v5.1.0.3
Cicer data from the Legume Information System
| Type | Family |
| Description | Escherichia coli NADPH-sulphite reductase (SiR) is a multimeric hemoflavoprotein composed of eight alpha-subunits (SiR-FP) and four beta-subunits (SiR-HP) that catalyses the six electron reduction of sulphite to sulphide. This is one of several activities required for the biosynthesis of L-cysteine from sulphate. The alpha component of NADPH-sulphite reductase is a flavoprotein, the beta component is a hemoprotein [ ]. The flavoprotein component catalyses the electron flow from NADPH to FAD to FMN to the hemoprotein component.This entry describes a clade of NADPH-dependent sulphite reductase flavoprotein subunit alpha from Proteobacteria. The proteins bind one FAD and one FMN as prosthetic groups and contains an NADPH-binding domain [ ]. |
| Short Name | CysJ_Proteobact |