assimilatory sulfite reductase (NADPH) hemoprotein subunit is a component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide
sulfite reductase (NADPH) hemoprotein, beta-component; Sulfite reductase (NADPH) catalyzes a six electron reduction of sulfite to sulfide in prokaryotic organisms. It is a complex oligomeric enzyme composed of two different peptides with a subunit composition of alpha(8)-beta(4). The alpha component, encoded by cysJ, is a flavoprotein containing both FMN and FAD, while the beta component, encoded by cysI, is a siroheme, iron-sulfur protein. In Salmonella typhimurium and Escherichia coli, both the alpha and beta subunits of sulfite reductase are located in a unidirectional gene cluster along with phosphoadenosine phosphosulfate reductase, which catalyzes a two step reduction of PAPS to give free sulfite. In cyanobacteria and plant species, sulfite reductase ferredoxin (EC 1.8.7.1) catalyzes the reduction of sulfite to sulfide. [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 273941 [Multi-domain] Cd Length: 541 Bit Score: 1069.36 E-value: 0e+00
Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; ...
15-566
0e+00
Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; Sulfite reductase, beta subunit (hemoprotein) is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 439925 [Multi-domain] Cd Length: 519 Bit Score: 582.08 E-value: 0e+00
Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the ...
173-326
9.47e-48
Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the biosynthetic assimilation of sulphur and nitrogen, respectfully. They are also both important for the dissimilation of oxidized anions for energy transduction.
Pssm-ID: 426031 [Multi-domain] Cd Length: 153 Bit Score: 163.60 E-value: 9.47e-48
sulfite reductase (NADPH) hemoprotein, beta-component; Sulfite reductase (NADPH) catalyzes a six electron reduction of sulfite to sulfide in prokaryotic organisms. It is a complex oligomeric enzyme composed of two different peptides with a subunit composition of alpha(8)-beta(4). The alpha component, encoded by cysJ, is a flavoprotein containing both FMN and FAD, while the beta component, encoded by cysI, is a siroheme, iron-sulfur protein. In Salmonella typhimurium and Escherichia coli, both the alpha and beta subunits of sulfite reductase are located in a unidirectional gene cluster along with phosphoadenosine phosphosulfate reductase, which catalyzes a two step reduction of PAPS to give free sulfite. In cyanobacteria and plant species, sulfite reductase ferredoxin (EC 1.8.7.1) catalyzes the reduction of sulfite to sulfide. [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 273941 [Multi-domain] Cd Length: 541 Bit Score: 1069.36 E-value: 0e+00
Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; ...
15-566
0e+00
Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; Sulfite reductase, beta subunit (hemoprotein) is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 439925 [Multi-domain] Cd Length: 519 Bit Score: 582.08 E-value: 0e+00
ferredoxin-sulfite reductase; Distantly related to the iron-sulfur hemoprotein of sulfite ...
14-556
4.66e-145
ferredoxin-sulfite reductase; Distantly related to the iron-sulfur hemoprotein of sulfite reductase (NADPH) found in Proteobacteria and Eubacteria, sulfite reductase (ferredoxin) is a cyanobacterial and plant monomeric enzyme that also catalyzes the reduction of sulfite to sulfide. [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 131097 [Multi-domain] Cd Length: 577 Bit Score: 430.81 E-value: 4.66e-145
Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the ...
173-326
9.47e-48
Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the biosynthetic assimilation of sulphur and nitrogen, respectfully. They are also both important for the dissimilation of oxidized anions for energy transduction.
Pssm-ID: 426031 [Multi-domain] Cd Length: 153 Bit Score: 163.60 E-value: 9.47e-48
precorrin-3B synthase; An iron-sulfur protein. An oxygen atom from dioxygen is incorporated ...
81-500
3.01e-19
precorrin-3B synthase; An iron-sulfur protein. An oxygen atom from dioxygen is incorporated into the macrocycle at C-20. In the aerobic cobalamin biosythesis pathway, four enzymes are involved in the conversion of precorrin-3A to precorrin-6A. The first of the four steps is carried out by EC 1.14.13.83, precorrin-3B synthase (CobG), yielding precorrin-3B as the product. This is followed by three methylation reactions, which introduce a methyl group at C-17 (CobJ; EC 2.1.1.131), C-11 (CobM; EC 2.1.1.133) and C-1 (CobF; EC 2.1.1.152) of the macrocycle, giving rise to precorrin-4, precorrin-5 and precorrin-6A, respectively. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 274131 [Multi-domain] Cd Length: 390 Bit Score: 89.85 E-value: 3.01e-19
Nitrite/Sulfite reductase ferredoxin-like half domain; Sulfite and Nitrite reductases are key ...
82-140
3.38e-11
Nitrite/Sulfite reductase ferredoxin-like half domain; Sulfite and Nitrite reductases are key to both biosynthetic assimilation of sulfur and nitrogen and dissimilation of oxidized anions for energy transduction. Two copies of this repeat are found in Nitrite and Sulfite reductases and form a single structural domain.
Pssm-ID: 377044 [Multi-domain] Cd Length: 67 Bit Score: 58.69 E-value: 3.38e-11
Nitrite/Sulfite reductase ferredoxin-like half domain; Sulfite and Nitrite reductases are key ...
353-417
5.02e-10
Nitrite/Sulfite reductase ferredoxin-like half domain; Sulfite and Nitrite reductases are key to both biosynthetic assimilation of sulfur and nitrogen and dissimilation of oxidized anions for energy transduction. Two copies of this repeat are found in Nitrite and Sulfite reductases and form a single structural domain.
Pssm-ID: 377044 [Multi-domain] Cd Length: 67 Bit Score: 55.61 E-value: 5.02e-10
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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