{PDOC00490} {PS00567; PHOSPHORIBULOKINASE} {BEGIN} ********************************* * Phosphoribulokinase signature * ********************************* Phosphoribulokinase (EC 2.7.1.19) (PRK) [1,2] is one of the enzymes specific to the Calvin's reductive pentose phosphate cycle which is the major route by which carbon dioxide is assimilated and reduced by autotrophic organisms. PRK catalyzes the ATP-dependent phosphorylation of ribulose 5-phosphate into ribulose 1,5-bisphosphate which is the substrate for RubisCO. PRK's of diverse origins show different properties with respect to the size of the protein, the subunit structure, or the enzymatic regulation. However an alignment of the sequences of PRK from plants, algae, photosynthetic and chemoautotrophic bacteria shows that there are a few regions of sequence similarity. As a signature pattern we have selected one of these regions. -Consensus pattern: K-[LIVM]-x-R-D-x(3)-R-G-x-[ST]-x-E -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: December 1991 / First entry. [ 1] Kossmann J., Klintworth R., Bowien B. "Sequence analysis of the chromosomal and plasmid genes encoding phosphoribulokinase from Alcaligenes eutrophus." Gene 85:247-252(1989). PubMed=2559876 [ 2] Gibson J.L., Chen J.-H., Tower P.A., Tabita F.R. "The form II fructose 1,6-bisphosphatase and phosphoribulokinase genes form part of a large operon in Rhodobacter sphaeroides: primary structure and insertional mutagenesis analysis." Biochemistry 29:8085-8093(1990). PubMed=2175647 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}