P04718 · RBL2_RHORU
- ProteinRibulose bisphosphate carboxylase
- GenecbbM
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids466 (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. 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 contrast to form I RuBisCO, the form II RuBisCO are composed solely of large subunits (By similarity).
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 | 111 | substrate; in homodimeric partner | ||||
Sequence: N | ||||||
Active site | 166 | Proton acceptor | ||||
Sequence: K | ||||||
Binding site | 168 | substrate | ||||
Sequence: K | ||||||
Binding site | 191 | Mg2+ (UniProtKB | ChEBI); via carbamate group | ||||
Sequence: K | ||||||
Binding site | 193 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 194 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 287 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 288 | substrate | ||||
Sequence: R | ||||||
Binding site | 321 | substrate | ||||
Sequence: H | ||||||
Site | 329 | Transition state stabilizer | ||||
Sequence: K | ||||||
Binding site | 368 | substrate | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | magnesium ion binding | |
Molecular Function | monooxygenase activity | |
Molecular Function | ribulose-bisphosphate carboxylase activity | |
Biological Process | reductive pentose-phosphate cycle |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRibulose bisphosphate carboxylase
- EC number
- Short namesRuBisCO
Gene names
Organism names
- Organism
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Rhodospirillales > Rhodospirillaceae > Rhodospirillum
Accessions
- Primary accessionP04718
- Secondary accessions
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 193 | Loss of activity, decreased affinity for Mg2+. | ||||
Sequence: D → N |
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000062666 | 1-466 | Ribulose bisphosphate carboxylase | |||
Sequence: MDQSSRYVNLALKEEDLIAGGEHVLCAYIMKPKAGYGYVATAAHFAAESSTGTNVEVCTTDDFTRGVDALVYEVDEARELTKIAYPVALFHRNITDGKAMIASFLTLTMGNNQGMGDVEYAKMHDFYVPEAYRALFDGPSVNISALWKVLGRPEVDGGLVVGTIIKPKLGLRPKPFAEACHAFWLGGDFIKNDEPQGNQPFAPLRDTIALVADAMRRAQDETGEAKLFSANITADDPFEIIARGEYVLETFGENASHVALLVDGYVAGAAAITTARRRFPDNFLHYHRAGHGAVTSPQSKRGYTAFVHCKMARLQGASGIHTGTMGFGKMEGESSDRAIAYMLTQDEAQGPFYRQSWGGMKACTPIISGGMNALRMPGFFENLGNANVILTAGGGAFGHIDGPVAGARSLRQAWQAWRDGVPVLDYAREHKELARAFESFPGDADQIYPGWRKALGVEDTRSALPA | ||||||
Modified residue | 191 | N6-carboxylysine | ||||
Sequence: K |
Structure
Sequence
- Sequence statusComplete
- Length466
- Mass (Da)50,504
- Last updated1987-08-13 v1
- Checksum37D8C0076CAF7D54
Keywords
- Technical term