||||||
Modified residue | 3 | N-acetylproline | ||||
Sequence: P | ||||||
Chain | PRO_0000031416 | 3-475 | Ribulose bisphosphate carboxylase large chain | |||
Sequence: PQTETKASVEFKAGVKDYKLTYYTPEYETLDTDILAAFRVSPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTNLDRYKGRCYHIEPVAGEENQYICYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPVAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYLNATAGTCEDMMKRAVFARELGVPIVMHDYLTGGFTANTTLSHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHIHSGTVVGKLEGERDITLGFVDLLRDDYTEKDRSRGIYFTQSWVSTPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNTIIREATKWSPELAAACEVWKEIKFEFPAMDTV | ||||||
Modified residue | 201 | N6-carboxylysine | ||||
Sequence: K | ||||||
Disulfide bond | 247 | Interchain; in linked form | ||||
Sequence: C |
Post-translational modification
The disulfide bond which can form between Cys-247 in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover (By similarity).
The disulfide bonds reported in 1RBO may be the result of oxidation during crystallization
The disulfide bonds reported in 1RBO may be the result of oxidation during crystallization
Keywords
- PTM
PTM databases
Structure
Family & Domains
Sequence similarities
Belongs to the RuBisCO large chain family. Type I subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length475
- Mass (Da)52,740
- Last updated1986-07-21 v1
- Checksum484FFFFD36BB1238
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 12 | in Ref. 2; CAB88737 | ||||
Sequence: E → G |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
V00168 EMBL· GenBank· DDBJ | CAA23473.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ400848 EMBL· GenBank· DDBJ | CAB88737.1 EMBL· GenBank· DDBJ | Genomic DNA |