{PDOC00142}
{PS00157; RUBISCO_LARGE}
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* Ribulose bisphosphate carboxylase large chain active site *
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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.

-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.
-Last update: November 1995 / Pattern and text revised.

[ 1] Miziorko H.M., Lorimer G.H.
     "Ribulose-1,5-bisphosphate carboxylase-oxygenase."
     Annu. Rev. Biochem. 52:507-535(1983).
     PubMed=6351728; DOI=10.1146/annurev.bi.52.070183.002451
[ 2] Akazawa T., Takabe T., Kobayashi H.
     Trends Biochem. Sci. 9:380-383(1984).
[ 3] Andersson I., Knight S., Schneider G., Lindqvist Y., Lundqvist T.,
     Branden C.-I., Lorimer G.H.
     Nature 337:229-234(1989).

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