PROSITE documentation PDOC00142

Ribulose bisphosphate carboxylase large chain active site

Description:

Ribulose bisphosphate carboxylase (EC 4.1.1.39) (RuBisCO) [1,2] catalyzes the initial step in Calvin's reductive pentose phosphate cycle in plants as well as purple and green bacteria. It consists of a large catalytic unit and a small subunit of undetermined function. In plants, the large subunit is coded by the chloroplastic genome while the small subunit is encoded in the nuclear genome. Molecular activation of RuBisCO by CO2 involves the formation of a carbamate with the epsilon-amino group of a conserved lysine residue. This carbamate is stabilized by a magnesium ion. One of the ligands of the magnesium ion is an aspartic acid residue close to the active site lysine [3]. We developed a pattern which includes both the active site residue and the metal ligand, and which is specific to RuBisCO large chains.

Last update:

November 1995 / Pattern and text revised.

Technical section:

PROSITE method (with tools and information) covered by this documentation:

RUBISCO_LARGE, PS00157Ribulose bisphosphate carboxylase large chain active site  (PATTERN)
Consensus pattern: G-x-[DN]-F-x-K-x-D-E
K is the active site residue] [The second D is a magnesium ligand
Sequences known to belong to this class detected by the pattern: ALL, except for Cheilopleuria biscuspis RuBisCO
Other sequence(s) detected in Swiss-Prot: 1
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Matching PDB structures: 1AUS 1BXN 1EJ7 1RBL ... [ALL]

References:

1 AuthorsMiziorko H.M., Lorimer G.H.
TitleRibulose-1,5-bisphosphate carboxylase-oxygenase.
SourceAnnu. Rev. Biochem. 52:507-535(1983).
PubMed ID6351728
DOI10.1146/annurev.bi.52.070183.002451
2 AuthorsAkazawa T., Takabe T., Kobayashi H.
SourceTrends Biochem. Sci. 9:380-383(1984).
3 AuthorsAndersson I., Knight S., Schneider G., Lindqvist Y., Lundqvist T., Branden C.-I., Lorimer G.H.
SourceNature 337:229-234(1989).

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