P31194 · RBL_MALDO
- ProteinRibulose bisphosphate carboxylase large chain
- GenerbcL
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids
- 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 (By similarity).
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' (By similarity).
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+
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Molecular Function | monooxygenase activity | |
Molecular Function | ribulose-bisphosphate carboxylase activity | |
Biological Process | photorespiration | |
Biological Process | reductive pentose-phosphate cycle |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRibulose bisphosphate carboxylase large chain
- EC number
- Short namesRuBisCO large subunit
Gene names
Encoded on
- Chloroplast
Organism names
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Rosales > Rosaceae > Amygdaloideae > Maleae > Malus
Accessions
- Primary accessionP31194
Subcellular Location
PTM/Processing
Features
Showing features for propeptide, modified residue, chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Propeptide | PRO_0000031297 | 1-2 | |||
Modified residue | 3 | N-acetylproline | |||
Chain | PRO_0000031298 | 3-53 | Ribulose bisphosphate carboxylase large chain | ||
Modified residue | 14 | N6,N6,N6-trimethyllysine | |||
Keywords
- PTM
Interaction
Subunit
Heterohexadecamer of 8 large chains and 8 small chains.
Structure
Family & Domains
Sequence similarities
Belongs to the RuBisCO large chain family. Type I subfamily.
Family and domain databases
Sequence
- Sequence statusFragment
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length53
- Mass (Da)5,854
- Last updated1993-07-01 v1
- MD5 ChecksumB0F284FA33C7AF41D0402354D32E09A2
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Non-terminal residue | 53 | ||||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X69750 EMBL· GenBank· DDBJ | CAA49405.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X69749 EMBL· GenBank· DDBJ | CAA49404.1 EMBL· GenBank· DDBJ | Genomic DNA |