Q9MU50 · Q9MU50_9LAMI
- ProteinRibulose bisphosphate carboxylase large chain
- GenerbcL
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids449 (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.
Catalytic activity
- 2 (2R)-3-phosphoglycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O
- D-ribulose 1,5-bisphosphate + O2 = 2-phosphoglycolate + (2R)-3-phosphoglycerate + 2 H+
Cofactor
Note: Binds 1 Mg2+ ion per subunit.
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
Gene names
Encoded on
- Chloroplast
Organism names
- Organism
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > asterids > lamiids > Lamiales > Plantaginaceae > Callitricheae > Callitriche
Accessions
- Primary accessionQ9MU50
Subcellular Location
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 | 15-135 | Ribulose bisphosphate carboxylase large subunit ferrodoxin-like N-terminal | ||||
Sequence: YYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYQIEPVPGEPDQYICYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPVAY | ||||||
Domain | 145-449 | Ribulose bisphosphate carboxylase large subunit C-terminal | ||||
Sequence: GIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRACYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKSQAETGEIKGHYLNATAGTCEEMMKRAIFARELGVPIVMHDYLTGGFTANTSLSHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHSGTVVGKLEGERDITLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLATEGNTIIREACKWSPELAAA |
Sequence similarities
Belongs to the RuBisCO large chain family. Type I subfamily.
Family and domain databases
Sequence
- Sequence statusFragment
- Length449
- Mass (Da)49,658
- Last updated2000-10-01 v1
- ChecksumCBD5B93823911BC3
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: S | ||||||
Non-terminal residue | 449 | |||||
Sequence: A |