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
-
4.2.99.8
- o-acetyl-l-serine
-
2.7.7.4
-
sulfhydrylase
-
cyanidioschyzon
-
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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Cofactor
Cofactor on EC 1.8.7.1 - assimilatory sulfite reductase (ferredoxin)
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[4Fe-4S]-center
in cocrystals, the [2Fe-2S] cluster of ferredoxin and the [4Fe-4S] cluster of SiR are in a close proximity
Fe-S center
the enzyme contains a [4Fe-4S]2+/1+ cluster and a siroheme active site
Ferredoxin
the enzyme can use its endogenous ferredoxin as well as the ferredoxin pssm2-Fd from its parasite myovirus P-SSM2. pssm2-Fd contains sequence features of host Fds, structure of the pssm2-Fd and structure comparisons, overview. Prochlorococcus marinus ferredoxin contains [4Fe-4S] centers, the myoviral ferredoxin contains [2Fe-2S] centers
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siroheme
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one per enzyme subunit, in the high-spin Fe3+ state in the reduced enzyme
siroheme
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1 mol per mol subunit, in the high-spin Fe3+ state in the reduced enzyme
when expressed in an Escherichia coli strain deficient in sulfite assimilation, pssm2-Fd complements bacterial growth when coexpressed with a Prochlorococcus marinus sulfite reductase, revealing that pssm2-Fd can transfer electrons to a host protein involved in nutrient assimilation. The high levels of structural similarity with cyanobacterial Fds and reactivity with a host sulfite reductase suggest that phage Fds evolved to transfer electrons to cyanobacterially encoded oxidoreductases. The phage Fds all localize to cluster VI, in close association with cyanobacterial Fds. Among the Fds in cluster VI, interactions with a range of oxidoreductases have been documented. Evaluation of the surface charge distribution of several different Fd and SIR structures
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additional information
when expressed in an Escherichia coli strain deficient in sulfite assimilation, pssm2-Fd complements bacterial growth when coexpressed with a Prochlorococcus marinus sulfite reductase, revealing that pssm2-Fd can transfer electrons to a host protein involved in nutrient assimilation. The high levels of structural similarity with cyanobacterial Fds and reactivity with a host sulfite reductase suggest that phage Fds evolved to transfer electrons to cyanobacterially encoded oxidoreductases. The phage Fds all localize to cluster VI, in close association with cyanobacterial Fds. Among the Fds in cluster VI, interactions with a range of oxidoreductases have been documented. Evaluation of the surface charge distribution of several different Fd and SIR structures
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additional information
when expressed in an Escherichia coli strain deficient in sulfite assimilation, pssm2-Fd complements bacterial growth when coexpressed with a Prochlorococcus marinus sulfite reductase, revealing that pssm2-Fd can transfer electrons to a host protein involved in nutrient assimilation. The high levels of structural similarity with cyanobacterial Fds and reactivity with a host sulfite reductase suggest that phage Fds evolved to transfer electrons to cyanobacterially encoded oxidoreductases. The phage Fds all localize to cluster VI, in close association with cyanobacterial Fds. Among the Fds in cluster VI, interactions with a range of oxidoreductases have been documented. Evaluation of the surface charge distribution of several different Fd and SIR structures
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