UniProt functional annotation for P00877

UniProt code: P00877.

Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii).
Taxonomy: Eukaryota; Viridiplantae; Chlorophyta; Chlorophyceae; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
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 3-phospho-D-glycerate + 2 H(+) = D-ribulose 1,5-bisphosphate + CO(2) + H(2)O.
Catalytic activity: 3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O(2).
Cofactor: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 1 Mg(2+) ion per subunit.;
Subunit: Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers. {ECO:0000269|PubMed:11641402, ECO:0000269|PubMed:11866526}.
Subcellular location: Plastid, chloroplast.
Ptm: The disulfide bond which can form between Cys-247 in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover (By similarity). The disulfide bond reported in 1IR2 may be the result of oxidation during crystallization. {ECO:0000250}.
Ptm: The electron density found in the position of Thr-471 (PubMed:11866526 only) suggests it is either O-methylthreonine, or Ile, which may be produced by RNA editing.
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".
Similarity: Belongs to the RuBisCO large chain family. Type I subfamily. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.