Q59458 · RBL1A_HYDMR
- ProteinRibulose bisphosphate carboxylase large chain 1
- GenecbbL1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids472 (go to sequence)
- Protein existenceEvidence at protein level
- 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. 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.
Kinetics
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
1.2 μmol/min/mg | with CO2 as substrate, expressed in E.coli |
The CO2/O2 specificity factor (tau) is 26.6.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 115 | substrate; in homodimeric partner | ||||
Sequence: N | ||||||
Binding site | 165 | substrate | ||||
Sequence: T | ||||||
Active site | 167 | Proton acceptor | ||||
Sequence: K | ||||||
Binding site | 169 | substrate | ||||
Sequence: K | ||||||
Binding site | 193 | Mg2+ (UniProtKB | ChEBI); via carbamate group | ||||
Sequence: K | ||||||
Binding site | 195 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 196 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 286 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 287 | substrate | ||||
Sequence: R | ||||||
Binding site | 319 | substrate | ||||
Sequence: H | ||||||
Site | 326 | Transition state stabilizer | ||||
Sequence: K | ||||||
Binding site | 371 | 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 large chain 1
- EC number
- Short namesRuBisCO large subunit 1
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Thiotrichales > Piscirickettsiaceae > Hydrogenovibrio
Accessions
- Primary accessionQ59458
- Secondary accessions
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000062624 | 1-472 | Ribulose bisphosphate carboxylase large chain 1 | |||
Sequence: MAKTYNAGVKEYRETYWMPEYEPKDSDFLACFKVVPQPGVPREEIAAAVAAESSTGTWTTVWTDLLTDLDYYKGRAYRIEDVPGDDSAFYAFIAYPIDLFEEGSIVSVMTSLVGNVFGFKALRSIRLEDIRFPLAYVMTCGGPPHGIQVERDKMDKYGRPMLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVTSQPFMRWRDRFLFCQDAIEKAQDETGERTGHYLNATAGTPEEMYERAEFAKEIGSPIVMHDFLTGGLTANTGLANYCRKNGLLLHIHRAMHGVIDRNPLHGIHFRVLSKVLRLSGGDHLHSGTVVGKLEGDRGSDLGWIDIMRDSFIAEDRSRGIMFDQDFGEMPGVIPVASGGIHVWHMPALVAIFGDDSVLQFGGGTIGHPWGNAVGAAVNLVALEACVQARNEGQEIEKNGKEILTNDGKHSPELKIAMETWKEIKFEFDTVDKLDLSHK | ||||||
Modified residue | 193 | N6-carboxylysine | ||||
Sequence: K |
Expression
Induction
Both mRNA and protein accumulate at 2% and 0.03% CO2, but not at 15% or 0.15% CO2 (at protein level).
Interaction
Subunit
Heterohexadecamer of 8 large chains and 8 small chains.
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length472
- Mass (Da)52,488
- Last updated1996-11-01 v1
- Checksum71FCAE86F7CF2530
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 298 | in Ref. 2; BAD15307 | ||||
Sequence: L → M | ||||||
Sequence conflict | 332-334 | in Ref. 2; BAD15307 | ||||
Sequence: GSD → EAT | ||||||
Sequence conflict | 399 | in Ref. 2; BAD15307 | ||||
Sequence: I → L | ||||||
Sequence conflict | 407 | in Ref. 2; BAD15307 | ||||
Sequence: V → A | ||||||
Sequence conflict | 411-413 | in Ref. 2; BAD15307 | ||||
Sequence: VNL → ANR | ||||||
Sequence conflict | 440-441 | in Ref. 2; BAD15307 | ||||
Sequence: DG → AA |