Q59462 · RBL2_HYDMR
- ProteinRibulose bisphosphate carboxylase
- GenecbbM
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids463 (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 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.
Kinetics
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
0.003 μmol/min/mg | with CO2 as substrate, expressed in E.coli |
The CO2/O2 specificity factor (tau) is 14.8.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 116 | substrate; in homodimeric partner | ||||
Sequence: N | ||||||
Active site | 171 | Proton acceptor | ||||
Sequence: K | ||||||
Binding site | 173 | substrate | ||||
Sequence: K | ||||||
Binding site | 196 | Mg2+ (UniProtKB | ChEBI); via carbamate group | ||||
Sequence: K | ||||||
Binding site | 198 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 199 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 294 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 295 | substrate | ||||
Sequence: R | ||||||
Binding site | 328 | substrate | ||||
Sequence: H | ||||||
Site | 336 | Transition state stabilizer | ||||
Sequence: K | ||||||
Binding site | 375 | 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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Thiotrichales > Piscirickettsiaceae > Hydrogenovibrio
Accessions
- Primary accessionQ59462
- Secondary accessions
PTM/Processing
Features
Showing features for initiator methionine, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000062662 | 2-463 | Ribulose bisphosphate carboxylase | |||
Sequence: DQSNRYADLTLTEEKLVADGNHLLVAYRLKPAAGYGFLEVAAHVAAESSTGTNVEVSTTDDFTRGVDALVYEIDEAAFGDKGGLMKIAYPVDLFDPNLIDGHYNVSHMWSLILGNNQGMGDHEGLRMLDFLVPEKMVKRFDGPATDISDLWKVLGRPEVDGGYIAGTIIKPKLGLRPEPFAKACYDFWLGGDFIKNDEPQANQNFCPMEVVIPKVAEAMDRAQQATGQAKLFSANVTADFHEEMIKRGEYVLGEFAKYGNEKHVAFLVDGFVTGPAGVTTSRRAFPDTYLHFHRAGHGAVTSYKSPMGMDPLCYMKLARLMGASGIHTGTMGYGKMEGHNDERVLAYMLERDECQGPYFYQKWYGMKPTTPIISGGMDALRLPGFFENLGHGNVINTCGGGSFGHIDSPAAGGISLGQAYACWKTGAEPIEAPREFARAFESFPGDADKIFPGWREKLGVHK | ||||||
Modified residue | 196 | N6-carboxylysine | ||||
Sequence: K |
Expression
Induction
mRNA expression is constant at all CO2 concentrations tested, however more protein accumulates at 15% and 2% CO2 than at 0.15% and 0.03% CO2 (at protein level).
Interaction
Structure
Sequence
- Sequence statusComplete
- Length463
- Mass (Da)50,729
- Last updated2007-01-23 v3
- ChecksumA7F8E289FF92E996
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 379 | in Ref. 3; BAD15326 | ||||
Sequence: D → N | ||||||
Sequence conflict | 422 | in Ref. 3; BAD15326 | ||||
Sequence: A → D | ||||||
Sequence conflict | 429 | in Ref. 3; BAD15326 | ||||
Sequence: E → D | ||||||
Sequence conflict | 433-435 | in Ref. 3; BAD15326 | ||||
Sequence: APR → YAKEHP |
Keywords
- Technical term