A0A248SPX9 · A0A248SPX9_9MAGN
- ProteinRibulose bisphosphate carboxylase large chain
- GenerbcL
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- 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+ = CO2 + D-ribulose 1,5-bisphosphate + H2O
- D-ribulose 1,5-bisphosphate + O2 = (2R)-3-phosphoglycerate + 2-phosphoglycolate + 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 | ||||
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 | ||||||
Active site | 294 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 295 | substrate | ||||
Sequence: R | ||||||
Binding site | 327 | substrate | ||||
Sequence: H | ||||||
Site | 334 | Transition state stabilizer | ||||
Sequence: K | ||||||
Binding site | 379 | substrate | ||||
Sequence: S |
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
- Organism
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Ranunculales > Circaeasteraceae > Circaeaster
Accessions
- Primary accessionA0A248SPX9
Subcellular Location
PTM/Processing
Features
Showing features for modified residue, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 14 | N6,N6,N6-trimethyllysine | ||||
Sequence: K | ||||||
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 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
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 24-144 | Ribulose bisphosphate carboxylase large subunit ferrodoxin-like N-terminal | ||||
Sequence: YYTPDYQTLETDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTNLDRYKGRCYNIEPVAGEDNQYICYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAY | ||||||
Domain | 154-462 | Ribulose bisphosphate carboxylase large subunit C-terminal | ||||
Sequence: GIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYEVLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYLNATAGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHSGTVVGKLEGEREITLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNEIIRQACKWSPELASACEIW |
Sequence similarities
Belongs to the RuBisCO large chain family. Type I subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length475
- Mass (Da)52,759
- Last updated2017-11-22 v1
- Checksum1E112390CDB2D71F
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KY908400 EMBL· GenBank· DDBJ | ASV47674.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
MT228704 EMBL· GenBank· DDBJ | QKI32435.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
MT228706 EMBL· GenBank· DDBJ | QKI32605.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
MT228708 EMBL· GenBank· DDBJ | QKI32775.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
MT228709 EMBL· GenBank· DDBJ | QKI32860.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
MT228710 EMBL· GenBank· DDBJ | QKI32945.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
MT228711 EMBL· GenBank· DDBJ | QKI33030.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
MT228712 EMBL· GenBank· DDBJ | QKI33115.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
MT228713 EMBL· GenBank· DDBJ | QKI33200.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
MT228714 EMBL· GenBank· DDBJ | QKI33285.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
MT228715 EMBL· GenBank· DDBJ | QKI33370.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
MT228716 EMBL· GenBank· DDBJ | QKI33455.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
MT228717 EMBL· GenBank· DDBJ | QKI33540.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
MT228718 EMBL· GenBank· DDBJ | QKI33625.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
MT228720 EMBL· GenBank· DDBJ | QKI33795.1 EMBL· GenBank· DDBJ | Genomic DNA |