O93627 · RBL_THEKO
- ProteinRibulose bisphosphate carboxylase
- GenerbcL
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids444 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the addition of molecular CO2 and H2O to ribulose 1,5-bisphosphate (RuBP), generating two molecules of 3-phosphoglycerate (3-PGA) (PubMed:10512715, PubMed:9988755).
Functions in an archaeal AMP degradation pathway, together with AMP phosphorylase and R15P isomerase (PubMed:17303759).
Functions in an archaeal AMP degradation pathway, together with AMP phosphorylase and R15P isomerase (PubMed:17303759).
Miscellaneous
Because the Archaea possessing a type III RuBisCO are all anaerobic, it is most likely that only the carboxylase activity of RuBisCO, and not the competitive oxygenase activity (by which RuBP reacts with O2 to form one molecule of 3-phosphoglycerate and one molecule of 2-phosphoglycolate), is biologically relevant in these strains.
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.
Temperature Dependence
Optimum temperature is 90 degrees Celsius (PubMed:9988755).
Highly thermostable, has a half-life of 220 minutes at 90 degrees Celsius (PubMed:9988755).
Highly thermostable, has a half-life of 220 minutes at 90 degrees Celsius (PubMed:9988755).
Features
Showing features for active site, binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 163 | Proton acceptor | ||||
Sequence: K | ||||||
Binding site | 165 | substrate | ||||
Sequence: K | ||||||
Binding site | 189 | Mg2+ (UniProtKB | ChEBI); via carbamate group | ||||
Sequence: K | ||||||
Binding site | 191 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 192 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 281 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 282 | substrate | ||||
Sequence: R | ||||||
Binding site | 314 | substrate | ||||
Sequence: H | ||||||
Site | 322 | Transition state stabilizer | ||||
Sequence: K | ||||||
Binding site | 367-369 | substrate | ||||
Sequence: SGG | ||||||
Binding site | 389-392 | substrate | ||||
Sequence: QLGG |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | magnesium ion binding | |
Molecular Function | oxidoreductase activity | |
Molecular Function | ribulose-bisphosphate carboxylase activity | |
Biological Process | AMP catabolic process | |
Biological Process | carbon fixation |
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
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Thermococci > Thermococcales > Thermococcaceae > Thermococcus
Accessions
- Primary accessionO93627
Proteomes
Phenotypes & Variants
Disruption phenotype
Cells lacking this gene show a slight decrease in growth as compared to the wild-type when they are grown in nutrient-rich medium.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 63 | Decrease in activity and in thermostability. Large decrease in activity; forms dimers; when associated with S-66 and S-69. | ||||
Sequence: E → S | ||||||
Mutagenesis | 66 | Large decrease in activity and in thermostability. Large decrease in activity; forms dimers; when associated with S-63 and S-69. | ||||
Sequence: R → S | ||||||
Mutagenesis | 69 | Slight decrease in activity; no change in thermostability. Large decrease in activity; forms dimers; when associated with S-63 and S-66. | ||||
Sequence: D → S |
PTM/Processing
Features
Showing features for initiator methionine, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000062678 | 2-444 | Ribulose bisphosphate carboxylase | |||
Sequence: VEKFDTIYDYYVDKGYEPSKKRDIIAVFRVTPAEGYTIEQAAGAVAAESSTGTWTTLYPWYEQERWADLSAKAYDFHDMGDGSWIVRIAYPFHAFEEANLPGLLASIAGNIFGMKRVKGLRLEDLYFPEKLIREFDGPAFGIEGVRKMLEIKDRPIYGVVPKPKVGYSPEEFEKLAYDLLSNGADYMKDDENLTSPWYNRFEERAEIMAKIIDKVENETGEKKTWFANITADLLEMEQRLEVLADLGLKHAMVDVVITGWGALRYIRDLAADYGLAIHGHRAMHAAFTRNPYHGISMFVLAKLYRLIGIDQLHVGTAGAGKLEGGKWDVIQNARILRESHYKPDENDVFHLEQKFYSIKAAFPTSSGGLHPGNIQPVIEALGTDIVLQLGGGTLGHPDGPAAGARAVRQAIDAIMQGIPLDEYAKTHKELARALEKWGHVTPV | ||||||
Modified residue | 189 | N6-carboxylysine | ||||
Sequence: K |
Expression
Induction
Up-regulated by nucleosides (at protein level).
Interaction
Subunit
Homodecamer, consisting of five dimer units which form a ring-like pentagonal structure. This arrangement is essential for its high thermostability (PubMed:12070156).
In contrast to form I RuBisCO, the form III RuBisCO is composed solely of large subunits (PubMed:9988755).
In contrast to form I RuBisCO, the form III RuBisCO is composed solely of large subunits (PubMed:9988755).
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length444
- Mass (Da)49,713
- Last updated2007-01-23 v5
- Checksum6E3AFF37367DD7FE
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB018555 EMBL· GenBank· DDBJ | BAA33863.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP006878 EMBL· GenBank· DDBJ | BAD86479.1 EMBL· GenBank· DDBJ | Genomic DNA |