IPR013580
Light-independent protochlorophyllide reductase subunit B-like, C-terminal
InterPro entry
Short name | LI-POR_suB-like_C |
Overlapping homologous superfamilies |
Description
This domain is found in Light-independent protochlorophyllide reductase subunit B (LI-POR subunit B, also known as DPOR subunit B) and similar bacterial and plant chloroplast proteins. It often appears at the C-terminal of nitrogenase component 1 type oxidoreductases (
IPR000510) and sometimes independently in certain bacterial proteins such as the Protochlorophyllide reductase BchB subunit of the cyanobacterium Synechocystis.
LI-POR subunit B is a component of the dark-operative protochlorophyllide reductase (DPOR), a nitrogenase-like metalloenzyme that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide), leading to the specific architecture of chlorophylls. The X-ray crystallographic structure of this complex from the marine cyanobacterium Prochlorococcus marinus showed that the C-terminal domain of subunit B closes the substrate-binding cavity at the interface with the other component of the complex, possibly preventing the organism from Pchlide-induced photodynamic damage
[1].
This domain is also associated with chlorophyllide reductase subunit Z, which converts chlorophylls (Chl) into bacteriochlorophylls (BChl) by reducing ring B of the tetrapyrrole
[2].
References
GO terms
biological process
molecular function
cellular component
- None
Cross References
Contributing Member Database Entry
- Pfam:PF08369