Light-independent protochlorophyllide reductase, iron-sulphur ATP-binding protein (IPR005971)

Short name: Protochlorophyllide_ATP-bd

Family relationships


Synonym: dark protochlorophyllide reductase

Protochlorophyllide reductase catalyzes the reductive formation of chlorophyllide from protochlorophyllide during biosynthesis of chlorophylls and bacteriochlorophylls. The light-independent (dark) form of protochlorophyllide reductase plays a key role in the ability of gymnosperms, algae, and photosynthetic bacteria to form chlorophyll in the dark. Genetic and sequence analyses have indicated that dark protochlorophyllide reductase consists of three protein subunits that exhibit significant sequence similarity to the three subunits of nitrogenase, which catalyzes the reductive formation of ammonia from dinitrogen. Dark protochlorophyllide reductase activity was shown to be dependent on the presence of all three subunits, ATP, and the reductant dithionite.

The BchL peptide (ChlL in chloroplast and cyanobacteria) is an ATP-binding iron-sulphur protein of the dark form protochlorophyllide reductase, an enzyme similar to nitrogenase [PMID: 10811655].

GO terms

Biological Process

GO:0015995 chlorophyll biosynthetic process
GO:0055114 oxidation-reduction process
GO:0019685 photosynthesis, dark reaction
GO:0046148 pigment biosynthetic process

Molecular Function

GO:0005524 ATP binding
GO:0016730 oxidoreductase activity, acting on iron-sulfur proteins as donors

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.