Cyanobacteria sequences

Clusters Fa and Fb of photosystem I from cyanobacteria and chloro-plasts are distinguished by their EPR signatures (26, 27) and their reduction potentials (-520 mV for Fa and -580 mV for Fb Ref. (28). The assignment of cysteines in the primary sequence as ligands to individual clusters has been achieved by site-specific mutagenesis (29, Fig. 3), and structural information with regard to the environment of both clusters has been obtained by NMR (24). 

In general, the 10 different forms of adenylyl cyclase can be divided into three major and two minor groups based on their functional attributes as well as on their sequence homology. The three major families are (1) the Ca2+/calmodulin-stimulated isoforms, which include AC1, AC3, and AC8 certain of these enzymes are inhibited by GPt (2) the G[ -stimulated isoforms, which include AC2, AC4, and AC7 and (3) the Ca2+ and Gai inhibited isoforms, which are AC5 and AC6. The other two categories each have a single member (4) AC9, which is the most divergent of the membrane-bound isoforms, is stimulated by G(IS, inhibited by calcineurin (a protein phosphatase), and is insensitive to forskolin (5) sAC, the only soluble isoform, is the most divergent and is most similar to the adenylyl cyclase found in Cyanobacteria. 

Cyanobacteria also contain a reversible/bidirectional hydrogenase, which is soluble and has the capacity to both take up and produce H2 (Bothe et al. 1991 Flores and Herrero 1994 Appel and Schulz 1998 Hansel and Lindblad 1998). The latter enzyme was called bidirectional hydrogenase until the respective structural genes were sequenced and characterized by Schmitz et al. (1995). It has been the subject of some interest as another possible means to produce H2 photosynthetically. 

Phycobiliproteins are found also in cryptophytes but, differently from cyanobacteria and red algae, they are not organized into a phycobilisome, but instead they are located in the thylakoid lumen. Unique for cryptophytes, their phycobiliproteins do not exhibit a trimeric aggregation state characteristic for cyanobacteria, but instead they are present as ai(3a2(3 heterodimers, with each a subunit having a distinct amino acid sequence. [40]... 

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