Protein Domain : Nitrite/sulphite reductase 4Fe-4S domain IPR006067

Type  Domain
Description  Sulphite reductases (SiRs) and related nitrite reductases (NiRs) catalyse the six-electron reduction reactions of sulphite to sulphide, and nitrite to ammonia, respectively. The Escherichia coli SiR enzyme is a complex composed of two proteins, a flavoprotein alpha-component (SiR-FP) and a hemoprotein beta-component (SiR-HP) ( ), and has an alpha(8)beta(4) quaternary structure [ ]. SiR-FP contains both FAD and FMN, while SiR-HP contains a Fe(4)S(4) cluster coupled to a siroheme through a cysteine bridge. Electrons are transferred from NADPH to FAD, and on to FMN in SiR-FP, from which they are transferred to the metal centre of SiR-HP, where they reduce the siroheme-bound sulphite.SiR-HP has a two-fold symmetry, which generates a distinctive three-domain alpha/beta fold that controls assembly and reactivity [ ]. In the E. coli SiR-HP enzyme (), the iron is bound to cysteine residues at positions 433, 439, 478 and 482, the latter also forming the siroheme ligand.
Short Name  NO2/SO3_Rdtase_4Fe4S_dom

0 Child Features

1 Gene Families

235 Genes

3 Ontology Annotations

0 Parent Features

14 Publications

USDA
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