1.8.7.1: assimilatory sulfite reductase (ferredoxin)
This is an abbreviated version!
For detailed information about assimilatory sulfite reductase (ferredoxin), go to the full flat file.
Word Map on EC 1.8.7.1
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1.8.7.1
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nitrite
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maize
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4.2.99.8
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o-acetyl-l-serine
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2.7.7.4
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sulfhydrylase
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cyanidioschyzon
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sulfurylase
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sulphite
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5'-phosphosulfate
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merolae
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viologen
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medicine
- 1.8.7.1
- nitrite
- maize
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4.2.99.8
- o-acetyl-l-serine
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2.7.7.4
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sulfhydrylase
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cyanidioschyzon
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sulfurylase
- sulphite
- 5'-phosphosulfate
- merolae
- viologen
- medicine
Reaction
+ 3 oxidized ferredoxin + 3 H2O = + 3 reduced ferredoxin + 6 H+
Synonyms
CMG021C, CmSiRB, coenzyme F420-dependent sulfite reductase, CYME_CMG021C, CYME_CMJ117C, DCP68, desulphoviridin, dissimilatory sulfite reductase, dSiR, EC 1.8.99.1, Fd-SiR, FdSiR, ferredoxin and sulfite reductase, ferredoxin sulfite reductase, ferredoxin-dependent sulfite reductase, ferredoxin-sulfite reductase, ferredoxin:sulfite oxidoreductase, ferredoxin:sulfite reductase, Fsr, NirA, PsSiR, SIR, SiRA, SirB, siroheme- and [Fe4-S4]-dependent NirA, sulfite reductase, sulfite reductase B, ZmSiR
ECTree
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General Information
General Information on EC 1.8.7.1 - assimilatory sulfite reductase (ferredoxin)
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evolution
malfunction
metabolism
physiological function
additional information
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
evolution
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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
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evolution
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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
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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
malfunction
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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
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malfunction
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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
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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
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
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the enzyme plays a role in chloroplast-nucleoid metabolism, plastid gene expression, and thylakoid membrane development
physiological function
ferredoxin sulfite reductase (FdSiR) catalyzes the six-electron reduction of sulfite to hydrogen sulfite and nitrite to ammonia
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
physiological function
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ferredoxin sulfite reductase (FdSiR) catalyzes the six-electron reduction of sulfite to hydrogen sulfite and nitrite to ammonia
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physiological function
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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
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physiological function
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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
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physiological function
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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
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physiological function
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ferredoxin sulfite reductase (FdSiR) catalyzes the six-electron reduction of sulfite to hydrogen sulfite and nitrite to ammonia
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the enzyme contains a [4Fe-4S]2+/1+ cluster and a siroheme active site
additional information
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the enzyme contains a [4Fe-4S]2+/1+ cluster and a siroheme active site
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additional information
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the enzyme contains a [4Fe-4S]2+/1+ cluster and a siroheme active site
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