1.8.7.1	evolution	the common feature of both assimilatory and dissimilatory sulfite reductases is that they share a highly conserved domain C-X5-C-n-C-X3-C for binding the siroheme and the [4Fe-4S] cluster. In addition to these two class of sulfite reductases there exists a third class of assimilatory sulfite reductase found in a number of strictly anaerobic bacteria, cf. EC 1.8.1.2 and EC 1.8.99.5	-, 764195	
1.8.7.1	malfunction	depletion of the enzyme results in chloroplast ablation	726184	
1.8.7.1	malfunction	wild-type FdSiR and mutant FdSiRC491G in the presence of the artificial electron donor methyl viologen are both able to reduce sulfite to H2S, but the detected lower rate of H2S evolution for mutant FdSiRC491G is likely related to its lower cofactor content	-, 764195	
1.8.7.1	metabolism	in addition to participating in the sulfate assimilation reductive pathway, the enzyme also plays a role in protecting leaves against the toxicity of sulfite accumulation	726232	
1.8.7.1	additional information	the enzyme contains a [4Fe-4S]2+/1+ cluster and a siroheme active site	-, 764195	
1.8.7.1	physiological function	ferredoxin sulfite reductase (FdSiR) catalyzes the six-electron reduction of sulfite to hydrogen sulfite and nitrite to ammonia	-, 764195	
1.8.7.1	physiological function	the enzyme plays a role in chloroplast-nucleoid metabolism, plastid gene expression, and thylakoid membrane development	726184	
1.8.7.1	physiological function	the life cycle of Prochlorococcus marinus is influenced by viruses. Cyanophages that infect it have evolved genomes with as many as 327 open reading frames (ORFs). Viruses from three clades infect Prochlorococcus marinus, including T4-like myoviruses, T7-like podoviruses, and, less commonly, members of Siphoviridae. In some ecosystems, as many as 50% of cyanobacteria may be infected at any point in time. The sulfite reductase from Prochlorococcus marinus can utilize, besides its endogenous ferredoxin, also the phage ferredoxin, pssm2-Fd, from its parasite myovirus P-SSM2	-, 765063